DB code: M00145
| CATH domain | 2.40.50.100 : OB fold (Dihydrolipoamide Acetyltransferase, E2P) | |
|---|---|---|
| 3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 | Catalytic domain | |
| 3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 | ||
| 3.20.20.- : TIM Barrel | ||
| E.C. | 2.1.3.1 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 2.40.50.100 : OB fold (Dihydrolipoamide Acetyltransferase, E2P) | M00163 M00222 M00188 M00189 T00223 M00190 M00191 M00208 |
| 3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 | M00122 S00849 D00254 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
|---|---|---|---|
| P02904 |
Methylmalonyl-CoA carboxyltransferase 1.3S subunit
|
EC
2.1.3.1
Biotin carboxyl carrier protein of transcarboxylase Transcarboxylase, 1.3S subunit |
PF00364
(Biotin_lipoyl)
[Graphical View] |
| Q8GBW6 |
Methylmalonyl-CoA carboxyltransferase 12S subunit
|
EC
2.1.3.1
Transcarboxylase 12S subunit |
PF01039
(Carboxyl_trans)
[Graphical View] |
| KEGG enzyme name |
|---|
|
methylmalonyl-CoA carboxytransferase
transcarboxylase methylmalonyl coenzyme A carboxyltransferase methylmalonyl-CoA transcarboxylase oxalacetic transcarboxylase methylmalonyl-CoA carboxyltransferase methylmalonyl-CoA carboxyltransferase (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxytransferasecarboxytransferase [incorrect] |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P02904 | BCCP_PROFR | (S)-methylmalonyl-CoA + pyruvate = propanoyl- CoA + oxaloacetate. | Transcarboxylase is composed of three subunits: 1.3S, 5S, and 12S. The core of the enzyme is composed of six 12S subunits. On each side of the core there are three pairs of 5S subunits. Each 5S dimer is attached to the core by two 1.3S subunits. Thus the total number of chains is 30 (6 + 12 + 12). | ||
| Q8GBW6 | 12S_PROFR | (S)-methylmalonyl-CoA + pyruvate = propanoyl- CoA + oxaloacetate. | Homohexamer. Transcarboxylase is composed of three subunits: 1.3S, 5S, and 12S. The core of the enzyme is composed of six 12S subunits. On each side of the core there are three pairs of 5S subunits. Each 5S dimer is attached to the core by two 1.3S subunits. Thus the total number of chains is 30 (6 + 12 + 12). |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00640 | Propanoate metabolism |
| Compound table | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | ||||||||||
| KEGG-id | C00120 | C00175 | C00038 | C00683 | C00022 | C00100 | C00036 | ||||||
| E.C. | |||||||||||||
| Compound | Biotin | Cobalt | Zinc | (S)-2-Methyl-3-oxopropanoyl-CoA | Pyruvate | Propanoyl-CoA | Oxaloacetate | ||||||
| Type | amide group,amine group,fatty acid,sulfide group | heavy metal | heavy metal | amine group,carbohydrate,carboxyl group,nucleotide ,peptide/protein,sulfide group | carbohydrate,carboxyl group | amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group | carbohydrate,carboxyl group | ||||||
| ChEBI |
15956 15956 |
48828 48828 |
29105 29105 |
15466 15466 |
32816 32816 |
15539 15539 |
30744 30744 |
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| PubChem |
171548 171548 |
104729 104729 |
32051 32051 |
11966111 439291 11966111 439291 |
1060 1060 |
439164 92753 439164 92753 |
970 970 |
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| 1dczA |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1dd2A |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on3A01 |
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Unbound | Unbound | Unbound | Bound:MCA | Analogue:DXX | Unbound | Unbound | |
| 1on3B01 |
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Unbound | Unbound | Unbound | Bound:MCA | Analogue:DXX | Unbound | Unbound | |
| 1on3C01 |
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Unbound | Unbound | Unbound | Bound:MCA | Analogue:DXX | Unbound | Unbound | |
| 1on3D01 |
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Unbound | Unbound | Unbound | Bound:MCA | Analogue:DXX | Unbound | Unbound | |
| 1on3E01 |
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Unbound | Unbound | Unbound | Bound:MCA | Analogue:DXX | Unbound | Unbound | |
| 1on3F01 |
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Unbound | Unbound | Unbound | Bound:MCA | Analogue:DXX | Unbound | Unbound | |
| 1on9A01 |
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Unbound | Unbound | Unbound | Analogue:MCA | Unbound | Unbound | Unbound | |
| 1on9B01 |
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Unbound | Unbound | Unbound | Analogue:MCA | Unbound | Unbound | Unbound | |
| 1on9C01 |
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Unbound | Unbound | Unbound | Analogue:MCA | Unbound | Unbound | Unbound | |
| 1on9D01 |
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Unbound | Unbound | Unbound | Analogue:MCA | Unbound | Unbound | Unbound | |
| 1on9E01 |
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Unbound | Unbound | Unbound | Analogue:MCA | Unbound | Unbound | Unbound | |
| 1on9F01 |
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Unbound | Unbound | Unbound | Analogue:MCA | Unbound | Unbound | Unbound | |
| 1on3A02 |
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Unbound | Analogue:_CD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on3B02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on3C02 |
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Unbound | Analogue:_CD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on3D02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on3E02 |
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Unbound | Analogue:_CD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on3F02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on9A02 |
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Unbound | Analogue:_CD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on9B02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on9C02 |
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Unbound | Analogue:_CD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on9D02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on9E02 |
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Unbound | Analogue:_CD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1on9F02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
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| resource | references | E.C. |
| Active-site residues | ||||||||||
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| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1dczA |
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| 1dd2A |
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| 1on3A01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on3B01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on3C01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on3D01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on3E01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on3F01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on9A01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on9B01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on9C01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on9D01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on9E01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on9F01 |
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TYR 185 | ALA 143;ALA 180;GLY 182;ALA 183 | |||
| 1on3A02 |
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HIS 388(metal binding) | GLY 414 | |||
| 1on3B02 |
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HIS 388(metal binding) | GLY 414 | |||
| 1on3C02 |
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HIS 388(metal binding) | GLY 414 | |||
| 1on3D02 |
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HIS 388(metal binding) | GLY 414 | |||
| 1on3E02 |
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HIS 388(metal binding) | GLY 414 | |||
| 1on3F02 |
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HIS 388(metal binding) | GLY 414 | |||
| 1on9A02 |
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HIS 388(metal binding) | GLY 414 | |||
| 1on9B02 |
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HIS 388(metal binding) | GLY 414 | |||
| 1on9C02 |
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HIS 388(metal binding) | GLY 414 | |||
| 1on9D02 |
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HIS 388(metal binding) | GLY 414 | |||
| 1on9E02 |
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HIS 388(metal binding) | GLY 414 | |||
| 1on9F02 |
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HIS 388(metal binding) | GLY 414 | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
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[12]
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Fig.7, p.4638-4639 | 2 |
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[16]
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Fig.6, p.2340-2341 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3910092 |
| Journal | Biochemistry |
| Year | 1985 |
| Volume | 24 |
| Pages | 6163-9 |
| Authors | Hoving H, Crysell B, Leadlay PF |
| Title |
Fluorine NMR studies on stereochemical aspects of reactions catalyzed by transcarboxylase, |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3735431 |
| Journal | J Mol Biol |
| Year | 1986 |
| Volume | 188 |
| Pages | 495-8 |
| Authors | Skrzypczak-Jankun E, Tulinsky A, Fillers JP, Kumar KG, Wood HG |
| Title | Preliminary crystallographic data and quaternary structural implications of the central subunit of the multi-subunit complex transcarboxylase |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2269346 |
| Journal | FEBS Lett |
| Year | 1990 |
| Volume | 277 |
| Pages | 156-8 |
| Authors | Bendrat K, Berger S, Buckel W, Etzel WA, Rohm KH |
| Title | Carbon-13 labelled biotin--a new probe for the study of enzyme catalyzed carboxylation and decarboxylation reactions |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1526981 |
| Journal | J Biol Chem |
| Year | 1992 |
| Volume | 267 |
| Pages | 18407-12 |
| Authors | Shenoy BC, Xie Y, Park VL, Kumar GK, Beegen H, Wood HG, Samols D |
| Title |
The importance of methionine residues for the catalysis of the biotin enzyme, |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8346913 |
| Journal | Arch Biochem Biophys |
| Year | 1993 |
| Volume | 304 |
| Pages | 359-66 |
| Authors | Shenoy BC, Samols D, Kumar GK |
| Title | The conserved methionines of the 1.3 S biotinyl subunit of transcarboxylase: effect of mutations on conformation and activity |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8420991 |
| Journal | J Biol Chem |
| Year | 1993 |
| Volume | 268 |
| Pages | 2232-8 |
| Authors | Shenoy BC, Kumar GK, Samols D |
| Title | Dissection of the biotinyl subunit of transcarboxylase into regions essential for activity and assembly |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9398186 |
| Journal | Biochemistry |
| Year | 1997 |
| Volume | 36 |
| Pages | 14676-82 |
| Authors | Reddy DV, Shenoy BC, Carey PR, Sonnichsen FD |
| Title | Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxylase: an NMR study |
| Related PDB | 1dcz 1dd2 |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9720239 |
| Journal | Carbohydr Res |
| Year | 1998 |
| Volume | 309 |
| Pages | 89-94 |
| Authors | Paramonov NA, Parolis LA, Parolis H, Boan IF, Anton J, Rodriguez-Valera F |
| Title | The structure of the exocellular polysaccharide produced by the Archaeon Haloferax gibbonsii (ATCC 33959) |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9792103 |
| Journal | Protein Sci |
| Year | 1998 |
| Volume | 7 |
| Pages | 2156-63 |
| Authors | Reddy DV, Rothemund S, Shenoy BC, Carey PR, Sonnichsen FD |
| Title | Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermanii |
| Related PDB | 1dcz 1dd2 |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10542197 |
| Journal | J Biol Chem |
| Year | 1999 |
| Volume | 274 |
| Pages | 31767-9 |
| Authors | Blanchard CZ, Chapman-Smith A, Wallace JC, Waldrop GL |
| Title | The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10704200 |
| Journal | Biochemistry |
| Year | 2000 |
| Volume | 39 |
| Pages | 2509-16 |
| Authors | Reddy DV, Shenoy BC, Carey PR, Sonnichsen FD |
| Title | High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii |
| Related PDB | 1dcz 1dd2 |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | Homologous enzyme |
| Medline ID | |
| PubMed ID | 10769118 |
| Journal | Biochemistry |
| Year | 2000 |
| Volume | 39 |
| Pages | 4630-9 |
| Authors | Benning MM, Haller T, Gerlt JA, Holden HM |
| Title | New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11173475 |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 2001 |
| Volume | 57 |
| Pages | 266-8 |
| Authors | Wang YF, Hyatt DC, Rivera RE, Carey PR, Yee VC |
| Title | Crystallization and preliminary X-ray analysis of the 12S central subunit of transcarboxylase from Propionibacterium shermanii |
| Related PDB | |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11841210 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 2191-7 |
| Authors | Rivera-Hainaj RE, Pusztai-Carey M, Venkat Reddy D, Choowongkomon K, Sonnichsen FD, Carey PR |
| Title | Characterization of the carboxylate delivery module of transcarboxylase: following spontaneous decarboxylation of the 1.3S-CO2- subunit by NMR and FTIR spectroscopies |
| Related PDB | |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12196011 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 10741-6 |
| Authors | Zheng X, Rivera-Hainaj RE, Zheng Y, Pusztai-Carey M, Hall PR, Yee VC, Carey PR |
| Title | Substrate binding induces a cooperative conformational change in the 12S subunit of transcarboxylase: Raman crystallographic evidence |
| Related PDB | |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12743028 |
| Journal | EMBO J |
| Year | 2003 |
| Volume | 22 |
| Pages | 2334-47 |
| Authors | Hall PR, Wang YF, Rivera-Hainaj RE, Zheng X, Pustai-Carey M, Carey PR, Yee VC |
| Title | Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
As annotated in Swiss-prot (P02904), The 12 subunit transfers a carboxyl group from the terminal of methyl-malonyl-CoA to the 1.3S subunit, |
| Created | Updated |
|---|---|
| 2004-03-19 | 2009-02-26 |