DB code: S00845

CATH domain	1.50.10.10 : Glycosyltransferase	Catalytic domain
E.C.	5.1.3.8
CSA
M-CSA
MACiE

CATH domain	Related DB codes (homologues)
1.50.10.10 : Glycosyltransferase	S00531 S00048 D00167 D00500 M00192 T00245 T00246

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	Pfam	RefSeq
A4UA16		N-acetyl-D-glucosamine 2-epimerase	PF07221 (GlcNAc_2-epim) [Graphical View]
P17560	N-acylglucosamine 2-epimerase	EC 5.1.3.8 N-acetyl-D-glucosamine 2-epimerase GlcNAc 2-epimerase AGE Renin-binding protein RnBP	PF07221 (GlcNAc_2-epim) [Graphical View]	NP_999065.1 (Protein) NM_213900.1 (DNA/RNA sequence)

KEGG enzyme name
N-Acylglucosamine 2-epimerase Acylglucosamine 2-epimerase N-Acetylglucosamine 2-epimerase

UniprotKB: Accession Number	Entry name	Activity	Subunit	Subcellular location	Cofactor
A4UA16	A4UA16_9NOST
P17560	RENBP_PIG	N-acyl-D-glucosamine = N-acyl-D-mannosamine.	Homodimer.

KEGG Pathways
Map code	Pathways	E.C.
MAP00530	Aminosugars metabolism

Compound table
	Cofactors	Substrates	Products	Intermediates
KEGG-id	C00002	C03000	C00625
E.C.
Compound	ATP	N-acyl-D-glucosamine	N-acyl-D-mannosamine
Type	amine group,nucleotide	amide group,carbohydrate	amide group,carbohydrate
ChEBI	15422 15422
PubChem	5957 5957

2gz6A00	Unbound	Unbound	Unbound
2gz6B00	Unbound	Unbound	Unbound
1fp3A00	Unbound	Unbound	Unbound
1fp3B00	Unbound	Unbound	Unbound

Reference for Active-site residues
resource	references	E.C.
literature [6]&[7]

Active-site residues
PDB	Catalytic residues	Cofactor-binding residues	Modified residues	Main-chain involved in catalysis	Comment

2gz6A00	ARG 57;HIS 239;GLU 242;GLU 308;HIS 372
2gz6B00	ARG 57;HIS 239;GLU 242;GLU 308;HIS 372
1fp3A00	ARG 60;HIS 248;GLU 251;GLU 318;HIS 382
1fp3B00	ARG 60;HIS 248;GLU 251;GLU 318;HIS 382

References for Catalytic Mechanism
References	Sections	No. of steps in catalysis
[6]	Figure 5, p.904-905
[7]	Figure 6, p.1453-1455

References
[1]
Resource
Comments	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID
PubMed ID	11061972
Journal	J Mol Biol
Year	2000
Volume	303
Pages	733-44
Authors	Itoh T, Mikami B, Maru I, Ohta Y, Hashimoto W, Murata K
Title	Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 A resolution.
Related PDB	1fp3
Related UniProtKB	P17560
[2]
Resource
Comments
Medline ID
PubMed ID	11706991
Journal	Cell Mol Life Sci
Year	2001
Volume	58
Pages	1650-65
Authors	Allard ST, Giraud MF, Naismith JH
Title	Epimerases: structure, function and mechanism.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID	11726282
Journal	J Biochem
Year	2001
Volume	130
Pages	815-21
Authors	Takahashi S, Hori K, Takahashi K, Ogasawara H, Tomatsu M, Saito K
Title	Effects of nucleotides on N-acetyl-d-glucosamine 2-epimerases (renin-binding proteins): comparative biochemical studies.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID	12137277
Journal	Nat Prod Rep
Year	2002
Volume	19
Pages	261-77
Authors	Samuel J, Tanner ME
Title	Mechanistic aspects of enzymatic carbohydrate epimerization.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID	16011304
Journal	Biomed Res
Year	2005
Volume	26
Pages	117-21
Authors	Takahashi S, Ogasawara H, Hiwatashi K, Hata K, Hori K, Koizumi Y, Sugiyama T
Title	Amino acid residues conferring the nucleotide binding properties of N-acetyl-D-glucosamine 2-epimerase (renin binding protein).
Related PDB
Related UniProtKB
[6]
Resource
Comments	NUCLEOTIDE SEQUENCE.
Medline ID
PubMed ID	17292397
Journal	J Mol Biol
Year	2007
Volume	367
Pages	895-908
Authors	Lee YC, Wu HM, Chang YN, Wang WC, Hsu WH
Title	The central cavity from the (alpha/alpha)6 barrel structure of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase contains two key histidine residues for reversible conversion.
Related PDB	2gz6
Related UniProtKB	A4UA16
[7]
Resource
Comments
Medline ID
PubMed ID	18328504
Journal	J Mol Biol
Year	2008
Volume	377
Pages	1443-59
Authors	Itoh T, Mikami B, Hashimoto W, Murata K
Title	Crystal structure of YihS in complex with D-mannose: structural annotation of Escherichia coli and Salmonella enterica yihS-encoded proteins to an aldose-ketose isomerase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID	19330485
Journal	Biotechnol Lett
Year	2009
Volume
Pages
Authors	Ito S, Hamada S, Ito H, Matsui H, Ozawa T, Taguchi H, Ito S
Title	Site-directed mutagenesis of possible catalytic residues of cellobiose 2-epimerase from Ruminococcus albus.
Related PDB
Related UniProtKB

Comments
Although this enzyme binds ATP at the site, which is composed of Trp56, Arg60 and Phe122 (of PDB;1fp3), its role in catalysis has not been elucidated yet (see [7]). This enzyme catalyzes the following reactions (see [6] & [7]): (A) Ring opening; intramolecular elimination: (B) Isomerization; Shift of double-bond from O=C-C to O-C=C, forming an enediol intermediate: (C) Isomerization; Shift of double-bond from C=C-O to C-C=O: (D) Ring closure; intramolecular addition:

Comments

Although this enzyme binds ATP at the site, which is composed of Trp56, Arg60 and Phe122 (of PDB;1fp3), its role in catalysis has not been elucidated yet (see [7]).
This enzyme catalyzes the following reactions (see [6] & [7]):
(A) Ring opening; intramolecular elimination:
(B) Isomerization; Shift of double-bond from O=C-C to O-C=C, forming an enediol intermediate:
(C) Isomerization; Shift of double-bond from C=C-O to C-C=O:
(D) Ring closure; intramolecular addition:

Created	Updated
2009-06-15	2010-03-29