DB code: M00133

RLCP classification 1.13.30000.10 : Hydrolysis
CATH domain 4.10.740.10 : Coagulation Factor IX
2.10.25.10 : Laminin
2.10.25.10 : Laminin
2.40.10.10 : Thrombin, subunit H Catalytic domain
2.40.10.10 : Thrombin, subunit H Catalytic domain
E.C. 3.4.21.22
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.10.25.10 : Laminin M00139 M00212 M00152 M00155 M00315 M00316
2.40.10.10 : Thrombin, subunit H M00139 D00214 M00167 D00426 D00428 D00429 D00430 D00431 D00432 D00433 D00434 D00435 M00227 M00209 D00194 D00197 D00211 D00212 D00216 M00212 D00224 D00497 M00217 M00216 D00528 D00848 D00850 D00851 D00852 D00855 M00152 M00155 M00157 M00181 M00315 M00316 M00317 M00348 M00349 T00074 T00410 T00411

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains MEROPS Pfam RefSeq
P16293 Coagulation factor IX
EC 3.4.21.22
Christmas factor
Coagulation factor IXa light chain
Coagulation factor IXa heavy chain
S01.214 (Serine)
PF00008 (EGF)
PF00594 (Gla)
PF00089 (Trypsin)
[Graphical View]
P00741 Coagulation factor IX
EC 3.4.21.22
Christmas factor
Coagulation factor IXa light chain
Coagulation factor IXa heavy chain
S01.214 (Serine)
PF00008 (EGF)
PF00594 (Gla)
PF00089 (Trypsin)
[Graphical View]
P00740 Coagulation factor IX
EC 3.4.21.22
Christmas factor
Plasma thromboplastin component
PTC
Coagulation factor IXa light chain
Coagulation factor IXa heavy chain
S01.214 (Serine)
PF00008 (EGF)
PF00594 (Gla)
PF00089 (Trypsin)
[Graphical View] 		NP_000124.1 (Protein)
NM_000133.3 (DNA/RNA sequence)

KEGG enzyme name
coagulation factor IXa
activated Christmas factor
blood-coagulation factor IXa
activated blood-coagulation factor IX
autoprothrombin II
blood platelet cofactor II
activated blood coagulation factor XI

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P16293 FA9_PIG Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa. Heterodimer of a light chain and a heavy chain, disulfide-linked. Secreted.
P00741 FA9_BOVIN Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa. Heterodimer of a light chain and a heavy chain, disulfide-linked. Secreted.
P00740 FA9_HUMAN Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa. Heterodimer of a light chain and a heavy chain, disulfide-linked. Secreted.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C01038 C00001 C01065 I00087 I00085 I00086
E.C.
Compound Coagulation Factor X H2O Coagulation Factor Xa Peptidyl-tetrahedral intermediate Acyl-enzyme Tetrahedral intermediate
Type peptide/protein H2O peptide/protein
ChEBI 15377
 15377
PubChem 22247451
 962
 22247451
 962
1pfxC01 Unbound Unbound Unbound Intermediate-analogue:PHE-PRO-ARG (chain I) Unbound
1rfnA01 Unbound Unbound Unbound Unbound Unbound
1pfxC02 Unbound Unbound Unbound Unbound Unbound
1rfnA02 Unbound Unbound Unbound Unbound Unbound
1pfxL01 Unbound Unbound Unbound Unbound Unbound
1pfxL02 Unbound Unbound Unbound Unbound Unbound
1rfnB Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P00741,P16293

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1pfxC01 SER 195 GLY 193;SER 195
1rfnA01 SER 195 GLY 193;SER 195
1pfxC02 HIS 57;ASP 102
1rfnA02 HIS 57;ASP 102
1pfxL01
1pfxL02
1rfnB

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.9797

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID 96003866
PubMed ID 7568220
Journal Proc Natl Acad Sci U S A
Year 1995
Volume 92
Pages 9796-800
Authors Brandstetter H, Bauer M, Huber R, Lollar P, Bode W
Title X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B.
Related PDB 1pfx
Related UniProtKB P16293
[2]
Resource
Comments
Medline ID
PubMed ID 9235979
Journal Biochemistry
Year 1997
Volume 36
Pages 9365-73
Authors Parker ET, Pohl J, Blackburn MN, Lollar P
Title Subunit structure and function of porcine factor Xa-activated factor VIII.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 9668086
Journal J Biol Chem
Year 1998
Volume 273
Pages 19049-54
Authors Fay PJ, Koshibu K
Title The A2 subunit of factor VIIIa modulates the active site of factor IXa.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 9925787
Journal J Mol Biol
Year 1999
Volume 285
Pages 2089-104
Authors Zhang E, St Charles R, Tulinsky A
Title Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 10605707
Journal Thromb Haemost
Year 1999
Volume 82
Pages 218-25
Authors Bajaj SP
Title Region of factor IXa protease domain that interacts with factor VIIIa: analysis of select hemophilia B mutants.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10595635
Journal Thromb Haemost
Year 1999
Volume 82
Pages 1443-5
Authors Feuerstein GZ, Toomey JR, Valocik R, Koster P, Patel A, Blackburn MN
Title An inhibitory anti-factor IX antibody effectively reduces thrombus formation in a rat model of venous thrombosis.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10467148
Journal Structure Fold Des
Year 1999
Volume 7
Pages 989-96
Authors Hopfner KP, Lang A, Karcher A, Sichler K, Kopetzki E, Brandstetter H, Huber R, Bode W, Engh RA
Title Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding.
Related PDB P00740 1rfn
Related UniProtKB

Comments
This protein is composed of a heavy chain, with a trypsin-like serine protease domain (peptidase family-S1), and a light chain with two EGF-like domains. According to the literature [1], the catalytic heavy chain has a catalytic triad, composed of Ser/His/Asp, which is characteristic for trypsin-like serine proteases.

Created Updated
2004-03-17 2011-02-17