1XGM

METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1xgma1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	Methionine aminopeptidase, insert domain	Methionine aminopeptidase, insert domain	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
A	d1xgma2	Alpha and beta proteins (a+b)	Creatinase/aminopeptidase	Creatinase/aminopeptidase	Creatinase/aminopeptidase	Methionine aminopeptidase	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
B	d1xgmb1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	Methionine aminopeptidase, insert domain	Methionine aminopeptidase, insert domain	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)
B	d1xgmb2	Alpha and beta proteins (a+b)	Creatinase/aminopeptidase	Creatinase/aminopeptidase	Creatinase/aminopeptidase	Methionine aminopeptidase	(Pyrococcus furiosus ) [TaxId: 2261 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Creatinase/aminopeptidase catalytic domain-like	8003202	3000126	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Creatinase/aminopeptidase catalytic domain-like	8003202	3000126	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Winged helix DNA-binding domain	8003204	3000034	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Winged helix DNA-binding domain	8003204	3000034	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Creatinase/aminopeptidase catalytic domain-like	8003202	3000126	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Creatinase/aminopeptidase catalytic domain-like	8003202	3000126	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	F_UNCLASSIFIED	e1xgmA1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF00557	e1xgmA2	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: PF00557	ECOD (1.6)
B	F_UNCLASSIFIED	e1xgmB1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF00557	e1xgmB2	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: PF00557	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.230.10	Alpha Beta	Alpha-Beta Complex	Creatine Amidinohydrolase	Creatinase/methionine aminopeptidase superfamily	CATH (4.3.0)
A	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
B	3.90.230.10	Alpha Beta	Alpha-Beta Complex	Creatine Amidinohydrolase	Creatinase/methionine aminopeptidase superfamily	CATH (4.3.0)
B	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00557	Metallopeptidase family M24 (Peptidase_M24)	Metallopeptidase family M24	This family contains metallopeptidases. It also contains non-peptidase homologues such as the N terminal domain of Spt16 which is a histone H3-H4 binding module [3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	METHIONINE AMINOPEPTIDASE	peptidase activity catalytic activity, acting on a protein initiator methionyl aminopeptidase activity aminopeptidase activity hydrolase activity exopeptidase activity catalytic activity metallopeptidase activity metalloaminopeptidase activity metalloexopeptidase activity cation binding ion binding binding metal ion binding peptidase activity catalytic activity, acting on a protein initiator methionyl aminopeptidase activity aminopeptidase activity hydrolase activity exopeptidase activity catalytic activity metallopeptidase activity metalloaminopeptidase activity metalloexopeptidase activity cation binding ion binding binding metal ion binding small molecule binding	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR002468	Peptidase M24A, methionine aminopeptidase, subfamily 2	Family
A, B	IPR001714	Peptidase M24, methionine aminopeptidase	Family
A, B	IPR018349	Peptidase M24A, methionine aminopeptidase, subfamily 2, binding site	Binding Site
A, B	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily
A, B	IPR036390	Winged helix DNA-binding domain superfamily	Homologous Superfamily
A, B	IPR036005	Creatinase/aminopeptidase-like	Homologous Superfamily
A, B	IPR028595	Methionine aminopeptidase, archaeal	Family
A, B	IPR000994	Peptidase M24	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	methionyl aminopeptidase M-CSA #917	Methionine aminopeptidase (MAP) catalyses the hydrolytic cleavage of the N-terminal methionine from newly synthesised polypeptides. These enzymes have a requirement for a divalent metal which has been shown to be feasible with multiple different metal ions including Co(II), Mn(II), Fe(II) and Zn(II) with Zinc showing to be the lowest activation energy .	Defined by 6 residues: ASP:A-82ASP:A-93HIS:A-153HIS:A-161GLU:A-187GLU:A-280 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.4.11.18 (PDB Primary Data) Search M-CSA Motif + EC 3.4.11.18

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.