3NZP

Crystal Structure of the Biosynthetic Arginine decarboxylase SpeA from Campylobacter jejuni, Northeast Structural Genomics Consortium Target BR53

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	F_UNCLASSIFIED	e3nzpA2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF17810	e3nzpA3	A: alpha bundles	X: Spectrin repeat-like	H: Helical bundle domain in arginine decarboxylase (From Topology)	T: Helical bundle domain in arginine decarboxylase	F: PF17810	ECOD (1.6)
A	F_UNCLASSIFIED	e3nzpA1	A: alpha bundles	X: Arginine decarboxylase C-terminal helical extension (From Topology)	H: Arginine decarboxylase C-terminal helical extension (From Topology)	T: Arginine decarboxylase C-terminal helical extension	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF02784	e3nzpA4	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF02784	ECOD (1.6)
B	F_UNCLASSIFIED	e3nzpB1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF17810	e3nzpB3	A: alpha bundles	X: Spectrin repeat-like	H: Helical bundle domain in arginine decarboxylase (From Topology)	T: Helical bundle domain in arginine decarboxylase	F: PF17810	ECOD (1.6)
B	F_UNCLASSIFIED	e3nzpB4	A: alpha bundles	X: Arginine decarboxylase C-terminal helical extension (From Topology)	H: Arginine decarboxylase C-terminal helical extension (From Topology)	T: Arginine decarboxylase C-terminal helical extension	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF02784	e3nzpB2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF02784	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.37.10	Mainly Beta	Beta Barrel	Lyase, Ornithine Decarboxylase	Chain A, domain 1	CATH (4.3.0)
A	3.20.20.10	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Alanine racemase	CATH (4.3.0)
A	1.20.58.930	Mainly Alpha	Up-down Bundle	Methane Monooxygenase Hydroxylase	Chain G, domain 1	CATH (4.3.0)
A	1.10.287.3440	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
B	2.40.37.10	Mainly Beta	Beta Barrel	Lyase, Ornithine Decarboxylase	Chain A, domain 1	CATH (4.3.0)
B	3.20.20.10	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Alanine racemase	CATH (4.3.0)
B	1.20.58.930	Mainly Alpha	Up-down Bundle	Methane Monooxygenase Hydroxylase	Chain G, domain 1	CATH (4.3.0)
B	1.10.287.3440	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02784	Pyridoxal-dependent decarboxylase, pyridoxal binding domain (Orn_Arg_deC_N)	Pyridoxal-dependent decarboxylase, pyridoxal binding domain	These pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates This domain has a TIM barrel fold.	Domain
A, B	PF17944	Arginine decarboxylase C-terminal helical extension (Arg_decarbox_C)	Arginine decarboxylase C-terminal helical extension	This small three helical domain is found at the C-terminus of the arginine decarboxylase enzyme.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Arginine decarboxylase	arginine decarboxylase activity carboxy-lyase activity lyase activity catalytic activity carbon-carbon lyase activity cation binding ion binding binding metal ion binding small molecule binding	organonitrogen compound metabolic process organonitrogen compound biosynthetic process polyamine metabolic process amine metabolic process biogenic amine biosynthetic process spermidine metabolic process organic substance metabolic process biosynthetic process amine biosynthetic process polyamine biosynthetic process organic substance biosynthetic process metabolic process spermidine biosynthetic process biogenic amine metabolic process organonitrogen compound metabolic process organonitrogen compound biosynthetic process polyamine metabolic process amine metabolic process biogenic amine biosynthetic process spermidine metabolic process organic substance metabolic process biosynthetic process amine biosynthetic process polyamine biosynthetic process organic substance biosynthetic process metabolic process spermidine biosynthetic process biogenic amine metabolic process catabolic process oxoacid metabolic process glutamine family amino acid catabolic process amino acid metabolic process arginine catabolic process organic acid metabolic process organic acid catabolic process alpha-amino acid metabolic process glutamine family amino acid metabolic process cellular catabolic process arginine metabolic process carboxylic acid catabolic process small molecule metabolic process amino acid catabolic process organonitrogen compound catabolic process cellular metabolic process carboxylic acid metabolic process L-amino acid catabolic process primary metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process cellular process small molecule catabolic process organic substance catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR029066	PLP-binding barrel	Homologous Superfamily
A, B	IPR040634	Arginine decarboxylase, helical bundle domain	Domain
A, B	IPR002985	Arginine decarboxylase	Family
A, B	IPR009006	Alanine racemase/group IV decarboxylase, C-terminal	Homologous Superfamily
A, B	IPR041128	Arginine decarboxylase, C-terminal helical	Domain
A, B	IPR000183	Ornithine/DAP/Arg decarboxylase	Family
A, B	IPR022644	Orn/DAP/Arg decarboxylase 2, N-terminal	Domain
A, B	IPR022653	Orn/DAP/Arg decarboxylase 2, pyridoxal-phosphate binding site	Binding Site

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.