Q4L574 (PURK_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N5-carboxyaminoimidazole ribonucleotide synthase
Short name=N5-CAIR synthase
EC=6.3.4.18

Alternative name(s):
5-(carboxyamino)imidazole ribonucleotide synthetase

Gene names

Name:	purK
Ordered Locus Names:	SH1892

Organism

Staphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]

Taxonomic identifier

279808 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO3- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) By similarity.
Catalytic activity	ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO3- = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the purK/purT family. Contains 1 ATP-grasp domain.
Sequence caution	The sequence BAE05201.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Purine biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	5-(carboxyamino)imidazole ribonucleotide synthase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cofactor binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro phosphoribosylaminoimidazole carboxylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 374	374	N5-carboxyaminoimidazole ribonucleotide synthase		PRO_0000075011
Regions
	Domain	112 – 296	185	ATP-grasp
	Nucleotide binding	183 – 186	4	ATP By similarity
	Nucleotide binding	266 – 267	2	ATP By similarity
Sites
	Binding site	108	1	ATP By similarity
	Binding site	148	1	ATP By similarity
	Binding site	159	1	ATP By similarity
	Binding site	191	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4L574 [UniParc]. Last modified February 7, 2006. Version 2. Checksum: 1E36AEF46296E436	FASTA	374	42,583
	10 20 30 40 50 60 MNFNKLKFGD TIGIIGGGQL GKMMAQSAQK MGFKVICLDP NPDSPCKSVA HEFITAAYDD 70 80 90 100 110 120 EEALHELGEK SDVITYEFEN ISAEQLIRLT QKFNIPQGYQ AIQLLQDRLT EKQTLQKAGS 130 140 150 160 170 180 KIVPFLPIKE EKDLNVVINQ LGYPFIVKTR FGGYDGKGQV LVKNEESIQE AKDLISQQEC 190 200 210 220 230 240 VAEQFLDIAL EVSLTVTIGN QKQITYFPLQ ENEHRNQILF KTIVPARSDK EQEARDEVNK 250 260 270 280 290 300 IINEVHFVGT FTVEFFIDKS NNLYVNEIAP RPHNSGHYSI EACDYSQFDT HILAVTGQNL 310 320 330 340 350 360 PKEIEILKPA VMMNLLGRDL DLLEDKFANH PEWHVHIYGK PERKPNRKMG HMTILTNNVD 370 ETEKAMLKQF EGRE

References

[1]

"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species." Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K. J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCSC1435.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006716 Genomic DNA. Translation: BAE05201.1. Different initiation.
RefSeq	YP_253807.1. NC_007168.1.
3D structure databases
ProteinModelPortal	Q4L574.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4L574.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000044790; EBSTAP00000043241; EBSTAG00000044788.
GeneID	3481921.
GenomeReviews	Gene locus SH1892 in contig AP006716_GR.
KEGG	sha:SH1892.
NMPDR	fig|279808.3.peg.1930.
PATRIC	19619891. VBIStaHae67511_1868.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0026.
GeneTree	EBGT00050000023923.
HOGENOM	HBG516369.
PhylomeDB	Q4L574.
ProtClustDB	PRK06019.
Enzyme and pathway databases
BioCyc	SHAE279808:SH1892-MONOMER.
Family and domain databases
InterPro	IPR005875. AIR_COase_ATPase-su. IPR011761. ATP-grasp. IPR003135. ATP-grasp_carboxylate-amine. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR011054. Rudment_hybrid_motif. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
KO	K01589.
Pfam	PF02826. 2-Hacid_dh_C. 1 hit. PF02222. ATP-grasp. 1 hit. [Graphical view]
SUPFAM	SSF52440. PreATP-grasp-like. 1 hit. SSF51246. Rudmnt_hyb_motif. 1 hit.
TIGRFAMs	TIGR01161. PurK. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PURK_STAHJ

Accession

Primary (citable) accession number: Q4L574

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	February 7, 2006
Last modified:	January 25, 2012
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program