N5-carboxyaminoimidazole ribonucleotide synthase - Staphylococcus epidermidis (strain ATCC 35984 / RP62A)

Contribute

Send feedback

Read comments (?) or add your own

Q5HQA5 (PURK_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	SERP0650

Organism

Staphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]

Taxonomic identifier

176279 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	375 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.

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 – 375

375

N5-carboxyaminoimidazole ribonucleotide synthase

PRO_0000075009

Regions

Domain

112 – 296

185

ATP-grasp

Nucleotide binding

183 – 186

ATP By similarity

Nucleotide binding

266 – 267

ATP By similarity

Sites

Binding site

108

ATP By similarity

Binding site

148

ATP By similarity

Binding site

159

ATP By similarity

Binding site

191

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q5HQA5 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: F17CF729A50414C4
Show »

FASTA

375

43,226

        10         20         30         40         50         60 
MNFSKLKFGA TIGIIGGGQL GKMMAQSAQK MGYKVIVLDP NEDCPCRYVA HQFIHANYDD 

        70         80         90        100        110        120 
EQALNQLGEN SDVVTYEFEN ISSEQLKKLT KLYHIPQGYQ AIELLQDRLT EKQTLLEANT 

       130        140        150        160        170        180 
QIVPFVQIQT NQDLLKAIEK LGFPFIVKTR FGGYDGKGQI LVRNDSELDE AYQLVEKQEC 

       190        200        210        220        230        240 
VAEQYLDIQK EVSLTVTIGN EQQTTYFPLQ ENEHQNQILF KTVVPARSDK ENEARKEVEK 

       250        260        270        280        290        300 
ITRAIHFVGT FTVEFFIDKE NNLYVNEIAP RPHNSGHYSI EACDYSQFDT HILAITGQKL 

       310        320        330        340        350        360 
PQAIELLKPT VMMNLLGRDL DLLENEFSRH PDWHIHIYGK KERKPDRKMG HMTLLTDDVN 

       370 
QTEQYMLMKF EGRDK

« Hide

References

[1]

"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H.

Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000029 Genomic DNA. Translation: AAW53996.1.
RefSeq	YP_188235.1. NC_002976.3.
3D structure databases
ProteinModelPortal	Q5HQA5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HQA5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000042862; EBSTAP00000041405; EBSTAG00000042860.
GeneID	3240490.
GenomeReviews	Gene locus SERP0650 in contig CP000029_GR.
KEGG	ser:SERP0650.
NMPDR	fig\|176279.3.peg.521.
PATRIC	19612173. VBIStaEpi130894_0630.
TIGR	SERP0650.
Phylogenomic databases
eggNOG	COG0026.
GeneTree	EBGT00050000023923.
HOGENOM	HBG516369.
OMA	GRKMGHF.
PhylomeDB	Q5HQA5.
ProtClustDB	PRK06019.
Enzyme and pathway databases
BioCyc	SEPI176279:SERP0650-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_STAEQ

Accession

Primary (citable) accession number: Q5HQA5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	February 15, 2005
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents