PURK_STAHJ
ID PURK_STAHJ Reviewed; 374 AA.
AC Q4L574;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE Short=N5-CAIR synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE EC=6.3.4.18 {ECO:0000255|HAMAP-Rule:MF_01928};
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_01928};
GN Name=purK {ECO:0000255|HAMAP-Rule:MF_01928}; OrderedLocusNames=SH1892;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole
CC ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR). {ECO:0000255|HAMAP-Rule:MF_01928}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP +
CC hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole +
CC ADP + 2 H(+) + phosphate; Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58730, ChEBI:CHEBI:137981, ChEBI:CHEBI:456216;
CC EC=6.3.4.18; Evidence={ECO:0000255|HAMAP-Rule:MF_01928};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_01928}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01928}.
CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC Rule:MF_01928}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE05201.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP006716; BAE05201.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_029376687.1; NC_007168.1.
DR AlphaFoldDB; Q4L574; -.
DR SMR; Q4L574; -.
DR STRING; 279808.SH1892; -.
DR EnsemblBacteria; BAE05201; BAE05201; SH1892.
DR GeneID; 58061988; -.
DR KEGG; sha:SH1892; -.
DR eggNOG; COG0026; Bacteria.
DR HOGENOM; CLU_011534_0_1_9; -.
DR OrthoDB; 1165275at2; -.
DR UniPathway; UPA00074; UER00942.
DR Proteomes; UP000000543; Chromosome.
DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1490.20; -; 1.
DR HAMAP; MF_01928; PurK; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR005875; PurK.
DR InterPro; IPR040686; PurK_C.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF02222; ATP-grasp; 1.
DR Pfam; PF17769; PurK_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01161; purK; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..374
FT /note="N5-carboxyaminoimidazole ribonucleotide synthase"
FT /id="PRO_0000075011"
FT DOMAIN 112..296
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 153..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 183..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 266..267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
SQ SEQUENCE 374 AA; 42583 MW; 1E36AEF46296E436 CRC64;
MNFNKLKFGD TIGIIGGGQL GKMMAQSAQK MGFKVICLDP NPDSPCKSVA HEFITAAYDD
EEALHELGEK SDVITYEFEN ISAEQLIRLT QKFNIPQGYQ AIQLLQDRLT EKQTLQKAGS
KIVPFLPIKE EKDLNVVINQ LGYPFIVKTR FGGYDGKGQV LVKNEESIQE AKDLISQQEC
VAEQFLDIAL EVSLTVTIGN QKQITYFPLQ ENEHRNQILF KTIVPARSDK EQEARDEVNK
IINEVHFVGT FTVEFFIDKS NNLYVNEIAP RPHNSGHYSI EACDYSQFDT HILAVTGQNL
PKEIEILKPA VMMNLLGRDL DLLEDKFANH PEWHVHIYGK PERKPNRKMG HMTILTNNVD
ETEKAMLKQF EGRE
