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Database: UniProt
Entry: H2C7K9_9CREN
LinkDB: H2C7K9_9CREN
Original site: H2C7K9_9CREN 
ID   H2C7K9_9CREN            Unreviewed;       339 AA.
AC   H2C7K9;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000256|RuleBase:RU361200};
DE            Short=N5-CAIR synthase {ECO:0000256|RuleBase:RU361200};
DE            EC=6.3.4.18 {ECO:0000256|RuleBase:RU361200};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000256|RuleBase:RU361200};
GN   Name=purK {ECO:0000256|RuleBase:RU361200};
GN   ORFNames=MetMK1DRAFT_00025580 {ECO:0000313|EMBL:EHP68135.1};
OS   Metallosphaera yellowstonensis MK1.
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=671065 {ECO:0000313|EMBL:EHP68135.1, ECO:0000313|Proteomes:UP000003980};
RN   [1] {ECO:0000313|EMBL:EHP68135.1, ECO:0000313|Proteomes:UP000003980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MK1 {ECO:0000313|EMBL:EHP68135.1,
RC   ECO:0000313|Proteomes:UP000003980};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Kozubal M., Macur R.E., Jay Z., Inskeep W., Woyke T.;
RT   "Improved High-Quality Draft sequence of Metallosphaera yellowstonensis
RT   MK1.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole
CC       ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole
CC       ribonucleotide (N5-CAIR). {ECO:0000256|RuleBase:RU361200}.
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:0000256|RuleBase:RU361200};
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:0000256|RuleBase:RU361200}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family.
CC       {ECO:0000256|RuleBase:RU361200}.
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DR   EMBL; JH597770; EHP68135.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2C7K9; -.
DR   STRING; 671065.MetMK1DRAFT_00025580; -.
DR   eggNOG; arCOG01597; Archaea.
DR   HOGENOM; CLU_011534_0_0_2; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000003980; Unassembled WGS sequence.
DR   GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion 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-UniPathway.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005875; PurK.
DR   InterPro; IPR040686; PurK_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   NCBIfam; TIGR01161; purK; 1.
DR   PANTHER; PTHR11609:SF5; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR   PANTHER; PTHR11609; PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7; 1.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF17769; PurK_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|RuleBase:RU361200};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|RuleBase:RU361200};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW   ECO:0000256|RuleBase:RU361200};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003980}.
FT   DOMAIN          82..261
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   339 AA;  39060 MW;  356C72F08A8266E3 CRC64;
     MILEGRKFPI TFLVYAEKGE PACRIADLCF KESYEKVIEE CDIVTFEFEH VDEAPLQLAE
     DLGKLLPRLN SVVLKRARHL EKEFLKREGF PVPRFVTVEG GDEALRVLRD EFNNVGVVKK
     SEGGYDGRGQ YFIRGDPDRY QFLREERGLF VVEELVNYDF EASIIAVRSG NEFRAYPPTF
     NYNEKGILVY NYGPYGNPEM IRLAEKLTEK LNYVGVMGIE FFIRRGKVMI NEYAPRVHNT
     GHYTLDGAEI SQFEHHLRAI TGMELGETRL LSPSGMVNLL GVHYPPMDVL RYGSVYWYGK
     EVRRRRKVGH VNVVGKDLED VRAKIENVMK LTYPNGLDL
//
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