ID H0GNP2_SACCK Unreviewed; 555 AA.
AC H0GNP2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 13-SEP-2023, entry version 47.
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000256|ARBA:ARBA00021059, ECO:0000256|PIRNR:PIRNR001340};
DE EC=4.1.1.21 {ECO:0000256|ARBA:ARBA00012329, ECO:0000256|PIRNR:PIRNR001340};
GN ORFNames=VIN7_4552 {ECO:0000313|EMBL:EHN04605.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN04605.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN04605.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN04605.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + H(+)
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2;
CC Xref=Rhea:RHEA:10792, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:137981; EC=4.1.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001244,
CC ECO:0000256|PIRNR:PIRNR001340};
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 (carboxylase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004747, ECO:0000256|PIRNR:PIRNR001340}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC family. Class I subfamily. {ECO:0000256|ARBA:ARBA00006114,
CC ECO:0000256|PIRNR:PIRNR001340}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHN04605.1}.
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DR EMBL; AGVY01000047; EHN04605.1; -; Genomic_DNA.
DR AlphaFoldDB; H0GNP2; -.
DR HOGENOM; CLU_011534_2_1_1; -.
DR PhylomeDB; H0GNP2; -.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000009009; Unassembled WGS sequence.
DR GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase 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:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1970; -; 1.
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 HAMAP; MF_01929; PurE_classI; 1.
DR HAMAP; MF_01928; PurK; 1.
DR InterPro; IPR016301; Ade2_fungi/plant.
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; IPR033747; PurE_ClassI.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR005875; PurK.
DR InterPro; IPR040686; PurK_C.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR01162; purE; 1.
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; PF00731; AIRC; 1.
DR Pfam; PF02222; ATP-grasp; 1.
DR Pfam; PF17769; PurK_C; 1.
DR PIRSF; PIRSF001340; AIR_carboxylase; 1.
DR SMART; SM01001; AIRC; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 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|PIRNR:PIRNR001340};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW ECO:0000256|PIRNR:PIRNR001340};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001340};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001340, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW ECO:0000256|PIRNR:PIRNR001340}.
FT DOMAIN 94..282
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 555 AA; 60641 MW; 2A24DFB7AB737DE6 CRC64;
MIVEAANRLN IKTVILDAEN SPAKQISNSN DHVNGSFSNP LDIEKLAEKC DVLTIEIEHV
DVPTLKNLQV KHPKLKIYPS PETIGLIQDK YIQKEHLIKN GIAVTQSVPV EQASETSLLN
VGRDLGFPFV LKSRTLAYDG RGNFVVKNKE MIPEALEVLK DRPLYAEKWA PFTKELAVMI
VRSVNGLVFS YPIVETIHKD NICDLCYAPA RVPDSVQLKA KLLAENAIKS FPGCGIFGVE
MFYLETGELL INEIAPRPHN SGHYTIDACV TSQFEAHLRS ILDLPMPKNF TSFSTITTNA
IMLNVLGDKH TKDKELETCE RALATPGSSV YLYGKESRPN RKVGHINIIA SSMAECEQRL
NYITGRTDIP IKISVAQKLD LEAMVKPLVG IIMGSDSDLP VMSAACAVLK DFGVPFEVTI
VSAHRTPHRM SAYAISASKR GIKTIIAGAG GAAHLPGMVA AMTPLPVIGV PVKGSCLDGV
DSLHSIVQMP RGVPVATVAI NNSTNAALLA VRLLGAYDSS YTTKMEQFLL KQEEEVLVKA
QKLETVGYEA YLENK
//
