ID A0A0D9Y4T3_9ORYZ Unreviewed; 703 AA.
AC A0A0D9Y4T3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=phosphoribosylaminoimidazole carboxylase {ECO:0000256|ARBA:ARBA00012329};
DE EC=4.1.1.21 {ECO:0000256|ARBA:ARBA00012329};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM01G07360.2};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM01G07360.2}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM01G07360.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 -!- 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}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC family. Class I subfamily. {ECO:0000256|ARBA:ARBA00006114}.
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DR AlphaFoldDB; A0A0D9Y4T3; -.
DR STRING; 40148.A0A0D9Y4T3; -.
DR EnsemblPlants; OGLUM01G07360.2; OGLUM01G07360.2; OGLUM01G07360.
DR Gramene; OGLUM01G07360.2; OGLUM01G07360.2; OGLUM01G07360.
DR eggNOG; KOG2835; Eukaryota.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000026961; 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-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01929; PurE_classI; 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; 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 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|PROSITE-
KW ProRule:PRU00409}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961}.
FT DOMAIN 175..363
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 29..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 76632 MW; ECFD3FE89BC17506 CRC64;
MHARLLSAPS HAFAASSSPL PFAAAHPCRA SWTPRPTSPP PPLSLLRATA SMHPSPPPEG
HSDQPVHGVT NTVVGVLGGG QLGKMLCQAA SQMGVRMAIL DPLEDCPASS VCHEHVVGSF
NDGATVSEFA KRCGVLTVEI EHVDAVTLEK LEKQGIDCEP KASTIMIIQD KYRQKTHFSK
FGIPLPDFVE VDTLSSIEKA GEMFGYPLMV KSKRLAYDGR GNAVAHDKKE LSSVVASLGG
FEHGLYVERW TSFVKELSVI VARSRDGSTV CYPVVETIHK DNICHVVEAP AEVPDKIKKL
ATNVAEKAIK SLEGAGVFAV ELFLTQDNQV LLNEVAPRPH NSGHHTIESC YTSQYEQHLR
AILGLPLGDP SMKAPASIMY NILGEDEGEA GFTQAHQLIE RALDISGASV HWYAKPEIRK
QRKMGHITIV GPSKYSVKAR LDKLLQRDAY DPKKVKPRAA IIMGSDSDLP VMKDAAVVLK
KFNIPFELTI VSAHRTPERM YHYALSAKER GLEVIIAGMV ASLTSVPVIG VPIMTSSLHG
TDSLLSIVQM PKGIPVATVA IGNAENAGLL AVRMLASRDP ELGDKATEYQ HDLRDMWRPG
EGVPTYEVKD VDETRRMSIS WRPGEGVPTY KVKDVDEARR MSISTSIFNK EKVFLAGHEE
EGPAQAQNLR DSLAEAKSDI VLHKNFADRG LATEAQAQME QFE
//
