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Database: UniProt
Entry: A0A367KU02_RHIST
LinkDB: A0A367KU02_RHIST
Original site: A0A367KU02_RHIST 
ID   A0A367KU02_RHIST        Unreviewed;       554 AA.
AC   A0A367KU02;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   13-SEP-2023, entry version 15.
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   Name=ADE2_3 {ECO:0000313|EMBL:RCI05675.1};
GN   ORFNames=CU098_012835 {ECO:0000313|EMBL:RCI05675.1};
OS   Rhizopus stolonifer (Rhizopus nigricans).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4846 {ECO:0000313|EMBL:RCI05675.1, ECO:0000313|Proteomes:UP000253551};
RN   [1] {ECO:0000313|EMBL:RCI05675.1, ECO:0000313|Proteomes:UP000253551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCI05675.1,
RC   ECO:0000313|Proteomes:UP000253551};
RX   PubMed=29674435; DOI=10.1534/g3.118.200235;
RA   Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA   Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA   Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA   Heitman J., Vilgalys R., Stajich J.E.;
RT   "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL   G3 (Bethesda) 8:2007-2018(2018).
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:RCI05675.1}.
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DR   EMBL; PJQM01000329; RCI05675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367KU02; -.
DR   STRING; 4846.A0A367KU02; -.
DR   EnsemblFungi; RCI05675; RCI05675; CU098_012835.
DR   UniPathway; UPA00074; UER00130.
DR   Proteomes; UP000253551; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253551}.
FT   DOMAIN          110..296
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   554 AA;  59747 MW;  A282116A73AE7816 CRC64;
     MDSQKVGILG GGQLGRMMIE AASRLNLQVT VLDDPTDAPA KQIEATQSHI HGAFNDASKI
     RELASQVDVL TVEIEHVDAE VLAAIEKEGH VRVCPSAFTV KTIQDKYVQK QHLTSHGIPV
     ADYVECPNTE AVKKAAQQFG YPFMLKSKTM AYDGKGNYAI KSEEDIEKAV ATLSKTPLYA
     EKWAPFVKEL AVMVVRRANG EVRAYPVVET IHKNSICHLV IAPAQIDGSV AAKAQGIAEL
     AIKTFPGAGI FGVEMFVMAD GEILLNEIAP RPHNSGHYTI EACETSQFEN HMRAVLDMPL
     GSTAMKVSAS IMVNILGENE DMESCYKPCH EALLADGATI HLYGKKACRA GRKMGHITLV
     GDSMMQVQKN LKPILEAIEP GVERPLTVRP LVAMIMGSDS DLPVMKVGAK ILKEFGIPFE
     LSIVSAHRTP IRMVEYAQSA AERGLMAIIA GAGGAAHLPG MVASMTPLPV IGVPVKGSSL
     DGVDSLHSIV QMPRGIPVAT VAINNSTNAA LLAIRILAAS IPSIQKQMVD YMNNMEGEVM
     NKIERLDNVG WENY
//
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