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Database: UniProt
Entry: A0A015L7Q2_RHIIW
LinkDB: A0A015L7Q2_RHIIW
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ID   A0A015L7Q2_RHIIW        Unreviewed;       559 AA.
AC   A0A015L7Q2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   13-SEP-2023, entry version 38.
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=RirG_039470 {ECO:0000313|EMBL:EXX75709.1};
OS   Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX75709.1, ECO:0000313|Proteomes:UP000022910};
RN   [1] {ECO:0000313|EMBL:EXX75709.1, ECO:0000313|Proteomes:UP000022910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA   Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA   Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA   Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA   Huang S.;
RT   "Single nucleus genome sequencing reveals high similarity among nuclei of
RT   an endomycorrhizal fungus.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXX75709.1}.
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DR   EMBL; JEMT01012375; EXX75709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A015L7Q2; -.
DR   STRING; 1432141.A0A015L7Q2; -.
DR   HOGENOM; CLU_011534_2_1_1; -.
DR   UniPathway; UPA00074; UER00130.
DR   Proteomes; UP000022910; 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:UP000022910}.
FT   DOMAIN          110..298
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   559 AA;  61343 MW;  0141747339140064 CRC64;
     MNSKKIGVLG GGQLGRMLVE AASRLNISVT ILDSPVNSPA KQIQATSTHV HGDFKDPLKI
     QELAQNVDVL TIEIEHVDVE ILEKLFSKKS VEIHPHPYTI RIIQDKFLQK THLSQNEIPV
     VDFIDIPDKE SLNIAIEKFS YPIMLKSKLL AYDGRGNYVI NSEDEITDAL KTLGNFKIPL
     YVERWTPFVK ELAVMVIRSV DGVIKSYPVV ETVHKENICH LVIVPAQVDG VILRCAKEIA
     EKAIQTLKGA GIFGVEMFLM KNGQIYINEI APRPHNSGHY TIEACETSQY ENHIRSILNM
     PIGSTSLKVP AAAMINVLGK SEDIHETLGP CVEALTTPGA TIHLYGKKEC RKGRKMGHIT
     VVADSISQLY KRINPILNID DENDTSTTSS KNIQPLVGII MGSDSDLPTM KACAEVLKSF
     DVPFELSIVS AHRTPMRMVE YAKTAHVRGL KAIIAGAGGA AHLPGMVAAL TPLLVIGVPV
     KGKSLDGVDS LYSIVQMPRG VPVATVAINN STNAGLLAVR HLGAFMPSYL QKMQEFTERQ
     ESEVLAKVDK LDQVGWENY
//
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