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Database: UniProt
Entry: A0A0F8CPV4_CERFI
LinkDB: A0A0F8CPV4_CERFI
Original site: A0A0F8CPV4_CERFI 
ID   A0A0F8CPV4_CERFI        Unreviewed;       618 AA.
AC   A0A0F8CPV4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   RecName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000256|ARBA:ARBA00021059};
DE            EC=4.1.1.21 {ECO:0000256|ARBA:ARBA00012329};
GN   Name=ADE1_3 {ECO:0000313|EMBL:KKF92787.1};
GN   ORFNames=CFO_g4860 {ECO:0000313|EMBL:KKF92787.1};
OS   Ceratocystis fimbriata f. sp. platani.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX   NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF92787.1, ECO:0000313|Proteomes:UP000034841};
RN   [1] {ECO:0000313|EMBL:KKF92787.1, ECO:0000313|Proteomes:UP000034841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFO {ECO:0000313|EMBL:KKF92787.1,
RC   ECO:0000313|Proteomes:UP000034841};
RA   Belbahri L.;
RT   "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT   trees.";
RL   Submitted (APR-2015) 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   -!- 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}.
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:KKF92787.1}.
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DR   EMBL; LBBL01000324; KKF92787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8CPV4; -.
DR   UniPathway; UPA00074; UER00130.
DR   Proteomes; UP000034841; 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   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   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}; Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KKF92787.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034841}.
FT   DOMAIN          119..319
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   618 AA;  66269 MW;  0AEF4F5E90CBDE90 CRC64;
     MSTSPIIGVA GGGQLGQMLT QAAFPLNIPI VTLDNKDAPA KKINHHDNHV TGSFKDAEKL
     RELARRCDFL TVEIEHIDAA VLQEIADNGV TLADGSAKSV EVHPAPRTLA LIKDKFRQKE
     YFASKGISVA EQLPISGGAD FAMSLADAAE KLGLPLMLKS RNDSYDGRGN LKLDTLDAEL
     VSRELGTENL YAEKMVPFVK ELSVMAVRSD VEQQTGGPRV PKTFPYPAVE TVHEDSICAT
     TFYPPRGVSK EINEKAQALA SKVADQLWGR GVFAVEMFLT SEGNLLINEV APRPHNSGHY
     TIEAIPQMSQ YKAQLYAIRG LIPASQKLTP RCASSIMINV LGGAGPASHV PLVSLAETLY
     NDDMDIHIHM YGKDAKPSRK IGHITLCSNK PIAELEALAQ PLIELASKIH AERVEAGSKA
     LRNAAAPAVV PSAAQKQAAA QVLVIMGSDS DMPVLRAGLE ILEEFKVPIR VDITSAHRTP
     GYMAEVVEAA ASEGIKVIIG AAGGAAHLPG MAASHTPLPV IGVPVKATHL DGVDSLHSIV
     QMPRGIPVAT VGINNSTNAA LLAIRILGAE FPEYRIKMEE YMTGMKDSVK AKSSKVLDIG
     WRAYLDDTIW PAWGHSSF
//
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