ID R7YPJ4_CONA1 Unreviewed; 569 AA.
AC R7YPJ4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=W97_02996 {ECO:0000313|EMBL:EON63768.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON63768.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; JH767565; EON63768.1; -; Genomic_DNA.
DR RefSeq; XP_007779085.1; XM_007780895.1.
DR AlphaFoldDB; R7YPJ4; -.
DR STRING; 1168221.R7YPJ4; -.
DR GeneID; 19900307; -.
DR eggNOG; KOG2835; Eukaryota.
DR HOGENOM; CLU_011534_2_1_1; -.
DR OMA; KTVRGGY; -.
DR OrthoDB; 7491at2759; -.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000016924; 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:UP000016924}.
FT DOMAIN 110..298
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 569 AA; 62058 MW; FF4D1D27C1693A5B CRC64;
MDGKVVGVLG GGQLGRMLIE AANRLGVRVN ILDSPGAPAK QISAHDGHVD GSFKDRKGIE
ELASRCDVLT VEIEHVDTEV LEDVQEKFEN VIIEPSWSTI RLIQDKYRQK EHLASHQVAT
AESVALDSNS EEELRNVGSK LGYPFMLKSR KEAYDGRGNF PVRSEEDVPA ALQALGKNAL
YAERWADFKM ELAVMVVKTQ DGTLAFPTVE THHENSVCKL VWAPARDIPR DVTKKAQDLA
KKAVAAFEGK GVFGVEMFLL KDGSLLINEI APRPHNSGHY TIEACPISQY DAHLRAILDL
PIPESSLRLR EPAIMLNILG GKAADSHIAF VRDHALANPR TSIHLYGKAE ARPGRKMGHV
TVTASTMREA ETLIQPLIDA VDDAAGKPLG PRETKQEKPL VAVIMGSDSD MPVLKGAFEI
LRKFGISYQA RILSAHRTPD RMFDFAKRAE GEGFRVIIAA AGGAAHLPGM TASDTVLPVI
GVPVRASHLD GLDSLLSEVQ MPRGVPCAVV GINNSTNAGL LAARILGVAD ERIRRAIREH
QEASWEEVKA KDERLKEIGP EEYLKGMGK
//
