(data stored in ACNUC7421 zone)

SWISSPROT: Q75BR1_ASHGO

ID   Q75BR1_ASHGO            Unreviewed;       565 AA.
AC   Q75BR1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 122.
DE   RecName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000256|PIRNR:PIRNR001340};
DE            EC=4.1.1.21 {ECO:0000256|PIRNR:PIRNR001340};
GN   ORFNames=AGOS_ACR210C {ECO:0000313|EMBL:AAS51436.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51436.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51436.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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|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|PIRNR:PIRNR001340}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC       family. Class I subfamily. {ECO:0000256|PIRNR:PIRNR001340}.
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DR   EMBL; AE016816; AAS51436.1; -; Genomic_DNA.
DR   RefSeq; NP_983612.1; NM_208965.1.
DR   STRING; 33169.AAS51436; -.
DR   EnsemblFungi; AAS51436; AAS51436; AGOS_ACR210C.
DR   GeneID; 4619744; -.
DR   KEGG; ago:AGOS_ACR210C; -.
DR   HOGENOM; HOG000034027; -.
DR   InParanoid; Q75BR1; -.
DR   KO; K11808; -.
DR   OMA; ITFDHEH; -.
DR   UniPathway; UPA00074; UER00130.
DR   Proteomes; UP000000591; Chromosome III.
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; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.7700; -; 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; IPR035893; PurE_sf.
DR   InterPro; IPR005875; PurK.
DR   InterPro; IPR040686; PurK_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
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; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52255; SSF52255; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01162; purE; 1.
DR   TIGRFAMs; TIGR01161; purK; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75BR1.
DR   SWISS-2DPAGE; Q75BR1.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001340, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Decarboxylase {ECO:0000256|PIRNR:PIRNR001340};
KW   Lyase {ECO:0000256|PIRNR:PIRNR001340};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001340, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|PIRNR:PIRNR001340};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          110..297
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   565 AA;  60780 MW;  080C2ED701291E02 CRC64;
     MDHRTVGILG GGQLGRMIVE AANRLNVKTV VLDGPNSPAK QINAVGEHVE GSFGVAADIE
     ELAQRSDVLT VEIEHVDVGT LRGLQAKMPS LTIYPTPEAI ELIQDKHVQK EHLSGHGVAV
     AESIAVEGTE PALVAVGEQL GYPYMLKARK LAYDGRGNFV VKSRDSIAEA LETLADRSLY
     AERWAPFVRE LAVMIVRSPE GQLFSYPMVE TVHQNNICHL CYAPARVADS IQLRAKLLAE
     RAVATLPGAG IFGVEMFLLE DGELLVNEIA PRPHNSGHYT IDACVTSQFE AHLRSILGLP
     MPRGFSSMAT SNTHAIMLNV LGDPQVKDKE LAICERALET PGASVYLYGK ESKPKRKVGH
     INIVASSMQE AERKLRFITG GAVSLEEDGH NPQGDASPLV GIIMGSDSDL PVMSKACEIL
     TQFGVPYEVT IVSAHRTPHR MSKYAIEASE RGIKAIIAGA GGAAHLPGMV AAMTPLPVIG
     VPVKGSVLDG VDSLHSIVQM PRGVPVATVA INNSTNAALL AVRLLGAYDT KYHALMQQFL
     LKQEEEVLGK AEKLETIGYR AYLDQ
//

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