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PUR6_CANAL
ID   PUR6_CANAL              Reviewed;         568 AA.
AC   Q92210; A0A1D8PK45; P78597; Q5ANJ5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Phosphoribosylaminoimidazole carboxylase;
DE            EC=4.1.1.21;
DE   AltName: Full=AIR carboxylase;
DE            Short=AIRC;
GN   Name=ADE2; OrderedLocusNames=CAALFM_C304520CA;
GN   ORFNames=CaO19.13327, CaO19.5906;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 32354 / B311;
RX   PubMed=9219341;
RX   DOI=10.1002/(sici)1097-0061(19970630)13:8<769::aid-yea133>3.0.co;2-p;
RA   Schmuke J.J., Davisson V.J., Bonar S.L., Gheesling-Mullis K., Dotson S.B.;
RT   "Sequence analysis of the Candida albicans ADE2 gene and physical
RT   separation of the two functionally distinct domains of the
RT   phosphoribosylaminoimidazole carboxylase.";
RL   Yeast 13:769-776(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=9200816;
RX   DOI=10.1002/(sici)1097-0061(19970615)13:7<673::aid-yea122>3.0.co;2-g;
RA   Tsang W.K.P., Cao B.-Y., Wang J.;
RT   "Sequence analysis of Candida albicans phosphoribosyl-aminoimidazole
RT   carboxylase (ADE2) gene.";
RL   Yeast 13:673-676(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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   -!- 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   -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC       family. Class I subfamily. {ECO:0000305}.
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DR   EMBL; U69606; AAC49755.1; -; Genomic_DNA.
DR   EMBL; U75582; AAC49742.1; -; Genomic_DNA.
DR   EMBL; CP017625; AOW28470.1; -; Genomic_DNA.
DR   RefSeq; XP_723120.1; XM_718027.1.
DR   AlphaFoldDB; Q92210; -.
DR   SMR; Q92210; -.
DR   BioGRID; 1218353; 1.
DR   STRING; 237561.Q92210; -.
DR   PRIDE; Q92210; -.
DR   GeneID; 3635259; -.
DR   KEGG; cal:CAALFM_C304520CA; -.
DR   CGD; CAL0000185210; ADE2.
DR   VEuPathDB; FungiDB:C3_04520C_A; -.
DR   eggNOG; KOG2835; Eukaryota.
DR   HOGENOM; CLU_011534_2_1_1; -.
DR   InParanoid; Q92210; -.
DR   OMA; CRAGRKM; -.
DR   OrthoDB; 945274at2759; -.
DR   BRENDA; 4.1.1.21; 1096.
DR   UniPathway; UPA00074; UER00130.
DR   PHI-base; PHI:196; -.
DR   PRO; PR:Q92210; -.
DR   Proteomes; UP000000559; Chromosome 3.
DR   GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IMP:CGD.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046084; P:adenine biosynthetic process; IMP:CGD.
DR   Gene3D; 3.30.1490.20; -; 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   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; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01162; purE; 1.
DR   TIGRFAMs; TIGR01161; purK; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Decarboxylase; Lyase; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..568
FT                   /note="Phosphoribosylaminoimidazole carboxylase"
FT                   /id="PRO_0000075021"
FT   DOMAIN          110..298
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         138..193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   VARIANT         219
FT                   /note="C -> W (in strain: ATCC 32354 / B311)"
FT   VARIANT         248
FT                   /note="L -> P (in strain: ATCC 32354 / B311)"
FT   VARIANT         332
FT                   /note="L -> S (in strain: ATCC 32354 / B311)"
FT   VARIANT         352
FT                   /note="T -> A (in strain: ATCC 32354 / B311)"
FT   CONFLICT        233..234
FT                   /note="AK -> GQ (in Ref. 1; AAC49755 and 2; AAC49742)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   568 AA;  62413 MW;  AEB63A6E0F193F44 CRC64;
     MDSKTVGILG GGQLGRMIVE AAHRLNIKTV ILDAAKSPAK QINALDDHVD GSFTNYDSIV
     KLAEKADVLT VEIEHVDVDA LIKVQEKFPK VEIYPLPETI RLIQDKYLQK NHLIKHDVAV
     TESVAVETNT VDDLLHIGEK FGYPYMLKSR TLAYDGRGNF VVKDKSYCEK ALEFLKDRPL
     YAEKWCPFTK ELAVMVVRSL EGEVFAYPTV ETIHENNICH LVYAPARIPD TLAKKASILA
     KNAVKSFLGC GIFGVEMFLL ENNELLINEI APRPHNSGHY TIDACVTSQF EAHVRAVTGL
     PMPKGFTEFS TSITNAIMLN VLGDKATPNK ELEICRRALE TPHASVYLYG KTTRPERKMG
     HINVVTSSMQ DAESRLSYIL GDTTEIPKSL ATDKESPLVG IIMGSDSDLP VMAVGARILK
     QFGVPFELTI VSAHRTPHRM SEYAIEAPKR GLKCIIAGAG GAAHLPGMVA AMTPLPVIGV
     PVKGSTLDGV DSLHSIVQMP RGIPVATVAI NNSTNAALLA IRILGAYDSK WLTEMNQYML
     NMETEVLGKA ETLEEIGYED YLTDKLKK
 
 
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