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Database: UniProt
Entry: O30019
LinkDB: O30019
Original site: O30019 
ID   PYCA_ARCFU              Reviewed;         506 AA.
AC   O30019;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   14-MAY-2014, entry version 98.
DE   RecName: Full=Pyruvate carboxylase subunit A;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase A;
GN   Name=pycA; OrderedLocusNames=AF_0220;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM
OS   9628 / NBRC 100126).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction,
CC       involving the ATP-dependent carboxylation of the covalently
CC       attached biotin in the first step and the transfer of the carboxyl
CC       group to pyruvate in the second.
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate + HCO(3)(-) = ADP + phosphate +
CC       oxaloacetate.
CC   -!- COFACTOR: Magnesium or manganese or cobalt (By similarity).
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Heterooctamer of four A and four B subunits (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC   -!- SIMILARITY: Contains 1 biotin carboxylation domain.
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DR   EMBL; AE000782; AAB91012.1; -; Genomic_DNA.
DR   PIR; D69277; D69277.
DR   RefSeq; NP_069058.1; NC_000917.1.
DR   ProteinModelPortal; O30019; -.
DR   SMR; O30019; 1-441.
DR   STRING; 224325.AF0220; -.
DR   PRIDE; O30019; -.
DR   EnsemblBacteria; AAB91012; AAB91012; AF_0220.
DR   GeneID; 1483431; -.
DR   KEGG; afu:AF0220; -.
DR   eggNOG; COG0439; -.
DR   KO; K01959; -.
DR   OMA; IRRMQNA; -.
DR   BioCyc; AFUL224325:GJBC-224-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; CPSase_L_chain; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR00514; accC; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Gluconeogenesis; Ligase; Magnesium;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding; Pyruvate;
KW   Reference proteome.
FT   CHAIN         1    506       Pyruvate carboxylase subunit A.
FT                                /FTId=PRO_0000146827.
FT   DOMAIN        1    443       Biotin carboxylation.
FT   DOMAIN      120    315       ATP-grasp.
FT   ACT_SITE    290    290       Potential.
FT   BINDING     116    116       ATP (By similarity).
FT   BINDING     199    199       ATP (By similarity).
FT   BINDING     234    234       ATP (By similarity).
SQ   SEQUENCE   506 AA;  57438 MW;  39B765F319235AD1 CRC64;
     MFSKILVANR GEIAVRVMRA CRELGIKTVG VYSSADKRAF HRVYADECYY IGKADPRDSY
     LNIDRIIEVA KKSGAEAIHP GYGFLAENAE FAERCEEEGI VFIGPSPEVI RIAGSKVRSR
     ESMQRAGVPV IPGSPKIDTV DEAKEWAEKI GYPVAVKASG GGGGIGIVVV NSQEELEEAF
     RKSKKLGESY FKDSTVYLEK YLARPRHIEV QILADQHGNV IHLGERECSI QRRHQKLIEE
     APSPALNEEM REELGKLAVK GAREIGYTNA GTFEFLYENG NFYFLEINSR LQVEHTITEV
     VTGIDIVKYQ IRIAYGEELR HGQEDVAIRG HAIECRINAE DPVNFYPRSG RILHYRSPGG
     IGIRVDSGIH MGYRIPEEYD SMISKLIAYG ETREEAIARM KRALYEYIIE GVETNIPFHF
     AVLNDEEFVR GNIHTKFVEE RNIAEKVKEY LRIFRPIKAR LDEIFMESEF TWEEISAIVT
     AIDAYEQELE RGIEERIWQA IFSLGA
//
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