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 01-MAY-2013, entry version 95.
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; EAPSPIM; -.
DR ProtClustDB; PRK08654; -.
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: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; SSF52440; PreATP-grasp-like; 1.
DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 1.
DR TIGRFAMs; TIGR00514; accC; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; FALSE_NEG.
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
//
