PYCA_ARCFU
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 03-AUG-2022, entry version 135.
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 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving
CC the ATP-dependent carboxylation of the covalently attached biotin in
CC the first step and the transfer of the carboxyl group to pyruvate in
CC the second.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Heterooctamer of four A and four B subunits. {ECO:0000250}.
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DR EMBL; AE000782; AAB91012.1; -; Genomic_DNA.
DR PIR; D69277; D69277.
DR RefSeq; WP_010877731.1; NC_000917.1.
DR AlphaFoldDB; O30019; -.
DR SMR; O30019; -.
DR STRING; 224325.AF_0220; -.
DR EnsemblBacteria; AAB91012; AAB91012; AF_0220.
DR GeneID; 24793754; -.
DR KEGG; afu:AF_0220; -.
DR eggNOG; arCOG01590; Archaea.
DR HOGENOM; CLU_000395_3_2_2; -.
DR OMA; FVEICSH; -.
DR OrthoDB; 36803at2157; -.
DR PhylomeDB; O30019; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 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; Gluconeogenesis; Ligase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Pyruvate; Reference proteome.
FT CHAIN 1..506
FT /note="Pyruvate carboxylase subunit A"
FT /id="PRO_0000146827"
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT DOMAIN 120..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT ACT_SITE 290
FT /evidence="ECO:0000255"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
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
