ID   PYCA_METJA              Reviewed;         501 AA.
AC   Q58626;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, 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=MJ1229;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-12, FUNCTION, AND MASS SPECTROMETRY.
RX   PubMed=11195096; DOI=10.1007/s002030000225;
RA   Mukhopadhyay B., Patel V.J., Wolfe R.S.;
RT   "A stable archaeal pyruvate carboxylase from the hyperthermophile
RT   Methanococcus jannaschii.";
RL   Arch. Microbiol. 174:406-414(2000).
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. {ECO:0000269|PubMed:11195096}.
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;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC   -!- ACTIVITY REGULATION: Inhibited by magnesium, when its concentration
CC       exceeded the ATP one, and by high concentration of ATP and alpha-
CC       ketoglutarate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5.;
CC       Temperature dependence:
CC         Optimum temperature is 80-90 degrees Celsius.;
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Heterooctamer of four A and four B subunits.
CC   -!- MASS SPECTROMETRY: Mass=55500; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11195096};
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DR   EMBL; L77117; AAB99232.1; -; Genomic_DNA.
DR   PIR; D64453; D64453.
DR   RefSeq; WP_010870741.1; NC_000909.1.
DR   AlphaFoldDB; Q58626; -.
DR   SMR; Q58626; -.
DR   STRING; 243232.MJ_1229; -.
DR   PRIDE; Q58626; -.
DR   EnsemblBacteria; AAB99232; AAB99232; MJ_1229.
DR   GeneID; 1452125; -.
DR   KEGG; mja:MJ_1229; -.
DR   eggNOG; arCOG01590; Archaea.
DR   HOGENOM; CLU_000395_3_2_2; -.
DR   InParanoid; Q58626; -.
DR   OMA; FVEICSH; -.
DR   OrthoDB; 36803at2157; -.
DR   PhylomeDB; Q58626; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000805; 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.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Gluconeogenesis; Ligase; Magnesium;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding; Pyruvate;
KW   Reference proteome.
FT   CHAIN           1..501
FT                   /note="Pyruvate carboxylase subunit A"
FT                   /id="PRO_0000146828"
FT   DOMAIN          1..445
FT                   /note="Biotin carboxylation"
FT   DOMAIN          120..316
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   ACT_SITE        291
FT                   /evidence="ECO:0000255"
FT   BINDING         116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   501 AA;  55403 MW;  04D2E401892F872F CRC64;
     MFNKVLIANR GEIAIRIIRA CWELGIKTVA VYSEADKRSL HATLADEAYC IGPAPAAKSY
     LNIDAILNVA EKAKVDAIHP GYGFLAENAE FARAVKKAGF EFIGPNPDAI EAMGSKINAK
     KIMKKAGVPL IPGSEGAIED IDEAIEIAEA IGFPVVVKAS AGGGGMGMSV AYSKEELKEV
     IESARNIAKS AFGDPTVFIE KYLENPRHIE IQLLGDKHGN IIHLGDRECS IQRRHQKLIE
     EAPSPIMTEE LRERMGEAAI KAGKAINYDS AGTVEFLYEN GNFYFLEMNT RIQVEHTVTE
     QVTGIDLVKA MIKIAAGEEL TLKQEDVKIR GHAIECRINA EDPLNDFVPC PGKIKLYRSP
     GGPGVRIDSG VYGGAEIPPY YDSMIAKLIT YGNSREEAIA RMKRALREYV IIGVKTNIPF
     HRAVLEEENF LKGNISTHYV EQNMHKLREK MVKYALESRD LYSVVSEKVF EKNKKIAAAV
     GGLTMYISQI MKENEVNNKE W