GenomeNet

Database: UniProt
Entry: Q58626
LinkDB: Q58626
Original site: Q58626 
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   16-JAN-2019, entry version 126.
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 /
OS   JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   Methanococcales; 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.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., 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,
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. {ECO:0000269|PubMed:11195096}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) +
CC         oxaloacetate + phosphate; Xref=Rhea:RHEA:20844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         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
CC       concentration exceeded the ATP one, and by high concentration of
CC       ATP and alpha-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; Range=1-501;
CC       Evidence={ECO:0000269|PubMed:11195096};
DR   EMBL; L77117; AAB99232.1; -; Genomic_DNA.
DR   PIR; D64453; D64453.
DR   RefSeq; WP_010870741.1; NC_000909.1.
DR   ProteinModelPortal; Q58626; -.
DR   SMR; Q58626; -.
DR   STRING; 243232.MJ_1229; -.
DR   EnsemblBacteria; AAB99232; AAB99232; MJ_1229.
DR   GeneID; 1452125; -.
DR   KEGG; mja:MJ_1229; -.
DR   eggNOG; arCOG01590; Archaea.
DR   eggNOG; COG0439; LUCA.
DR   InParanoid; Q58626; -.
DR   KO; K01959; -.
DR   OMA; FVEICSH; -.
DR   OrthoDB; 36803at2157; -.
DR   PhylomeDB; Q58626; -.
DR   BioCyc; MJAN243232:G1GKE-1334-MONOMER; -.
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; Complete proteome; Direct protein sequencing;
KW   Gluconeogenesis; Ligase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Pyruvate;
KW   Reference proteome.
FT   CHAIN         1    501       Pyruvate carboxylase subunit A.
FT                                /FTId=PRO_0000146828.
FT   DOMAIN        1    445       Biotin carboxylation.
FT   DOMAIN      120    316       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   ACT_SITE    291    291       {ECO:0000255}.
FT   BINDING     116    116       ATP. {ECO:0000250}.
FT   BINDING     200    200       ATP. {ECO:0000250}.
FT   BINDING     235    235       ATP. {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
//
DBGET integrated database retrieval system