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Database: UniProt
Entry: Q58628
LinkDB: Q58628
Original site: Q58628 
ID   PYCB_METJA              Reviewed;         567 AA.
AC   Q58628;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JAN-2019, entry version 127.
DE   RecName: Full=Pyruvate carboxylase subunit B;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase B;
GN   Name=pycB; OrderedLocusNames=MJ1231;
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 190-195; 260-270; 277-289; 277-289; 309-325;
RP   328-358; 370-380; 386-409; 422-438; 491-506 AND 491-506, FUNCTION, AND
RP   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=64160; Method=MALDI; Range=1-567;
CC       Evidence={ECO:0000269|PubMed:11195096};
DR   EMBL; L77117; AAB99233.1; -; Genomic_DNA.
DR   PIR; F64453; F64453.
DR   RefSeq; WP_010870743.1; NC_000909.1.
DR   ProteinModelPortal; Q58628; -.
DR   SMR; Q58628; -.
DR   STRING; 243232.MJ_1231; -.
DR   EnsemblBacteria; AAB99233; AAB99233; MJ_1231.
DR   GeneID; 1452127; -.
DR   KEGG; mja:MJ_1231; -.
DR   eggNOG; arCOG02095; Archaea.
DR   eggNOG; COG0511; LUCA.
DR   eggNOG; COG5016; LUCA.
DR   InParanoid; Q58628; -.
DR   KO; K01960; -.
DR   OMA; MSMTYGH; -.
DR   OrthoDB; 19729at2157; -.
DR   PhylomeDB; Q58628; -.
DR   BioCyc; MJAN243232:G1GKE-1336-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:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005776; OadA.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01108; oadA; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Biotin; Complete proteome; Direct protein sequencing;
KW   Gluconeogenesis; Ligase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Pyruvate;
KW   Reference proteome.
FT   CHAIN         1    567       Pyruvate carboxylase subunit B.
FT                                /FTId=PRO_0000146830.
FT   DOMAIN        2    262       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   DOMAIN      492    567       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   REGION       10     14       Substrate binding. {ECO:0000250}.
FT   METAL        11     11       Divalent metal cation. {ECO:0000250}.
FT   METAL       172    172       Divalent metal cation; via carbamate
FT                                group. {ECO:0000250}.
FT   METAL       201    201       Divalent metal cation. {ECO:0000250}.
FT   METAL       203    203       Divalent metal cation. {ECO:0000250}.
FT   BINDING      81     81       Substrate. {ECO:0000250}.
FT   BINDING     337    337       Substrate. {ECO:0000250}.
FT   MOD_RES     172    172       N6-carboxylysine. {ECO:0000250}.
FT   MOD_RES     533    533       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   567 AA;  63908 MW;  5E07800622545628 CRC64;
     MVKIVDTTFR DAQQSLIATR MRTEDMLPIA EKMDEVGFYS MEVWGGATFD ACIRYLNEDP
     WERLRALKKR IQNTPLQMLL RGQNLVGYRH YPDDIVEKFV IKAHENGIDI FRIFDALNDV
     RNMETAIKTA KKVGAEVQGA ICYTISPVHT IDQYVELAKK LEEMGCDSIC IKDMAGLLTP
     YEGYELVKRL KEEISLPIDV HSHCTSGLAP MTYLKVIEAG ADMVDCAISP FAMGTSQPPT
     ESIVVALKGT KYDTGLDLKL LNEIRDYFMK VREKYKMLFS PISQIVDARV LVYQVPGGML
     SNLVSQLKEQ GALDKFEEVL QEIPRVRKDL GYPPLVTPTS QIVGTQAVLN VLTEERYKII
     TNEVVNYVKG FYGKPPAPIN PELLKRVLDE GEKPITCRPA DLLPPEWEKV KKEAEEKGIV
     KKEEDILTYA LYPQIAVKFL RGELKAEPIP KEKDIGKILE IPTEYIVEVD GEKFEVKIEP
     KIGTELKRKK EVITAEMEGA VTSPFRGMVT KIKVKEGDKV KKGDVIVVLE AMKMEHPIES
     PVEGTVERIL IDEGDAVNVG DVIMIIK
//
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