PYCB_METJA
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 03-AUG-2022, entry version 136.
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 / 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 190-195; 260-270; 277-289; 277-289; 309-325; 328-358;
RP 370-380; 386-409; 422-438; 491-506 AND 491-506, FUNCTION, AND MASS
RP 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=64160; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11195096};
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DR EMBL; L77117; AAB99233.1; -; Genomic_DNA.
DR PIR; F64453; F64453.
DR RefSeq; WP_010870743.1; NC_000909.1.
DR AlphaFoldDB; Q58628; -.
DR SMR; Q58628; -.
DR STRING; 243232.MJ_1231; -.
DR PRIDE; Q58628; -.
DR EnsemblBacteria; AAB99233; AAB99233; MJ_1231.
DR GeneID; 1452127; -.
DR KEGG; mja:MJ_1231; -.
DR eggNOG; arCOG02095; Archaea.
DR HOGENOM; CLU_000395_4_2_2; -.
DR InParanoid; Q58628; -.
DR OMA; GYHALEM; -.
DR OrthoDB; 19729at2157; -.
DR PhylomeDB; Q58628; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; Direct protein sequencing; Gluconeogenesis; Ligase;
KW Magnesium; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Pyruvate; Reference proteome.
FT CHAIN 1..567
FT /note="Pyruvate carboxylase subunit B"
FT /id="PRO_0000146830"
FT DOMAIN 2..262
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT DOMAIN 492..567
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT BINDING 10..14
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 172
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 533
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT 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
