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Database: UniProt
Entry: O27179
LinkDB: O27179
Original site: O27179 
ID   PYCB_METTH              Reviewed;         568 AA.
AC   O27179;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   10-APR-2019, entry version 120.
DE   RecName: Full=Pyruvate carboxylase subunit B;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase B;
GN   Name=pycB; OrderedLocusNames=MTH_1107;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 /
OS   JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K.,
RA   Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA   Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA   Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA   McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA   Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum
RT   deltaH: functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9478969; DOI=10.1074/jbc.273.9.5155;
RA   Mukhopadhyay B., Stoddard S.F., Wolfe R.S.;
RT   "Purification, regulation, and molecular and biochemical
RT   characterization of pyruvate carboxylase from Methanobacterium
RT   thermoautotrophicum strain deltaH.";
RL   J. Biol. Chem. 273:5155-5166(1998).
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.
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 ADP and alpha-ketoglutarate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.;
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.;
CC   -!- SUBUNIT: Heterooctamer of four A and four B subunits.
DR   EMBL; AE000666; AAB85596.1; -; Genomic_DNA.
DR   EMBL; AF039105; AAC12719.1; -; Genomic_DNA.
DR   PIR; C69014; C69014.
DR   RefSeq; WP_010876731.1; NC_000916.1.
DR   ProteinModelPortal; O27179; -.
DR   SMR; O27179; -.
DR   EnsemblBacteria; AAB85596; AAB85596; MTH_1107.
DR   GeneID; 24854231; -.
DR   KEGG; mth:MTH_1107; -.
DR   PATRIC; fig|187420.15.peg.1083; -.
DR   eggNOG; arCOG02095; Archaea.
DR   eggNOG; COG0511; LUCA.
DR   eggNOG; COG5016; LUCA.
DR   KO; K01960; -.
DR   OMA; MSMTYGH; -.
DR   OrthoDB; 19729at2157; -.
DR   BioCyc; MetaCyc:MONOMER-14538; -.
DR   Proteomes; UP000005223; 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-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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; 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    568       Pyruvate carboxylase subunit B.
FT                                /FTId=PRO_0000146831.
FT   DOMAIN        4    264       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   DOMAIN      493    568       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   REGION       12     16       Substrate binding. {ECO:0000250}.
FT   METAL        13     13       Divalent metal cation. {ECO:0000250}.
FT   METAL       174    174       Divalent metal cation; via carbamate
FT                                group. {ECO:0000250}.
FT   METAL       203    203       Divalent metal cation. {ECO:0000250}.
FT   METAL       205    205       Divalent metal cation. {ECO:0000250}.
FT   BINDING      83     83       Substrate. {ECO:0000250}.
FT   BINDING     339    339       Substrate. {ECO:0000250}.
FT   MOD_RES     174    174       N6-carboxylysine. {ECO:0000250}.
FT   MOD_RES     534    534       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   568 AA;  63955 MW;  D328715AB0328DBB CRC64;
     MKGIKVVETA FRDAHQSLLA TRLRTRDMTP IAEEMDRVGF FSLEAWGGAT FDTCIRYLNE
     DPWERLRELK EHVKRTPIQM LLRGQNLVGY KHYPDDIVRK FIEKSYENGV DVFRIFDALN
     DIRNMEYAIK VAREQEAHVQ GVICYTISPY HTLESYVDFA RELEALECDS VAIKDMAGLI
     SPHDAYELVR ALKEETDLMV NLHCHCTSGM TPMSYYAACE AGVDILDTAI SPLSWGASQP
     PTESIVAALR DTPYDTGLDL EILKNIKKYF EEIRKKYSSI LDPIAEQIDT DVLIYQIPGG
     MLSNLVAQLK EQNALDRYEE VLEEMPRVRK DMGYPPLVTP TSQIVGIQAV MNVLSGERYS
     MVTNEVKDYF RGLYGRPPAP LNEEVARKVI GDEKPIDCRP ADILKPQYDE CRRKGEEMGI
     IEKEEDILTL ALYPAIAPKF LRGEIEEEPL EPPAEEMAPT GEVPTVFHVE VDGDEFEVKV
     VPTGYMTIEE AEPEPVDVEG AVKSTMQGMV VKLKVSEGDQ VNAGDVVAVV EAMKMENDIQ
     TPHGGVVEKI YTAEGEKVET GDIIMVIK
//
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