PYCB_METTH
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 03-AUG-2022, entry version 130.
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 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium 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., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT 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 characterization
RT of pyruvate carboxylase from Methanobacterium thermoautotrophicum strain
RT deltaH.";
RL J. Biol. Chem. 273:5155-5166(1998).
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.
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 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.
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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 AlphaFoldDB; O27179; -.
DR SMR; O27179; -.
DR STRING; 187420.MTH_1107; -.
DR PRIDE; O27179; -.
DR EnsemblBacteria; AAB85596; AAB85596; MTH_1107.
DR GeneID; 24854231; -.
DR KEGG; mth:MTH_1107; -.
DR PATRIC; fig|187420.15.peg.1083; -.
DR HOGENOM; CLU_000395_4_2_2; -.
DR OMA; GYHALEM; -.
DR BioCyc; MetaCyc:MON-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; Direct protein sequencing; Gluconeogenesis; Ligase;
KW Magnesium; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Pyruvate; Reference proteome.
FT CHAIN 1..568
FT /note="Pyruvate carboxylase subunit B"
FT /id="PRO_0000146831"
FT DOMAIN 4..264
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT DOMAIN 493..568
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT BINDING 12..16
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /note="via carbamate group"
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 205
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 174
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 534
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT 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
