ID PYCA_METTH Reviewed; 491 AA.
AC O27939;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 151.
DE RecName: Full=Pyruvate carboxylase subunit A;
DE EC=6.4.1.1;
DE AltName: Full=Pyruvic carboxylase A;
GN Name=pycA; OrderedLocusNames=MTH_1917;
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 1-17.
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 -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Heterooctamer of four A and four B subunits.
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DR EMBL; AE000666; AAB86377.1; -; Genomic_DNA.
DR PIR; A69123; A69123.
DR RefSeq; WP_010877513.1; NC_000916.1.
DR AlphaFoldDB; O27939; -.
DR SMR; O27939; -.
DR STRING; 187420.MTH_1917; -.
DR PaxDb; 187420-MTH_1917; -.
DR EnsemblBacteria; AAB86377; AAB86377; MTH_1917.
DR GeneID; 77404306; -.
DR KEGG; mth:MTH_1917; -.
DR PATRIC; fig|187420.15.peg.1873; -.
DR HOGENOM; CLU_000395_3_2_2; -.
DR InParanoid; O27939; -.
DR BioCyc; MetaCyc:MONOMER-14537; -.
DR UniPathway; UPA00138; -.
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:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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 NCBIfam; TIGR00514; accC; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 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; Direct protein sequencing; Gluconeogenesis; Ligase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding; Pyruvate;
KW Reference proteome.
FT CHAIN 1..491
FT /note="Pyruvate carboxylase subunit A"
FT /id="PRO_0000146829"
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT ACT_SITE 291
FT /evidence="ECO:0000255"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 491 AA; 54657 MW; 5789C34DA7475C2E CRC64;
MFSKILVANR GEIAIRVMRA CRELGIKSVA VYSEADKNAL FTRYADEAYE IGKPAPSQSY
LRIDRILEVA EKAGAEAIHP GYGFLAENPR LGEECEKQGI KLIGPKGSVI EAMGDKITSK
KLMKKAGVPV IPGTDQGVSD PDEAARIADS IGYPVIIKAS AGGGGIGMRA VYEEDELIRA
MESTQSVAAS AFGDPTVYIE KYLERPRHIE FQVMADESGN VIHLADRECS IQRRHQKLIE
EAPSPIMTPE LRERMGSAAV KAAEYIGYEN AGTVEFLYSN GDFYFLEMNT RIQVEHPITE
VITGVDLVKE QIRVASGEEL RFTQKDINIR GHAIECRINA ENPLADFAPN PGKITGYRSP
GGIGVRVDSG VYMNYEIPPF YDSMISKLIV WGMDRQEAIN RMKRALSEYI ILGVKTTIPF
HKAIMRNEAF RRGELHTHFV DEYRRGIDAE MRKIVKEDQE MVERLQSTFL PSKKVAAISA
AIGTYMHSRR G
//
