PYC_BACSU
ID PYC_BACSU Reviewed; 1148 AA.
AC Q9KWU4; O07640; Q9KWU5;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Pyruvate carboxylase;
DE EC=6.4.1.1;
DE AltName: Full=Pyruvic carboxylase;
DE Short=PYC;
GN Name=pyc; Synonyms=pycA, ylaP; OrderedLocusNames=BSU14860;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 229-1148.
RC STRAIN=168;
RA Bertero M., Presecan E., Glaser P., Richou A., Danchin A.;
RT "Bacillus subtilis chromosomal region downstream nprE.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=4146915; DOI=10.1016/s0021-9258(19)43509-6;
RA Diesterhaft M.D., Freese E.;
RT "Role of pyruvate carboxylase, phosphoenolpyruvate carboxykinase, and malic
RT enzyme during growth and sporulation of Bacillus subtilis.";
RL J. Biol. Chem. 248:6062-6070(1973).
CC -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC carboxylation of the covalently attached biotin in the first step and
CC the transfer of the carboxyl group to pyruvate in the second, leading
CC to oxaloacetate production. Fulfills an anaplerotic function in
CC B.subtilis as it is necessary for growth on glucose, but is not
CC required for sporulation. {ECO:0000269|PubMed:4146915}.
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=biotin; Xref=ChEBI:CHEBI:57586;
CC -!- ACTIVITY REGULATION: Allosterically activated by acetyl-CoA. Inhibited
CC by the biotin-complexing protein avidin.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB09721.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL009126; CAB13359.1; -; Genomic_DNA.
DR EMBL; Z97025; CAB09721.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z98682; CAB11339.1; -; Genomic_DNA.
DR PIR; F69685; F69685.
DR RefSeq; NP_389369.1; NC_000964.3.
DR RefSeq; WP_003244778.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; Q9KWU4; -.
DR SMR; Q9KWU4; -.
DR STRING; 224308.BSU14860; -.
DR jPOST; Q9KWU4; -.
DR PaxDb; Q9KWU4; -.
DR PRIDE; Q9KWU4; -.
DR EnsemblBacteria; CAB13359; CAB13359; BSU_14860.
DR GeneID; 935920; -.
DR KEGG; bsu:BSU14860; -.
DR PATRIC; fig|224308.179.peg.1620; -.
DR eggNOG; COG1038; Bacteria.
DR InParanoid; Q9KWU4; -.
DR OMA; YAIQSRV; -.
DR PhylomeDB; Q9KWU4; -.
DR BioCyc; BSUB:BSU14860-MON; -.
DR PRO; PR:Q9KWU4; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR005930; Pyruv_COase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01235; pyruv_carbox; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW ATP-binding; Biotin; Ligase; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..1148
FT /note="Pyruvate carboxylase"
FT /id="PRO_0000146826"
FT DOMAIN 1..457
FT /note="Biotin carboxylation"
FT DOMAIN 125..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 534..802
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT DOMAIN 1071..1146
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT ACT_SITE 242
FT /evidence="ECO:0000255"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 542..546
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 615
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 712
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 741
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 743
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 876
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 234
FT /note="Involved in CO(2) fixation"
FT /evidence="ECO:0000255"
FT MOD_RES 712
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 1112
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
SQ SEQUENCE 1148 AA; 127937 MW; 98D14DD56F361620 CRC64;
MSQQSIQKVL VANRGEIAIR IFRACTELNI RTVAVYSKED SGSYHRYKAD EAYLVGEGKK
PIDAYLDIEG IIDIAKRNKV DAIHPGYGFL SENIHFARRC EEEGIVFIGP KSEHLDMFGD
KVKAREQAEK AGIPVIPGSD GPAETLEAVE QFGQANGYPI IIKASLGGGG RGMRIVRSES
EVKEAYERAK SEAKAAFGND EVYVEKLIEN PKHIEVQVIG DKQGNVVHLF ERDCSVQRRH
QKVIEVAPSV SLSPELRDQI CEAAVALAKN VNYINAGTVE FLVANNEFYF IEVNPRVQVE
HTITEMITGV DIVQTQILVA QGHSLHSKKV NIPEQKDIFT IGYAIQSRVT TEDPQNDFMP
DTGKIMAYRS GGGFGVRLDT GNSFQGAVIT PYYDSLLVKL STWALTFEQA AAKMVRNLQE
FRIRGIKTNI PFLENVAKHE KFLTGQYDTS FIDTTPELFN FPKQKDRGTK MLTYIGNVTV
NGFPGIGKKE KPAFDKPLGV KVDVDQQPAR GTKQILDEKG AEGLANWVKE QKSVLLTDTT
FRDAHQSLLA TRIRSHDLKK IANPTAALWP ELFSMEMWGG ATFDVAYRFL KEDPWKRLED
LRKEVPNTLF QMLLRSSNAV GYTNYPDNVI KEFVKQSAQS GIDVFRIFDS LNWVKGMTLA
IDAVRDTGKV AEAAICYTGD ILDKNRTKYD LAYYTSMAKE LEAAGAHILG IKDMAGLLKP
QAAYELVSAL KETIDIPVHL HTHDTSGNGI YMYAKAVEAG VDIIDVAVSS MAGLTSQPSA
SGFYHAMEGN DRRPEMNVQG VELLSQYWES VRKYYSEFES GMKSPHTEIY EHEMPGGQYS
NLQQQAKGVG LGDRWNEVKE MYRRVNDMFG DIVKVTPSSK VVGDMALYMV QNNLTEKDVY
EKGESLDFPD SVVELFKGNI GQPHGGFPEK LQKLILKGQE PITVRPGELL EPVSFEAIKQ
EFKEQHNLEI SDQDAVAYAL YPKVFTDYVK TTESYGDISV LDTPTFFYGM TLGEEIEVEI
ERGKTLIVKL ISIGEPQPDA TRVVYFELNG QPREVVIKDE SIKSSVQERL KADRTNPSHI
AASMPGTVIK VLAEAGTKVN KGDHLMINEA MKMETTVQAP FSGTIKQVHV KNGEPIQTGD
LLLEIEKA
