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Database: UniProt
Entry: Q9KWU4
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Original site: Q9KWU4 
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   10-APR-2019, entry version 120.
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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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;
RA   Diesterhaft M.D., Freese E.;
RT   "Role of pyruvate carboxylase, phosphoenolpyruvate carboxykinase, and
RT   malic 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
CC       and the transfer of the carboxyl group to pyruvate in the second,
CC       leading to oxaloacetate production. Fulfills an anaplerotic
CC       function in B.subtilis as it is necessary for growth on glucose,
CC       but is not required for sporulation. {ECO:0000269|PubMed:4146915}.
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=biotin; Xref=ChEBI:CHEBI:57586;
CC   -!- ACTIVITY REGULATION: Allosterically activated by acetyl-CoA.
CC       Inhibited 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; Positions=369; Evidence={ECO:0000305};
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   ProteinModelPortal; Q9KWU4; -.
DR   SMR; Q9KWU4; -.
DR   STRING; 224308.BSU14860; -.
DR   jPOST; Q9KWU4; -.
DR   PaxDb; Q9KWU4; -.
DR   PRIDE; Q9KWU4; -.
DR   EnsemblBacteria; CAB13359; CAB13359; BSU14860.
DR   GeneID; 935920; -.
DR   KEGG; bsu:BSU14860; -.
DR   PATRIC; fig|224308.179.peg.1620; -.
DR   eggNOG; ENOG4108JIJ; Bacteria.
DR   eggNOG; COG1038; LUCA.
DR   HOGENOM; HOG000282801; -.
DR   InParanoid; Q9KWU4; -.
DR   KO; K01958; -.
DR   OMA; GQPHGGF; -.
DR   PhylomeDB; Q9KWU4; -.
DR   BioCyc; BSUB:BSU14860-MONOMER; -.
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:0009374; F:biotin binding; IEA:InterPro.
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; Complete proteome; Ligase; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome.
FT   CHAIN         1   1148       Pyruvate carboxylase.
FT                                /FTId=PRO_0000146826.
FT   DOMAIN        1    457       Biotin carboxylation.
FT   DOMAIN      125    321       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      534    802       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   DOMAIN     1071   1146       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   REGION      542    546       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    242    242       {ECO:0000255}.
FT   METAL       543    543       Divalent metal cation. {ECO:0000250}.
FT   METAL       712    712       Divalent metal cation; via carbamate
FT                                group. {ECO:0000250}.
FT   METAL       741    741       Divalent metal cation. {ECO:0000250}.
FT   METAL       743    743       Divalent metal cation. {ECO:0000250}.
FT   BINDING     121    121       ATP. {ECO:0000250}.
FT   BINDING     205    205       ATP. {ECO:0000250}.
FT   BINDING     240    240       ATP. {ECO:0000250}.
FT   BINDING     615    615       Substrate. {ECO:0000250}.
FT   BINDING     876    876       Substrate. {ECO:0000250}.
FT   SITE        234    234       Involved in CO(2) fixation.
FT                                {ECO:0000255}.
FT   MOD_RES     712    712       N6-carboxylysine. {ECO:0000250}.
FT   MOD_RES    1112   1112       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-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
//
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