GenomeNet

Database: UniProt
Entry: Q9UUE1
LinkDB: Q9UUE1
Original site: Q9UUE1 
ID   PYC_SCHPO               Reviewed;        1185 AA.
AC   Q9UUE1; P78822;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 133.
DE   RecName: Full=Pyruvate carboxylase;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase;
DE            Short=PCB;
GN   Name=pyr1; ORFNames=SPBC17G9.11c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / HM123;
RA   Saito A., Kazuta Y., Toh H., Kondo H., Tanabe T.;
RT   "Biotin-dependent enzymes in Schizosaccharomyces pombe: cloning and
RT   nucleotide sequences of acetyl-CoA carboxylase and pyruvate
RT   carboxylase.";
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
DR   EMBL; D78170; BAA11239.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB52809.1; -; Genomic_DNA.
DR   PIR; T39734; T39734.
DR   RefSeq; NP_595900.1; NM_001021807.2.
DR   ProteinModelPortal; Q9UUE1; -.
DR   SMR; Q9UUE1; -.
DR   BioGrid; 276216; 1.
DR   STRING; 4896.SPBC17G9.11c.1; -.
DR   iPTMnet; Q9UUE1; -.
DR   MaxQB; Q9UUE1; -.
DR   PaxDb; Q9UUE1; -.
DR   PRIDE; Q9UUE1; -.
DR   EnsemblFungi; SPBC17G9.11c.1; SPBC17G9.11c.1:pep; SPBC17G9.11c.
DR   GeneID; 2539661; -.
DR   KEGG; spo:SPBC17G9.11c; -.
DR   EuPathDB; FungiDB:SPBC17G9.11c; -.
DR   PomBase; SPBC17G9.11c; pyr1.
DR   HOGENOM; HOG000282801; -.
DR   InParanoid; Q9UUE1; -.
DR   KO; K01958; -.
DR   OMA; GQPHGGF; -.
DR   PhylomeDB; Q9UUE1; -.
DR   Reactome; R-SPO-196780; Biotin transport and metabolism.
DR   Reactome; R-SPO-70263; Gluconeogenesis.
DR   UniPathway; UPA00138; -.
DR   PRO; PR:Q9UUE1; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
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; ISO:PomBase.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:PomBase.
DR   GO; GO:0006094; P:gluconeogenesis; ISO:PomBase.
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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Biotin; Complete proteome; Cytoplasm; Gluconeogenesis;
KW   Ligase; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Reference proteome; Zinc.
FT   CHAIN         1   1185       Pyruvate carboxylase.
FT                                /FTId=PRO_0000146823.
FT   DOMAIN       32    484       Biotin carboxylation.
FT   DOMAIN      154    351       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      570    838       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   DOMAIN     1108   1183       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   REGION      578    582       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    326    326       {ECO:0000250}.
FT   METAL       579    579       Divalent metal cation. {ECO:0000250}.
FT   METAL       747    747       Divalent metal cation; via carbamate
FT                                group. {ECO:0000250}.
FT   METAL       777    777       Divalent metal cation. {ECO:0000250}.
FT   METAL       779    779       Divalent metal cation. {ECO:0000250}.
FT   BINDING     150    150       ATP. {ECO:0000250}.
FT   BINDING     234    234       ATP. {ECO:0000250}.
FT   BINDING     269    269       ATP. {ECO:0000250}.
FT   BINDING     651    651       Substrate. {ECO:0000250}.
FT   BINDING     912    912       Substrate. {ECO:0000250}.
FT   MOD_RES     747    747       N6-carboxylysine. {ECO:0000250}.
FT   MOD_RES    1149   1149       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   CONFLICT     68     68       R -> I (in Ref. 1; BAA11239).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1185 AA;  130861 MW;  D39706DCD83915D9 CRC64;
     MTSKYDALLH NQSTNTNPFS KLQDRSSLLG EKFTKVLVAN RSEIAIRVFR TAHELSMHTV
     AIYSYEDRLS MHRQKADESY PIGKVGQYSP VGAYLAIDEI VSIAKRTGAN LVHPGYGFLS
     ENAEFARKVN EAGMQFVGPS PEVIDSLGDK TKARAIAIRC GVPVVPGTPG PVEHYEEAEA
     FVKEYGLPVI IKAAMGGGGR GMRVVRSADT LKESFERARS EALASFGDGT VFIERFLDKP
     KHIEIQLMAD KAGNVIHLHE RDCSVQRRHQ KVVEIAPAKD LDPKIRQALY DDAIKIAKEV
     KYCNAGTAEF LLDQKGRHYF IEINPRIQVE HTITEEITGV DIVSAQLHVA AGFTLPEIGL
     TQDKISTRGF AIQCRVTTED PNNGFAPDIG KIEVYRSAGG NGVRLDGANG FAGSVITPHY
     DSMLVKCTCH DATYEYTRRK MIRSLIEFRV RGVKTNIPFV LRLLMHDTFI QGNCWTTFID
     DTPELFQLYR SRNRAQKLLA YLGDLAVNGS SIKGQNGEPA LKSEIVMPVL LDSTGNQIDV
     SHPSEKGWRK LLLDNGPAAF AKAVRNHKRG LIMDTTWRDA HQSLLATRVR TIDLVNIAPY
     TSHALASAYS LEMWGGATFD VSMRFLHECP WDRLRRLRKL VPNIPFQMLL RGANGLCYSS
     LPDNVIYFFC EQAKKNGIDI FRVFDALNDV NNLSLGIDAA KRAGGVVEAT MCYSGDMLNP
     KKKYNLDYYV NLVDKMVEMG IHILGIKDMA GVMKPKAARL LISAIREKHP ELPIHVHTHD
     SAGTAVASMA AALEAGADVV DVATDSMSGL TSQPSFGAVL ASVDGTDKQL EFDNNQLREI
     DSYWAQMRLL YSPFESEIKG TDSDVYNHEI PGGQLTNLKF QATSLGLGTQ WAETKKAYIE
     ANKLLGDIIK VTPTSKVVGD LAQFMVQNKL SAEDVENRAT TLDFPASVLD FFQGLMGQPY
     GGFPEPLRTN VLKGRRQPLT DRPGKFLPAA DFDAIRKLLS EKFGVSSDCD IAAYTQFPGV
     FEEYRQFVDR YGDLTTVPTK FFLSRPEMNE EMHVEIDQGK TLIVKFVALG PLNPRTGQRE
     VYFELNGENR HVTVEDKKAA IETVTRPRAD PGNPGHVAAP MSGTIVEIRV KEGAKVKKGD
     IIAVLSAMKM EIVISAPHSG VLKSLAVVQG DSVNGGDLCA VLEHE
//
DBGET integrated database retrieval system