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Database: UniProt
Entry: PYC_SCHPO
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Original site: PYC_SCHPO 
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   27-MAR-2024, entry version 151.
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; Schizosaccharomycetaceae;
OC   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 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., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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. {ECO:0000250}.
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; 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}.
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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   AlphaFoldDB; Q9UUE1; -.
DR   SMR; Q9UUE1; -.
DR   BioGRID; 276216; 3.
DR   STRING; 284812.Q9UUE1; -.
DR   iPTMnet; Q9UUE1; -.
DR   MaxQB; Q9UUE1; -.
DR   PaxDb; 4896-SPBC17G9-11c-1; -.
DR   EnsemblFungi; SPBC17G9.11c.1; SPBC17G9.11c.1:pep; SPBC17G9.11c.
DR   GeneID; 2539661; -.
DR   KEGG; spo:SPBC17G9.11c; -.
DR   PomBase; SPBC17G9.11c; pyr1.
DR   VEuPathDB; FungiDB:SPBC17G9.11c; -.
DR   eggNOG; KOG0369; Eukaryota.
DR   HOGENOM; CLU_000395_0_1_1; -.
DR   InParanoid; Q9UUE1; -.
DR   OMA; YAIQSRV; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IBA:GO_Central.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:PomBase.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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   NCBIfam; TIGR01235; pyruv_carbox; 1.
DR   PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
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; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 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; Cytoplasm; Gluconeogenesis; Ligase; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome; Zinc.
FT   CHAIN           1..1185
FT                   /note="Pyruvate carboxylase"
FT                   /id="PRO_0000146823"
FT   DOMAIN          32..484
FT                   /note="Biotin carboxylation"
FT   DOMAIN          154..351
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          570..838
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   DOMAIN          1108..1183
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   ACT_SITE        326
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         578..582
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         579
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         651
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         747
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         777
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         779
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         912
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         747
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1149
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
FT   CONFLICT        68
FT                   /note="R -> I (in Ref. 1; BAA11239)"
FT                   /evidence="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
//
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