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 03-AUG-2022, entry version 145.
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; 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 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; 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; 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
