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PCKG_MYCLB
ID   PCKG_MYCLB              Reviewed;         609 AA.
AC   B8ZTI5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000255|HAMAP-Rule:MF_00452};
DE            Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452};
DE            Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00452};
DE            EC=4.1.1.32 {ECO:0000255|HAMAP-Rule:MF_00452};
GN   Name=pckG {ECO:0000255|HAMAP-Rule:MF_00452}; OrderedLocusNames=MLBr02624;
OS   Mycobacterium leprae (strain Br4923).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=561304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Br4923;
RX   PubMed=19881526; DOI=10.1038/ng.477;
RA   Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA   Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA   Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA   Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA   Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA   Rougemont J., Brennan P.J., Cole S.T.;
RT   "Comparative genomic and phylogeographic analysis of Mycobacterium
RT   leprae.";
RL   Nat. Genet. 41:1282-1289(2009).
CC   -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to
CC       phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC       pathway that produces glucose from lactate and other precursors derived
CC       from the citric acid cycle. {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00452};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00452};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00452};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family. {ECO:0000255|HAMAP-Rule:MF_00452}.
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DR   EMBL; FM211192; CAR72724.1; -; Genomic_DNA.
DR   RefSeq; WP_010909000.1; NC_011896.1.
DR   AlphaFoldDB; B8ZTI5; -.
DR   SMR; B8ZTI5; -.
DR   EnsemblBacteria; CAR72724; CAR72724; MLBr02624.
DR   KEGG; mlb:MLBr02624; -.
DR   HOGENOM; CLU_028872_1_1_11; -.
DR   OMA; GPTNNWV; -.
DR   OrthoDB; 267285at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000006900; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd00819; PEPCK_GTP; 1.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 1.
DR   HAMAP; MF_00452; PEPCK_GTP; 1.
DR   InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR   InterPro; IPR013035; PEP_carboxykinase_C.
DR   InterPro; IPR008209; PEP_carboxykinase_GTP.
DR   InterPro; IPR035077; PEP_carboxykinase_GTP_C.
DR   InterPro; IPR035078; PEP_carboxykinase_GTP_N.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
DR   PANTHER; PTHR11561; PTHR11561; 1.
DR   Pfam; PF00821; PEPCK_GTP; 1.
DR   Pfam; PF17297; PEPCK_N; 1.
DR   PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR   SUPFAM; SSF68923; SSF68923; 1.
DR   PROSITE; PS00505; PEPCK_GTP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese;
KW   Metal-binding; Nucleotide-binding.
FT   CHAIN           1..609
FT                   /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT                   /id="PRO_1000192345"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         220..222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         229
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         249
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         272..277
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         296
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         387..389
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         389
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         420
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         515..518
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
SQ   SEQUENCE   609 AA;  67732 MW;  8916B6733622590B CRC64;
     MTSATIPGLD TAPTNHQKLL SWLEEVAELT HPAQVVFADG SDEEWQQLTE RLVAAGTFKK
     LNDEKHPNSY LALSDPSDVA RVESRTFICS EREIDAGPTN NWMDPAEMRS TMTELYRGCM
     RGRTMWVVPF CMGPPGAEDP KLGVEITDSE YVVASMKVMT RMGTSALEKI GDDGFFVKAL
     HSVGAPLQPG QQDMPWPCNE TKYITHFPET REIWSYGSGY GGNALLGKKC YSLRIASAMA
     HDEGWLAEHM LILKLISPEN KAYYFAAAFP SACGKTNLAM LQPTIPGWRA ETLGDDIAWM
     RFGKDGRLYA VNPEFGFFGV APGTNWKSNP NAMRTIAAGN TVFTNVALTD DNDVWWEGLE
     GEPAHLIDWK GNDWYAGKTE TPAAHSNSRY CTPMSQCPIL APEWDDPRGV PISVILFGAR
     RKTTVPLVTQ ARNWQHGVFM GATMGSEQTA AAEGKVGTVR RDPMAMLPFM GYHVGDYFQH
     WIDLGKHSDE SNLPKVFFVN WFRRGEGGKF LWPGFGENSR VLKWIVDRIE HKAGGQDTLI
     GIVPTATDLD LDGLDISSDD VAKALAVDPA EWRNELPLIE EWFEFVGDKL PSGMQDEFEA
     LKQRLAKED
 
 
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