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PCKG_CHLMU
ID   PCKG_CHLMU              Reviewed;         599 AA.
AC   Q9PLL6;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=TC_0083;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF73531.1; -; Genomic_DNA.
DR   RefSeq; WP_010229325.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PLL6; -.
DR   SMR; Q9PLL6; -.
DR   STRING; 243161.TC_0083; -.
DR   EnsemblBacteria; AAF73531; AAF73531; TC_0083.
DR   GeneID; 1245613; -.
DR   KEGG; cmu:TC_0083; -.
DR   eggNOG; COG1274; Bacteria.
DR   HOGENOM; CLU_028872_1_1_0; -.
DR   OMA; GPTNNWV; -.
DR   OrthoDB; 267285at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000800; 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..599
FT                   /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT                   /id="PRO_0000103597"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         216..218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         225
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         268..273
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         292
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         381..383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         383
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         414
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         507..510
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
SQ   SEQUENCE   599 AA;  66438 MW;  27E9983EF9227854 CRC64;
     MTGDWMSKIT HSGLKSWIEE VIALVSPKDV RLCDGSEAEY QQLCQQMQEA GVMTLLNPEL
     HPNCFLVRSS PDDVARVEQF TFICTKTKEE AGPTNNWRDP QEMRAELHEL FQGCMQGRTL
     YIVPFCMGPL HSPFSLVGIE ITDSPYVVCS MKIMTRMGAS VLEMLGSSGT FYKCLHSVGK
     PLAPGEKDVA WPCNPGHMRI VHFQDDSSVM SFGSGYGGNA LLGKKCVALR LASYLGHKQG
     WLAEHMLVIG VTNPEGRKKY FAAAFPSACG KTNLAMLMPK LPGWKVECIG DDIAWIRPGD
     DGRLYAVNPE FGFFGVAIGT SEKTNPNALA TCHSDSIFTN VALTSDGDVW WEGKTATPPQ
     GMIDWKGRNW TPGGEPAAHP NARFTAPLDH CPSLDPQWDS PQGVPLEAII FGGRRTETIP
     LVYESLSWEH GVMMGAGMSS TTTAAIAGEL GKLRHDPFAM LPFCGYNMAA YFEHWLSFAG
     KGLQLPRIFS VNWFRKDENG QFIWPGFSEN LRVLEWIFRR TDGEDSIARR TPIGYLPTEE
     GLNTTGLNLS RDALQSLLAV DTQGWRAEVN NIREYCSIFG SDMPRQILEE LSRIENELK
 
 
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