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PCKG_BORA1
ID   PCKG_BORA1              Reviewed;         621 AA.
AC   Q2L1L0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=BAV1626;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ49235.1; -; Genomic_DNA.
DR   RefSeq; WP_012417297.1; NC_010645.1.
DR   AlphaFoldDB; Q2L1L0; -.
DR   SMR; Q2L1L0; -.
DR   STRING; 360910.BAV1626; -.
DR   PRIDE; Q2L1L0; -.
DR   EnsemblBacteria; CAJ49235; CAJ49235; BAV1626.
DR   GeneID; 41393480; -.
DR   KEGG; bav:BAV1626; -.
DR   eggNOG; COG1274; Bacteria.
DR   HOGENOM; CLU_028872_1_1_4; -.
DR   OMA; GPTNNWV; -.
DR   OrthoDB; 267285at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001977; 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; Reference proteome.
FT   CHAIN           1..621
FT                   /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT                   /id="PRO_1000060287"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         224..226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         233
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         253
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         276..281
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         302
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         396..398
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         398
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         429
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         526..529
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
SQ   SEQUENCE   621 AA;  67910 MW;  70C191E3B587F43F CRC64;
     MTQAAEATLP PLNVPSYVKH ARLIDWVQGV VALTKPARVV WCDGSQEEAD RLCEQMVQAG
     TMRRLNPAKR PNSYLAWSDP SDVARVEDRT FICSQREEDA GPTNNWAAPA EMRNTLQGLF
     DGAMRGRTLY VVPFSMGPLG SPIAHIGVEL SDSPYVAVNM RIMTRMGRAV WDVLGADGEF
     VPCVHSVGMP LAEGQADVAW PCNPVKYIVH YPETREIWSF GSGYGGNALL GKKCFALRIA
     STMGRDEGWL AEHMLILGVT TPKGRKFHVA AAFPSACGKT NFAMLIPPSG MDGWKVSTIG
     DDIAWIKPGQ DGRLRAINPE AGYFGVAPGT SEKTNPNAMA TLKANVIFTN VALTDDGDVW
     WEGMTDTPPA HLIDWQGKDW TPEIARETGR KAAHPNARFT APASQCPSID PEWENPQGVA
     IDAFIFGGRR STTIPLVTEA RDWVQGVYMA ATMGSETTAA AVGQQGVVRR DPFAMLPFCG
     YNMADYFNHW LAVGQRLADA GATLPRIYCV NWFRKGPNGK FVWPGFGENM RVLKWMLGRL
     SGEAGGQEQV FGISPSYGDV DWTGLEFTPD QFQQVISVEA PAWREELALH GELFEQLAQG
     LPPALSRAKA DIEHRLAAVQ A
 
 
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