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G6PI_THET8
ID   G6PI_THET8              Reviewed;         415 AA.
AC   Q5SLL6;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE            EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE            Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN   Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=TTHA0277;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of hypothetical protein TT0277 from Thermus thermophilus
RT   HB8.";
RL   Submitted (JUN-2006) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC       to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC         Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC         EC=5.3.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00473};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00473}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000255|HAMAP-Rule:MF_00473}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00473}.
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DR   EMBL; AP008226; BAD70100.1; -; Genomic_DNA.
DR   RefSeq; WP_011227825.1; NC_006461.1.
DR   RefSeq; YP_143543.1; NC_006461.1.
DR   PDB; 1ZZG; X-ray; 1.95 A; A/B=1-415.
DR   PDBsum; 1ZZG; -.
DR   AlphaFoldDB; Q5SLL6; -.
DR   SMR; Q5SLL6; -.
DR   STRING; 300852.55771659; -.
DR   EnsemblBacteria; BAD70100; BAD70100; BAD70100.
DR   GeneID; 3168044; -.
DR   KEGG; ttj:TTHA0277; -.
DR   PATRIC; fig|300852.9.peg.277; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_037303_1_0_0; -.
DR   OMA; IGVWYIN; -.
DR   PhylomeDB; Q5SLL6; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   EvolutionaryTrace; Q5SLL6; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd05015; SIS_PGI_1; 1.
DR   CDD; cd05016; SIS_PGI_2; 1.
DR   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR035476; SIS_PGI_1.
DR   InterPro; IPR035482; SIS_PGI_2.
DR   PANTHER; PTHR11469; PTHR11469; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR   PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW   Reference proteome.
FT   CHAIN           1..415
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180759"
FT   ACT_SITE        267
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        406
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           12..18
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           20..32
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           52..61
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           79..88
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          94..98
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           103..112
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          118..127
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           130..147
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           148..154
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          155..159
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          161..164
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           165..173
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          176..179
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           193..201
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           206..221
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           224..226
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           228..238
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   TURN            239..241
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          242..249
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   TURN            253..256
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           257..269
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          270..272
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          282..287
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           290..292
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   TURN            293..295
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           296..301
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          306..314
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           329..331
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   TURN            332..336
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           339..356
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   STRAND          360..370
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           371..391
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           400..402
FT                   /evidence="ECO:0007829|PDB:1ZZG"
FT   HELIX           403..414
FT                   /evidence="ECO:0007829|PDB:1ZZG"
SQ   SEQUENCE   415 AA;  46081 MW;  A8C23A5C2E3EFC56 CRC64;
     MLRLDTRFLP GFPEALSRHG PLLEEARRRL LAKRGEPGSM LGWMDLPEDT ETLREVRRYR
     EANPWVEDFV LIGIGGSALG PKALEAAFNE SGVRFHYLDH VEPEPILRLL RTLDPRKTLV
     NAVSKSGSTA ETLAGLAVFL KWLKAHLGED WRRHLVVTTD PKEGPLRAFA EREGLKAFAI
     PKEVGGRFSA LSPVGLLPLA FAGADLDALL MGARKANETA LAPLEESLPL KTALLLHLHR
     HLPVHVFMVY SERLSHLPSW FVQLHDESLG KVDRQGQRVG TTAVPALGPK DQHAQVQLFR
     EGPLDKLLAL VIPEAPLEDV EIPEVEGLEA ASYLFGKTLF QLLKAEAEAT YEALAEAGQR
     VYALFLPEVS PYAVGWLMQH LMWQTAFLGE LWEVNAFDQP GVELGKVLTR KRLAG
 
 
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