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GPI_SINMW
ID   GPI_SINMW               Reviewed;         214 AA.
AC   A6UCB5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01410};
DE            Short=GPI {ECO:0000255|HAMAP-Rule:MF_01410};
DE            EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_01410};
DE   AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_01410};
DE            Short=PGI {ECO:0000255|HAMAP-Rule:MF_01410};
DE   AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_01410};
DE            Short=PHI {ECO:0000255|HAMAP-Rule:MF_01410};
GN   Name=pgiA {ECO:0000255|HAMAP-Rule:MF_01410}; OrderedLocusNames=Smed_2463;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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_01410};
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_01410}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01410}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01410}.
CC   -!- SIMILARITY: Belongs to the archaeal-type GPI family.
CC       {ECO:0000255|HAMAP-Rule:MF_01410}.
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DR   EMBL; CP000738; ABR61295.1; -; Genomic_DNA.
DR   RefSeq; WP_012066686.1; NC_009636.1.
DR   RefSeq; YP_001328130.1; NC_009636.1.
DR   AlphaFoldDB; A6UCB5; -.
DR   SMR; A6UCB5; -.
DR   STRING; 366394.Smed_2463; -.
DR   EnsemblBacteria; ABR61295; ABR61295; Smed_2463.
DR   GeneID; 61611297; -.
DR   KEGG; smd:Smed_2463; -.
DR   PATRIC; fig|366394.8.peg.5649; -.
DR   eggNOG; COG2140; Bacteria.
DR   HOGENOM; CLU_105797_0_0_5; -.
DR   OMA; YPADAGH; -.
DR   OrthoDB; 1276228at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000001108; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_01410; G6P_isomerase_arch; 1.
DR   InterPro; IPR016758; G6P_isomerase_archaea/bacteria.
DR   InterPro; IPR010551; G6P_isomerase_prok.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF06560; GPI; 1.
DR   PIRSF; PIRSF019325; Glucose-6-phosphate_isomerase; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Iron; Isomerase; Metal-binding.
FT   CHAIN           1..214
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_1000068451"
FT   BINDING         92
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01410"
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01410"
FT   BINDING         101
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01410"
FT   BINDING         140
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01410"
SQ   SEQUENCE   214 AA;  23911 MW;  6A2E7CA62D19768B CRC64;
     MTKLFEPAAC QVDLRTGAMS AATGAYQKRF RDLAGLYADE AAFSAMRENW NDTVVYEVSE
     FRPNERSGDL IFGTTRMLPG KVGDEYFVTR GHIHRQSDRP EIYYGQKGSG LMLLESPEGE
     VRIVAIDART VCYVPPYWIH RSVNIGGEEL VMLFCYPADS GQDYDCIAKA GGMRVRIVDD
     GEGGWKQVDN SSWRKRDAAT IAALYGLEKK EKSA
 
 
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