G6PI_VIBA3
ID G6PI_VIBA3 Reviewed; 550 AA.
AC B7VI73;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=VS_0288;
OS Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=575788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LGP32;
RA Mazel D., Le Roux F.;
RT "Vibrio splendidus str. LGP32 complete genome.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; FM954972; CAV17310.1; -; Genomic_DNA.
DR RefSeq; WP_009847896.1; NC_011753.2.
DR AlphaFoldDB; B7VI73; -.
DR SMR; B7VI73; -.
DR STRING; 575788.VS_0288; -.
DR EnsemblBacteria; CAV17310; CAV17310; VS_0288.
DR KEGG; vsp:VS_0288; -.
DR PATRIC; fig|575788.5.peg.1667; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_6; -.
DR OMA; IGVWYIN; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000009100; Chromosome 1.
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 Gene3D; 1.10.1390.10; -; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR023096; G6P_Isomerase_C.
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; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..550
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000135541"
FT ACT_SITE 356
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 387
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 515
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 550 AA; 60970 MW; 759BB6F4C6BD6643 CRC64;
MLKNINPTQT QAWKALTAHF ESAQDMDMKE LFAQDAKRFE SFSTRFGSDI LVDYSKNLID
AETMQHLFAL ANETEVKSAI EAMFGGDAIN KTEGRSVLHT ALRNRSDKPV MVDGKDVMPA
VNAVLAKMEL FTHRIVSGEW KGYTGKEITD VVNIGIGGSD LGPYMVTEAL TPYKTRLNMH
FVSNVDGTHI VETLKPLNPE TTLFLVASKT FTTQETMTNA HSARDWFLAE AGDSAHVAKH
FAALSTNAAS VAEFGIDTDN MFEFWDWVGG RYSLWSAIGL SISLSIGFDN FAELLDGAHE
MDNHFASTEF ESNIPVILAL IGVWYNNFHG AESEAILPYD QYMHRFAAYF QQGNMESNGK
FVDREGNPVE YQTGPIIWGE PGTNGQHAFY QLIHQGTKLI PSDFIAPAIS HNPASDHHQK
LMSNFFAQTE ALAFGKTKET VEAEFLAAGK TAEEVAELVP FKVFEGNRPT NSILVKQINP
RSLGNLIAMY EHKIFVQGVI WNIFSFDQWG VELGKQLANQ ILPELADDAQ VTSHDSSTNG
LINAFKALKA