ID G2Z413_FLABF Unreviewed; 547 AA.
AC G2Z413;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000256|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000256|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000256|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000256|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000256|HAMAP-Rule:MF_00473,
GN ECO:0000313|EMBL:CCB68348.1};
GN OrderedLocusNames=FBFL15_0198 {ECO:0000313|EMBL:CCB68348.1};
OS Flavobacterium branchiophilum (strain FL-15).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1034807 {ECO:0000313|EMBL:CCB68348.1, ECO:0000313|Proteomes:UP000009186};
RN [1] {ECO:0000313|EMBL:CCB68348.1, ECO:0000313|Proteomes:UP000009186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FL-15 {ECO:0000313|EMBL:CCB68348.1,
RC ECO:0000313|Proteomes:UP000009186};
RX PubMed=21926215; DOI=10.1128/AEM.05625-11;
RG 1:IP;
RG Microbial Evolutionary Genomics,F-75015 Paris;
RG France 2:CNRS;
RG URA2171;
RG F-75015 Paris,France 3:Unite de Virologie et Immunologie Mol.;
RG INRA,78352 Jouy en Josas Cedex;
RG France. 4:Unite de Mathemathique;
RG Informatique et Genome,INRA;
RG 78352 Jouy en Josas Cedex;
RG France. 5:CEA/Genoscope;
RG Evry;
RG France;
RA Touchon M., Barbier P., Bernardet J.F., Loux V., Vacherie B., Barbe V.,
RA Rocha E.P., Duchaud E.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT branchiophilum.";
RL Appl. Environ. Microbiol. 77:7656-7662(2011).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000256|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:0000256|ARBA:ARBA00029321,
CC ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|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:0000256|ARBA:ARBA00004926, ECO:0000256|HAMAP-Rule:MF_00473,
CC ECO:0000256|RuleBase:RU000612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ859183; CCB68348.1; -; Genomic_DNA.
DR RefSeq; WP_014082828.1; NC_016001.1.
DR AlphaFoldDB; G2Z413; -.
DR STRING; 1034807.FBFL15_0198; -.
DR KEGG; fbr:FBFL15_0198; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_10; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000009186; 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 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; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 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 {ECO:0000256|HAMAP-Rule:MF_00473};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW Rule:MF_00473};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00473};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00473};
KW Reference proteome {ECO:0000313|Proteomes:UP000009186}.
FT ACT_SITE 355
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 386
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 514
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 547 AA; 61782 MW; 8328A66EC93223F7 CRC64;
MALQNTNPTQ TSAWQLLEQH FQEMKTISMK EMFASDPDRS SKFHIQWDDF LIDYSKNIIN
SKTMQHLLDL TKEVQLKEAI DQYFEGGIIN KTENRAVLHT ALRSTEAEAV MVDNQNVLLE
IAAVKAKMKQ FSDDIILGNK KGYTNQNFTD VVNIGIGGSD LGPAMVVEAL QFYKNHLNVH
FVSNIDGDHA QEIIKNLNPE TTLFVIVSKT FTTQETLTNS ETIKKWFLQK ASPEDVAKHF
VAVSTNIQNV TLFGIHPDHI FPMWDWVGGR FSLWSAVGLT ISLAIGYNQF DNLLSGAHKM
DQHFKNTPFD HNIPVVLALI SVWYNNFFGA ESEAIIPYTQ YLQKLAPYLQ QGIMESNGKS
IDRNGNAVTY QTGTIVWGEP GSNSQHAFFQ LIHQGTKLIP SDFIGFVKSL YGNEDHHNKL
MSNFFAQTEA LLNGKNYDQV QAEFSKNDFA TGKAAFLTPF KIFEGNKPTN TILIQQLTPS
TLGALIAMYE HKIFVQGIIW NIFSYDQWGV ELGKQLANSI LSEIETGKIN AHDHSTAFLL
DYYLKNK
//
