ID A0A135I470_9GAMM Unreviewed; 550 AA.
AC A0A135I470;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:KXF80233.1};
GN ORFNames=ATN88_10305 {ECO:0000313|EMBL:KXF80233.1};
OS Enterovibrio coralii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Enterovibrio.
OX NCBI_TaxID=294935 {ECO:0000313|EMBL:KXF80233.1, ECO:0000313|Proteomes:UP000070529};
RN [1] {ECO:0000313|EMBL:KXF80233.1, ECO:0000313|Proteomes:UP000070529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 912 {ECO:0000313|EMBL:KXF80233.1,
RC ECO:0000313|Proteomes:UP000070529};
RA Gomez-Gil B., Enciso-Ibarra J.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXF80233.1}.
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DR EMBL; LNTY01000055; KXF80233.1; -; Genomic_DNA.
DR RefSeq; WP_067419462.1; NZ_LNTY01000055.1.
DR AlphaFoldDB; A0A135I470; -.
DR STRING; 294935.ATN88_10305; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000070529; Unassembled WGS sequence.
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:UP000070529}.
FT ACT_SITE 356
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 387
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 515
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 550 AA; 61072 MW; 409F59F9C4B8305C CRC64;
MLKSINPTQT AAWKALTAHF EDAQDLTLTS LFANDPNRFD KFSVQFGNDI LLDYSKNLIS
EQTLDKLFAL ADETELKDAI SAMFRGDKIN QTEDRSVLHV ALRNRSNTPI MVDGEDVMPA
VNAVLEKMKS FSDRVIGGEW KGYTGKEITD VVNIGIGGSD LGPYMVSEAL AAYKSRLNLH
FVSNVDGTHI AETLKGLNPE TTLFLIASKT FTTQETMTNA LSARDWFLAT AEDQAHVAKH
FAALSTNATA VSEFGIDTEN MFEFWDWVGG RYSLWSAIGL SICLSIGYDN FIELLSGAHE
MDQHFQSTPF TENLPVLLAL IGIWYNNFHG AESEAILPYD QYLHRFAAYF QQGNMESNGK
YVDRDGNPVD YQTGPIIWGE PGTNGQHAFY QLIHQGTKLI PCDFIAPAIS HNPLSDHHPK
LMANFFAQTE ALAFGKTREQ VEAEFAAAGK SAEDVAALVP FKVFEGNRPT NSILVKQVTP
SVLGALIAMY EHKIFVQGVI WNIFSFDQWG VELGKQLANQ ILPELADQEE VDSHDSSTNG
LINAFKQWRA
//
