ID S7JAE6_VIBFL Unreviewed; 550 AA.
AC S7JAE6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 ORFNames=L910_3491 {ECO:0000313|EMBL:EPP19160.1};
OS Vibrio fluvialis PG41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1336752 {ECO:0000313|EMBL:EPP19160.1, ECO:0000313|Proteomes:UP000014854};
RN [1] {ECO:0000313|EMBL:EPP19160.1, ECO:0000313|Proteomes:UP000014854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG41 {ECO:0000313|EMBL:EPP19160.1,
RC ECO:0000313|Proteomes:UP000014854};
RX PubMed=23895343; DOI=10.1186/1757-4749-5-20;
RA Khatri I., Mahajan S., Dureja C., Subramanian S., Raychaudhuri S.;
RT "Evidence of a new metabolic capacity in an emerging diarrheal pathogen:
RT lessons from the draft genomes of Vibrio fluvialis strains PG41 and
RT I21563.";
RL Gut Pathog. 5:20-20(2013).
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:EPP19160.1}.
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DR EMBL; ASXS01000039; EPP19160.1; -; Genomic_DNA.
DR RefSeq; WP_020332707.1; NZ_ASXS01000039.1.
DR AlphaFoldDB; S7JAE6; -.
DR PATRIC; fig|1336752.4.peg.4855; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000014854; 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}.
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; 61100 MW; B20A2C8E87A0DE11 CRC64;
MLKNINPTQT QAWKALTAHF ESAQDMDLKT LFAEDSQRFA KYSTRFGNDI LVDYSKNLVN
EETMKHLFAL AEETDVKSAI QAMFSGEAIN QTEGRSVLHT ALRNRSNTPV MVKGEDVMPA
VNAVLEKMKS FSERIIGGEW KGFTGKAITD VVNIGIGGSD LGPYMVTEAL TPYKNHLTMH
FVSNVDGTHI AETLKKVNPE TTLFLVASKT FTTQETMTNA HSARDWFLAT AGDEAHVAKH
FAALSTNAQA VAEFGIDTDN MFEFWDWVGG RYSLWSAIGL SIILSIGFDN FVELLTGAHE
MDKHFVETPF ESNIPMILAL IGIWYNNFHG AESEAILPYD QYMHRFAAYF QQGNMESNGK
FVDRDGNPVT YQTGPIIWGE PGTNGQHAFY QLIHQGTKLI PCDFIAPALT HNAVSDHHQK
LMSNFFAQTE ALAFGKSAEV VKAEFIKAGK TEEEVAALIP FKVFEGNRPT NSILVKQITP
RSLGNLIAMY EHKIFVQGVI WNIFTFDQWG VELGKQLANQ ILPELADGAQ ISSHDSSTNG
LINAFKAFRG
//
