ID E2SLT0_9FIRM Unreviewed; 424 AA.
AC E2SLT0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:EFP61512.1};
GN ORFNames=HMPREF0983_02050 {ECO:0000313|EMBL:EFP61512.1};
OS Erysipelotrichaceae bacterium 3_1_53.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP61512.1, ECO:0000313|Proteomes:UP000006223};
RN [1] {ECO:0000313|EMBL:EFP61512.1, ECO:0000313|Proteomes:UP000006223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_53 {ECO:0000313|EMBL:EFP61512.1,
RC ECO:0000313|Proteomes:UP000006223};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C.,
RA Daigneault M., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL Submitted (JUL-2010) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00473}.
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:EFP61512.1}.
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DR EMBL; ACTJ01000044; EFP61512.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SLT0; -.
DR STRING; 658659.HMPREF0983_02050; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_037303_0_1_9; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000006223; 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 HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
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; 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 278
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 414
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 424 AA; 47296 MW; 6134E9037DE8B035 CRC64;
MMKLDTKHAF LKEDISSYQD IVTKCHEDLH NKTGKGNDYV GWVEWPNTYD KEEYARLKSV
AAGIRETCDV LMVCGIGGSY LGARAAVEMI NGMYSNKKPE IIFFGNTFSS TYIAQVMDYI
KDKEVAVNVI SKSGTTTETA LAFRLLKQFM EEKYGKEGAA KRIVATTDKA RGTLKTIADK
EGYETFVIPD DIGGRFSVIT PVGLFPIAVA GIDTDAIMSG LKKAYEDLKD PDLNKNDAYA
YAVCRRILEN QGKDVEMLVS YETQMTMVAE WWKQLFGESE GKEGKGNLPT SANFSTDLHS
LGQFVQDGKK VLYETLLLID KPALDLTFPE DADNLDGMNY LAGKSVDWVN KMACQGTLEA
HEETGGVSNL ILTLDDMSAE SFGYMCYFFF KACAITCYML DINPFNQPGV EVYKKNMFRL
LGKK
//
