ID I5ATR1_EUBCE Unreviewed; 526 AA.
AC I5ATR1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=EubceDRAFT1_1373 {ECO:0000313|EMBL:EIM57184.1};
OS [Eubacterium] cellulosolvens 6.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=633697 {ECO:0000313|EMBL:EIM57184.1, ECO:0000313|Proteomes:UP000005753};
RN [1] {ECO:0000313|EMBL:EIM57184.1, ECO:0000313|Proteomes:UP000005753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6 {ECO:0000313|EMBL:EIM57184.1,
RC ECO:0000313|Proteomes:UP000005753};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Anderson I.J., Johnson E.,
RA Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EIM57184.1, ECO:0000313|Proteomes:UP000005753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6 {ECO:0000313|EMBL:EIM57184.1,
RC ECO:0000313|Proteomes:UP000005753};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Johnson E., Mukhopadhyay B.,
RA Anderson I., Woyke T.;
RT "Improved High-Quality Draft sequence of Eubacterium cellulosolvens 6.";
RL Submitted (FEB-2012) 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}.
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DR EMBL; CM001487; EIM57184.1; -; Genomic_DNA.
DR AlphaFoldDB; I5ATR1; -.
DR STRING; 633697.EubceDRAFT1_1373; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_9; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000005753; 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:UP000005753}.
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 502
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 526 AA; 56753 MW; 9D9B1981FAD5DD39 CRC64;
MINWKNLNEL SSYQELGKVK PLDLAEAMTG QKGADRVGKY TVDMAEGLTY NYAAKAVDDD
ILGALAKLAE EAQLAEKFEE LYNGAVVNTG EKRLVLHQLT RGQLGNAVEA DGTDKRSFYI
EQQKRIADFA NKVHAGEIAN AKGEKFTTVV QIGIGGSDLG PRAMYLALEN WAKKTGTFKM
NAAFISNVDP DDASAVLGSI DVAHSLFILV SKSGTTLETL TNQAFVMDAL KKEGLDPAKH
MIAVTSETSP IAHSADFLDA FYMDDYIGGR YSSTSAVGGA VLSLAFGPEV FAAFLDGAAA
EDKLSTEKDL LKNPAMLDAL IGVYERNILG FPSTAILPYS QALSRFPAHL QQLDMESNGK
SVNRFGEPIG YVTGPIIFGE PGTNGQHSFY QLLHQGTDIV PLQFVGFRKS QIQNDVDIQG
STSQQKLCAN VAAQIVAFAC GKENADLNKN FKGGRPSSII IGDDLNPKTL GALLAHFENK
VMFQGFVWNI NSFDQEGVQL GKTLAKAVLA HETEGALTEY SKLLNI
//
