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Database: UniProt
Entry: R5UVV2_9BACE
LinkDB: R5UVV2_9BACE
Original site: R5UVV2_9BACE 
ID   R5UVV2_9BACE            Unreviewed;       445 AA.
AC   R5UVV2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=BN535_02571 {ECO:0000313|EMBL:CCZ72862.1};
OS   Bacteroides caccae CAG:21.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1263037 {ECO:0000313|EMBL:CCZ72862.1, ECO:0000313|Proteomes:UP000017990};
RN   [1] {ECO:0000313|EMBL:CCZ72862.1, ECO:0000313|Proteomes:UP000017990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:21 {ECO:0000313|Proteomes:UP000017990};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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}.
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:CCZ72862.1}.
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DR   EMBL; CBAN010000073; CCZ72862.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5UVV2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000017990; 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; 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        287
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   445 AA;  48872 MW;  FDD98212CDC7FF3D CRC64;
     MISLNIEKTF GFISKEKVSA YEAEVKAAQE MLEKGTGKGN DFLGWLHLPS SISKEHLADL
     NATAKVLRDN CEVVIIAGIG GSYLGARAVI EALSNSFTWL QEKKTAPIMI YAGHNISEDY
     LFELTEYLKD KKFGVINISK SGTTTETALA FRLLKKQCED QRGKETAKQV IVAVTDAKKG
     AARVTADKEG YKTFIIPDNV GGRFSVLTPV GLLPIAVAGF DIEQLVAGAA DMEKACGADV
     PFAENPAAIY AATRNELYRN GKKIEILVNF CPKLHYVSEW WKQLYGESEG KDNKGIFPAS
     VDFSTDLHSM GQWIQEGERS IFETVISLDK VDHKLEVPSD EANLDGLNFL AGKRVDEVNK
     MAELGTQLAH VDGGVPNMRI VLPSLSEYNI GSLLYFFEKA CGISGYLLGV NPFNQPGVEA
     YKKNMFALLN KPGYEEESKA IQSRL
//
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