UniProt: A0A1Q2M6P1

Database: UniProt
Entry: A0A1Q2M6P1_9GAMM

LinkDB:  A0A1Q2M6P1_9GAMM 
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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (3)   
All databases (18)   

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ID   A0A1Q2M6P1_9GAMM        Unreviewed;       537 AA.
AC   A0A1Q2M6P1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=Mag101_12815 {ECO:0000313|EMBL:AQQ68415.1};
OS   Microbulbifer agarilyticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=260552 {ECO:0000313|EMBL:AQQ68415.1, ECO:0000313|Proteomes:UP000188219};
RN   [1] {ECO:0000313|EMBL:AQQ68415.1, ECO:0000313|Proteomes:UP000188219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP101 {ECO:0000313|EMBL:AQQ68415.1,
RC   ECO:0000313|Proteomes:UP000188219};
RA   Jung J., Bae S.S., Baek K.;
RT   "Genome of Microbulbifer agarilyticus GP101.";
RL   Submitted (FEB-2017) 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; CP019650; AQQ68415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2M6P1; -.
DR   STRING; 260552.Mag101_12815; -.
DR   KEGG; maga:Mag101_12815; -.
DR   eggNOG; COG0166; Bacteria.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000188219; 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:UP000188219}.
FT   ACT_SITE        347
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        378
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        506
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   537 AA;  59132 MW;  2BE1AD5E84AB5DCA CRC64;
     MDALPLSAAI AVLQQHKDQQ RWSLRDLFAS NSDRAQSFSA EAAGLYLDYS KNLLNADTLQ
     NLLDYTDTAN LKSSIEALFA GANINNTEHR PALHTALRFQ GEPKTEHEQA VADCRVQMSQ
     FVEQVHSGAW TGFSGKRIRH VVNIGIGGSD LGPRMVWEAL RPWHKQDLTT HFVANIDGAD
     LSDTLASLPA DETLFIVASK SFSTLETRQN ALSARQWVLD AGCSESDLEK HFVAVSSNIV
     AAQDFGIAAQ NIFPMWDWVG GRYSLWSAIG LPIALACGFD AYSDLLKGAN AMDTHFAEAE
     FSQNLPVLMA LIHFWYRQCW GAGSLAVLPY AQRLAKFPAW LQQLDMESLG KSVTRDGQPL
     PYPSGAVIWG AEGSNGQHSF HQLLHQGTDM IPADFVAIKE PTSELKEQHQ WLLSCCLSQS
     QALLRGKSLA EARRELEASG HTHKEVHQLA PHKVVPGNRP SNTLIVEKLD PFHLGSLLAL
     YEHKVFTFGC LLDINPFDQW GVELGKVLGN GVHAAIDGEV PEDWDGSTAL LLKKLLK
//

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