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Database: UniProt
Entry: A6T0F5_JANMA
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Original site: A6T0F5_JANMA 
ID   A6T0F5_JANMA            Unreviewed;       546 AA.
AC   A6T0F5;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 99.
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:ABR88949.1};
GN   OrderedLocusNames=mma_2312 {ECO:0000313|EMBL:ABR88949.1};
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR88949.1, ECO:0000313|Proteomes:UP000006388};
RN   [1] {ECO:0000313|EMBL:ABR88949.1, ECO:0000313|Proteomes:UP000006388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille {ECO:0000313|EMBL:ABR88949.1,
RC   ECO:0000313|Proteomes:UP000006388};
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA   Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the convergent
RT   evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR88949.1; -; Genomic_DNA.
DR   RefSeq; WP_012080165.1; NC_009659.1.
DR   AlphaFoldDB; A6T0F5; -.
DR   STRING; 375286.mma_2312; -.
DR   KEGG; mms:mma_2312; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_4; -.
DR   OMA; IGVWYIN; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000006388; 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:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
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:UP000006388}.
FT   ACT_SITE        353
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        384
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        512
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   546 AA;  60465 MW;  7DC21A4630B28A80 CRC64;
     MRTTLTATAA FQALQQHHTE NKGRQVRHLF AQDPARFDKL SVEGAGLFLD YSKNIVDDKT
     MTLLYALARE TEVEAQRDAM FAGKEVNRTE HRAVLHTALR KPRNEKLLLG QQDIVPEIHE
     VLDRMAVFSE RVRSGAWRGF DDREITDIVN IGIGGSYLGP KMTCQALRSF AHPRLNTHFV
     SNVDGHDLDA LLSRINPATT LFIIASKGFN TAETMMNAQS ARAWFLRHAT ESDLSKHFVA
     VSTHLDAVQA FGIAPENMFP FWDWVGGRYS VWSAIGLALM LSIGPECFKD FLAGAHAMDR
     HFQDTPLEQN LPVILALIGI WNRNFLGSSS ISIAPYHQDL RLFPGYLQQL EMESNGKSVQ
     VDGAKTSTTT CPVIWGDVGT NGQHAYFQLL HQGTDIMAVD FIAALKPTHA LEQHQVLLLA
     NCFAQSEAFM RGKNAEEVRA DMQAQGLPAA EIEKLLPHRI FPGNRPSNTI LMDTLNPGAL
     GALIALYEHK VFVQGAIWGI NSFDQWGVEL GKLLAKNIAA ELGDKAKPEQ HDSSTNGLIA
     RARAAL
//
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