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Database: UniProt
Entry: A0A0F7M2U7_9GAMM
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ID   A0A0F7M2U7_9GAMM        Unreviewed;       545 AA.
AC   A0A0F7M2U7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=IMCC21906_00952 {ECO:0000313|EMBL:AKH68632.1};
OS   Spongiibacter sp. IMCC21906.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; Spongiibacter.
OX   NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH68632.1, ECO:0000313|Proteomes:UP000035013};
RN   [1] {ECO:0000313|EMBL:AKH68632.1, ECO:0000313|Proteomes:UP000035013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH68632.1,
RC   ECO:0000313|Proteomes:UP000035013};
RA   Cho J.-C., Yang S.-J., Kang I.;
RT   "Complete genome sequence of IMCC21906 belonging to the
RT   Gammaproteobacteria.";
RL   Submitted (MAY-2015) 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; CP011477; AKH68632.1; -; Genomic_DNA.
DR   RefSeq; WP_052763363.1; NZ_CP011477.1.
DR   AlphaFoldDB; A0A0F7M2U7; -.
DR   STRING; 1620392.IMCC21906_00952; -.
DR   KEGG; spoi:IMCC21906_00952; -.
DR   PATRIC; fig|1620392.3.peg.999; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000035013; 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; 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:UP000035013}.
FT   ACT_SITE        352
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        383
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        511
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   545 AA;  58860 MW;  C325D9744989AD17 CRC64;
     MTQDDASHAL SALPEWQTLT QLADASASTL LKTRFQNDPN RAQCYSGDLG SLFVDYSKHH
     LDQDILDALL ALADSAKLSE KLSAQRSGAA VNNTENRKAS YPDLRQWASK TGSDPELANM
     YDKMPQLVDA VHSGKHTGTT GKAFTDVVNI GIGGSDFGPR LLCDALSNQG STKLKAHFAA
     NIDPSVISDI LAQTPPETTL FLVASKSFGT QETRSNAEAA MAWLRAATGQ QDISDHVIAI
     TSKPSAAEAF GIKPSQILSV PEWIGGRFSV WSGFGLAVAL YAGMDAFKDF LLGGHDVDQH
     VENTPLTDNI PVILGLLDVW YRNFWGYTSQ AILPYEHRLG LLPTYLQQLF MESAGKSVDV
     NGNRLGTGTG NVIWGTEGTN GQHSFHQLLH QGGDAIPCDF ITALRSYNPI ADQHQALVAN
     CFGQSLVLMN GQSAAEAEAE LLSQGVPPEE AATLGKHKAM LGNKPSTTIT MEMLTPRALG
     SLIALYEYRL FTASFIWNIN PFDQWGVERG KQVSKLLMEG LSNGGAKDVD SSTAQLMQRF
     AKAQQ
//
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