ID A0A0C5W8Y7_9FLAO Unreviewed; 539 AA.
AC A0A0C5W8Y7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:AJR02717.1};
GN ORFNames=AW14_02690 {ECO:0000313|EMBL:AJR02717.1};
OS Siansivirga zeaxanthinifaciens CC-SAMT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Siansivirga.
OX NCBI_TaxID=1454006 {ECO:0000313|EMBL:AJR02717.1, ECO:0000313|Proteomes:UP000032229};
RN [1] {ECO:0000313|EMBL:AJR02717.1, ECO:0000313|Proteomes:UP000032229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-SAMT-1 {ECO:0000313|EMBL:AJR02717.1,
RC ECO:0000313|Proteomes:UP000032229};
RA Young C.-C., Hameed A., Huang H.-C., Shahina M.;
RL Submitted (FEB-2014) 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; CP007202; AJR02717.1; -; Genomic_DNA.
DR RefSeq; WP_044637397.1; NZ_CP007202.1.
DR AlphaFoldDB; A0A0C5W8Y7; -.
DR STRING; 1454006.AW14_02690; -.
DR KEGG; sze:AW14_02690; -.
DR PATRIC; fig|1454006.5.peg.513; -.
DR HOGENOM; CLU_017947_3_1_10; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000032229; 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:UP000032229}.
FT ACT_SITE 355
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 386
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 506
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 539 AA; 60714 MW; 6ABAA24EA5F19AD5 CRC64;
MALPSINPTT TKSWNNLQKH FNEISGLHMK DLFAEDKDRA NKFTIKWEDF YVDFSKNRIT
EETFKHLLEL ADEVKLKDAI KSQFSGEIIN ETEGRAVLHT ALRAPKDADF KVDGVNVMPE
IYAVKEKIEA FTNKVVNGEQ KGFTGKSFTD VVNIGIGGSD LGPAMVVDSL QFYKNHLTTH
FVSNVDGDHV NEVIKKLNPE TTLFVIVSKT FTTQETLSNA NTIKEWFLKS ASEEAIAKHF
VAVSTNIKNV KSFGIDENNI FPMWDWVGGR FSLWSAVGLT ISLAVGYSNY ESLLKGANKM
DEHFKNEDFK SNIPVVLALL TIWYNNFFKA ESEAVIPYSQ YLNQFATYLQ QGIMESNGKS
VDRNGHPIKY QTGTIIWGEP GTNSQHAFFQ LIHQGTKLIP ADFIGFVSSL HGNQDHQDKL
MSNFLAQTEA LLNGKTETEV IAEGATGNLT PFKVFQGNKP TNTIFINKLT PESLGELIAM
YEHKIFVQGI IWNIFSYDQF GVELGKQLAN KILQEFNNST TNAHDSSTQN LLNYYKQFK
//
