ID A0A0D0F2Q2_9FLAO Unreviewed; 547 AA.
AC A0A0D0F2Q2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:KIO52392.1};
GN ORFNames=IW18_14560 {ECO:0000313|EMBL:KIO52392.1};
OS Flavobacterium hibernum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=37752 {ECO:0000313|EMBL:KIO52392.1, ECO:0000313|Proteomes:UP000032061};
RN [1] {ECO:0000313|EMBL:KIO52392.1, ECO:0000313|Proteomes:UP000032061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12611 {ECO:0000313|EMBL:KIO52392.1,
RC ECO:0000313|Proteomes:UP000032061};
RA Stropko S.J., Pipes S.E., Newman J.D.;
RT "Genome of Flavobacterium hibernum DSM 12611.";
RL Submitted (JAN-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}.
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:KIO52392.1}.
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DR EMBL; JPRK01000011; KIO52392.1; -; Genomic_DNA.
DR RefSeq; WP_041518666.1; NZ_UGGR01000004.1.
DR AlphaFoldDB; A0A0D0F2Q2; -.
DR STRING; 37752.IW18_14560; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000032061; 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 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}.
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 514
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 547 AA; 61357 MW; 9F54C6FD9F59362E CRC64;
MALNTTNPTG TEAWKNLQNH YNAIHETTIQ ELFQQDNARV EKFNLQWNDF LVDYSKNNIS
QETVSLLLEL SNSIGLKDAI AQYFGGAIIN QTENRAVLHT ALRAPESAVI NVDGENVIPE
VYEVKNKIKN FTEEVISGQR KGFTGKAFTD IVNIGIGGSD LGPVMAVEAL QFYKNHLKTH
FVSNVDGDHV NEIIKKLNPE TTLFLIVSKT FTTQETLSNS ETIKEWFLKS ASQEDIAKHF
VAVSTNIQKV TEFGINPDNV FPMWDWVGGR FSLWSAVGLS IALAIGFDNY NQLLVGANEM
DEHFRSTEFD ENIPVILALL SVWYNNFYGA ESEALIPYTQ YLSKLAPYLQ QATMESNGKS
VGRDGKPVNY QTGTIIWGEP GTNSQHAFFQ LIHQGTKLIP TDFIGFIKPL YGNEDHHDKL
MSNFFAQTEA LMNGKTAAQV QTEFDKQGLS AEKASYLLPF KVFTGNKPTN TILIEKLTPK
SLGSLIALYE HKIFVQGVIW NIFSFDQWGV ELGKQLANSI LDEINTKTVK DHDSSTSFLL
NHFLKNK
//
