ID A0A0P7AWC5_9FLAO Unreviewed; 545 AA.
AC A0A0P7AWC5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=I595_1413 {ECO:0000313|EMBL:KPM32986.1};
OS Croceitalea dokdonensis DOKDO 023.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Croceitalea.
OX NCBI_TaxID=1300341 {ECO:0000313|EMBL:KPM32986.1, ECO:0000313|Proteomes:UP000050280};
RN [1] {ECO:0000313|EMBL:KPM32986.1, ECO:0000313|Proteomes:UP000050280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOKDO 023 {ECO:0000313|EMBL:KPM32986.1,
RC ECO:0000313|Proteomes:UP000050280};
RA Kwon S.-K., Lee H.K., Kwak M.-J., Kim J.F.;
RT "Genome sequence of the marine flavobacterium Croceitalea dokdonensis DOKDO
RT 023 that contains proton- and sodium-pumping rhodopsins.";
RL Submitted (SEP-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:KPM32986.1}.
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DR EMBL; LDJX01000002; KPM32986.1; -; Genomic_DNA.
DR RefSeq; WP_054558552.1; NZ_LDJX01000002.1.
DR AlphaFoldDB; A0A0P7AWC5; -.
DR STRING; 1300341.I595_1413; -.
DR PATRIC; fig|1300341.3.peg.1606; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000050280; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050280}.
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 545 AA; 61183 MW; 141FBC6952033563 CRC64;
MSLPKIDPTT TKAWPKLEAH FKTTKEIHLK DLFAEDADRG RTFSIQWKDF LVDFSKNRIT
TETFSLLQEL AQEVGLQQAI SSYFKGEPIN ETEGRAVLHT ALRAKKTDRI MLGGSNVVDE
VYAVKKDIKS FTDAIISGTK TGFTGKAFTD VVNIGIGGSD LGPAMVVESL KFYKNHLRTH
FVSNVDGDHV HETLKELNPE TTLFVVVSKT FTTQETLSNA TTIKKWFLQH ATQQDIAKHF
AAVSTNTEKI AEFGISDSHV FPMWDWVGGR FSLWSAVGLT IALAIGFEKY DQLLQGANEM
DTHFKETDFS GNIPVVLALI SVWYNNFYGA ETEAIIPYTQ YLGRFSAYLQ QGIMESNGKS
VDRNGKITPY QTGTIIWGEP GTNSQHAFFQ LIHQGTKLIP SDFIGFKNSL HGDSDHHNKL
MANFFAQTEA LMNGKTQQEV IAEFKESGKS EKEVNALVPF KVFEGNKPTN TLLIDRLTPK
SLGSLIALYE HKIFVQGVLW NIFSYDQWGV ELGKQLAKKT LSDIENSEIS KHDSSTMRLL
QYFKK
//
