ID A0A0A2MJ30_9FLAO Unreviewed; 546 AA.
AC A0A0A2MJ30;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:KGO91586.1};
GN ORFNames=Q766_17100 {ECO:0000313|EMBL:KGO91586.1};
OS Flavobacterium subsaxonicum WB 4.1-42 = DSM 21790.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121898 {ECO:0000313|EMBL:KGO91586.1, ECO:0000313|Proteomes:UP000030111};
RN [1] {ECO:0000313|EMBL:KGO91586.1, ECO:0000313|Proteomes:UP000030111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB 4.1-42 {ECO:0000313|EMBL:KGO91586.1,
RC ECO:0000313|Proteomes:UP000030111};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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:KGO91586.1}.
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DR EMBL; JRLY01000017; KGO91586.1; -; Genomic_DNA.
DR RefSeq; WP_026989886.1; NZ_JRLY01000017.1.
DR AlphaFoldDB; A0A0A2MJ30; -.
DR STRING; 1121898.GCA_000422725_03803; -.
DR eggNOG; COG0166; Bacteria.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000030111; 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:UP000030111}.
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 546 AA; 60078 MW; D3CDC961A9E4C1C0 CRC64;
MALQNINPTS TAAWKALGEH FAEMQTASMQ DMFAADTNRA EKFHIKWNDF LIDYSKNIIN
PKTLELLQDL AKQVDLSGAI ASYFGGDAIN RTEGRAVLHT ALRAPESANV LVDGANVLPE
VYAVKNKIKA FTEAIISGAQ TGYTGKPFTD VVNVGIGGSD LGPNMVVEAL KFYKTPLNVR
FISNVDGDHV TESLKGLDPE TTLFVIASKT FTTQETLTNA ETARDWFLNT ASQADVAKHF
VAVSTNIQKV TEFGIDPNNV FPMWDWVGGR FSLWSAVGLS IALAVGFDNF DGMLKGAHDM
DEHFRTAAFE DNIPVVLALL SVWYNNFFGA ESEALIPYTQ YLQKLAPYLQ QGIMESNGKS
VGRDGKPVTY QTGTIIWGEP GTNSQHAFFQ LIHQGTKLIP TDFIGFIEPL YGNKDHHDKL
MSNFFAQTEA LLNGKAEAVV RAEFEKAGVT GEKADYLTPF KIFTGNKPTN TLLIKKLTPE
TLGSLVALYE HKIFVQGVIW NIFSYDQWGV ELGKQLANSI LGEINSGDVK QHDSSTTFLL
KAFLGK
//
