ID A0A1V3NFZ4_9GAMM Unreviewed; 551 AA.
AC A0A1V3NFZ4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=B1C78_10190 {ECO:0000313|EMBL:OOG23772.1};
OS Thioalkalivibrio denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=108003 {ECO:0000313|EMBL:OOG23772.1, ECO:0000313|Proteomes:UP000189462};
RN [1] {ECO:0000313|EMBL:OOG23772.1, ECO:0000313|Proteomes:UP000189462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALJD {ECO:0000313|EMBL:OOG23772.1,
RC ECO:0000313|Proteomes:UP000189462};
RA Ahn A.-C., Meier-Kolthoff J., Overmars L., Richter M., Woyke T.,
RA Sorokin D.Y., Muyzer G.;
RT "Genomic diversity within the haloalkaliphilic genus Thioalkalivibrio.";
RL Submitted (FEB-2017) 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:OOG23772.1}.
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DR EMBL; MVBK01000058; OOG23772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3NFZ4; -.
DR STRING; 108003.B1C78_10190; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000189462; 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:UP000189462}.
FT ACT_SITE 354
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 385
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 513
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 551 AA; 61946 MW; E204FA6522BDDC24 CRC64;
MTMQVNRTRA WQALASHYDA MQNVHMKALF AQDPARFEKF SLRFGDLLLD YSKNRITEET
RDLLLDLARD RDVESWRDRM FSGERINITE DRAVLHVALR NRSNRPIRVD GEDVMPAVNG
VLERMAAFTR KVRSGEWTGH TGKRIRHVVN IGIGGSDLGP VMVCEALRPY GHEDLTMHFV
SNVDGAHMGQ TLERVDPEST LFIIASKTFT TQETLTNART ARDWLVRHAG DEAAVAKHFV
AVSTNRQGVA AFGIDPEHMF SFWDWVGGRY SLWSAIGLPI ALYVGMERFE ALLEGAHAMD
EHFRSAPLES NLPVILALLG VWYVDFFGAG SHAILPYDQC LHRFPAYLQQ ADMESNGKSV
DRQGRSVGYD TGPVIWGEPG TNGQHAFYQL IHQGTRLIPC DFLAPCESHY PLGDHHHILL
SNFFAQTEAL MRGRTLEEVR AEMLGAGADP DQVARVAPHR VFEGNRPSNS LLFRRLDPHT
LGSLIALYEH KIFVQSVIWG VNAYDQWGVE LGKQLARAIL PELDSEAPVD AHDASTNGLI
NHYRRMTGCE V
//
