ID A0A0A7JG77_9PSED Unreviewed; 554 AA.
AC A0A0A7JG77;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=NJ69_00360 {ECO:0000313|EMBL:AIZ31568.1};
OS Pseudomonas parafulva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=157782 {ECO:0000313|EMBL:AIZ31568.1, ECO:0000313|Proteomes:UP000030632};
RN [1] {ECO:0000313|EMBL:AIZ31568.1, ECO:0000313|Proteomes:UP000030632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRS01-1 {ECO:0000313|EMBL:AIZ31568.1,
RC ECO:0000313|Proteomes:UP000030632};
RA Liu Q.;
RT "Genome sequence of Pseudomonas parafulva CRS01-1, an antagonistic
RT bacterium isolated from rice field.";
RL Submitted (OCT-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; CP009747; AIZ31568.1; -; Genomic_DNA.
DR RefSeq; WP_039575142.1; NZ_CP031641.1.
DR AlphaFoldDB; A0A0A7JG77; -.
DR KEGG; ppv:NJ69_00360; -.
DR eggNOG; COG0166; Bacteria.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000030632; 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}.
FT ACT_SITE 359
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 390
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 518
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 554 AA; 61514 MW; CF48A7B144E8A0E9 CRC64;
MAYYRTPHDV TALPAWQALK QHRDAMQGFS MREAFAADPK RFEQFSLSSC GLFLDYSKNL
ITEQTRDLLV DLAREVGLEE AIKAMFSGEI INGSEGRPVL HTALRRPVGD KLNVGGVNVM
PEVHKVLNQI TELVGRIHDG LWRGYSEKPI TDVVNIGIGG SFLGPELVSE ALLPYAQRGV
RCHYLANIDG SEFHELSAKL RAETTLFIVS SKSFNTLETL KNAQAARTWY LAQGGSEAEL
YRHFIAVSSN KTAAVAFGIR EENIFPMWDW VGGRYSLWSA IGLPIALAIG TANFKELLSG
AYTMDQHFQT APFEKNMPVL LALLGVWYGN FWNASSHAIL PYDHYLRNIT KHLQQLDMES
NGKSVLTDGS PVKTETGPVI WGGVGCNGQH AYHQLLHQGT QMIPADFIVP VVSFNPVADH
HQWLYANCLS QSQALMLGKT REEAETELRA KGLNEADVET LAPHKVIPGN RPSNTLVVER
ISPRRLGALV AMYEHKVFVQ SVIWGINAFD QWGVELGKEL GKGVYQRLVG SLEESAEDGS
TQGLINYFRG RHRG
//
