ID A0A074TJS2_9RHOB Unreviewed; 535 AA.
AC A0A074TJS2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, 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=DL1_04825 {ECO:0000313|EMBL:KEP69218.1};
OS Thioclava dalianensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1185766 {ECO:0000313|EMBL:KEP69218.1, ECO:0000313|Proteomes:UP000027725};
RN [1] {ECO:0000313|EMBL:KEP69218.1, ECO:0000313|Proteomes:UP000027725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DLFJ1-1 {ECO:0000313|EMBL:KEP69218.1,
RC ECO:0000313|Proteomes:UP000027725};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thioclava dalianensis DLFJ1-1.";
RL Submitted (MAR-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}.
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:KEP69218.1}.
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DR EMBL; JHEH01000016; KEP69218.1; -; Genomic_DNA.
DR RefSeq; WP_038066913.1; NZ_JHEH01000016.1.
DR AlphaFoldDB; A0A074TJS2; -.
DR STRING; 1185766.SAMN05216224_10113; -.
DR eggNOG; COG0166; Bacteria.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000027725; 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:UP000027725}.
FT ACT_SITE 340
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 371
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 500
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 535 AA; 58124 MW; 6BDF4F51C43CFC23 CRC64;
MSTWQDLRRK SDAVAARHIS DLFENDKRAA GFTREFGPFT FDFSKTNIDD ETLDLLLKLA
QERDVAGKAE AMFTGAPINE TEGRAVLHTA LRNLDASVEV DGRDVMPEVR ATYARMVEFA
SAVRSGAFAG QGGKITDVVN IGIGGSDLGP AMATLALAPY HDGPRCHFVS NVDGAHIHDT
LAGLDPETTL VIVASKTFTT IETMTNAETA KRWMGQSVRE PAAQFAALST AADKTADFGI
DPARVFGFAD WVGGRYSMWG PIGLSVMIAV GPDDFAQFLK GAAQMDAHFR EAPLAENLPV
LLALVGLWHN QFCDYATRAV LPYEQRLLRL PAYLQQLEME SNGKRVSMDG KDLPVHSGPV
VWGEPGTNGQ HAFYQLIHQG TRVIPCEFMV GAQGHEPDLA HQHMLLVANC LAQSEALMRG
RSLAEATQIM RDKGLEGAEL DRQARHRVFP GSRPSTTLLY PKLTPEVFGG IIALYEHRVF
VEGAILGINS FDQWGVELGK ELALALSPVL SGEKDGADKD GSTRQLVAKV QGLRA
//
