ID A0A0B0HAC7_SOVGS Unreviewed; 531 AA.
AC A0A0B0HAC7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=gpi {ECO:0000313|EMBL:KHF25632.1};
GN Synonyms=pgi {ECO:0000256|HAMAP-Rule:MF_00473};
GN ORFNames=BOV88_03735 {ECO:0000313|EMBL:OOY35759.1}, JV46_18220
GN {ECO:0000313|EMBL:KHF25632.1};
OS Solemya velum gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2340 {ECO:0000313|EMBL:KHF25632.1, ECO:0000313|Proteomes:UP000030856};
RN [1] {ECO:0000313|EMBL:KHF25632.1, ECO:0000313|Proteomes:UP000030856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH {ECO:0000313|EMBL:KHF25632.1,
RC ECO:0000313|Proteomes:UP000030856};
RX PubMed=25342549; DOI=10.1186/1471-2164-15-924;
RA Dmytrenko O., Russell S.L., Loo W.T., Fontanez K.M., Liao L., Roeselers G.,
RA Sharma R., Stewart F.J., Newton I.L., Woyke T., Wu D., Lang J.M.,
RA Eisen J.A., Cavanaugh C.M.;
RT "The genome of the intracellular bacterium of the coastal bivalve, Solemya
RT velum: a blueprint for thriving in and out of symbiosis.";
RL BMC Genomics 15:924-924(2014).
RN [2] {ECO:0000313|EMBL:OOY35759.1, ECO:0000313|Proteomes:UP000190962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MA-KB16 {ECO:0000313|EMBL:OOY35759.1};
RA Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT "Mixed transmission modes and dynamic genome evolution in an obligate
RT animal-bacterial symbiosis.";
RL Submitted (NOV-2016) 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:KHF25632.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRAA01000001; KHF25632.1; -; Genomic_DNA.
DR EMBL; MPNX01000003; OOY35759.1; -; Genomic_DNA.
DR RefSeq; WP_043115297.1; NZ_MPRZ01000012.1.
DR AlphaFoldDB; A0A0B0HAC7; -.
DR STRING; 2340.JV46_18220; -.
DR GeneID; 67403870; -.
DR PATRIC; fig|2340.3.peg.148; -.
DR eggNOG; COG0166; Bacteria.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000030856; Unassembled WGS sequence.
DR Proteomes; UP000190962; 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:UP000030856}.
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 389
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 500
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 531 AA; 59493 MW; 370842ACE02B532C CRC64;
MKVEKYDITA TDSWSALKKL TRSISELRIS ELYAADNSRV EKYSLKCAGV YLDFSKNLVD
ENVRRALLDL LSESPFEEQR EAMFRGYAIN TTEQRPVLHT ALRSDKQMLA DDGLENLGTQ
IEAQKQHIKE VSDKIRSGNW RGSSGRQVTD VINLGIGGSD LGPRMVCEAL KEFAHPSVRC
HFVSNVDGEL INSTLKKLDP ETTLVIISSK TFTTQETLLN ANTAAAWFRE HLSLENPYAT
SHFIGVTASP ENAIKLGVLE ENLLEFWDWV GGRYSLWSTI GLSIAISLGY ERFEKLLNGA
REMDRHFRSS PADQNMPVIM ALLGLWYTDF FDAESQAVIP YCQRMVEFPT YLQQLDMESN
GKLVMHDGSA VNCKTGPIVW GQTGTNGQHS FFQLLHQGSH MVPVDFIGVL KDKMSSPDHH
RVLLANMLAQ SAALMQGKQA EESEPYRHYP GNRPSNVILM DELSPYTLGA LIALYEHKVF
VQGCLWNINS FDQWGVELGK VLADKLLSEE SDKSDLDDST RTLLAAVDAT L
//
