ID W6A826_9MOLU Unreviewed; 426 AA.
AC W6A826;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:AHI53142.1};
GN ORFNames=SCULI_v1c08020 {ECO:0000313|EMBL:AHI53142.1};
OS Spiroplasma culicicola AES-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276246 {ECO:0000313|EMBL:AHI53142.1, ECO:0000313|Proteomes:UP000019267};
RN [1] {ECO:0000313|EMBL:AHI53142.1, ECO:0000313|Proteomes:UP000019267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AES-1 {ECO:0000313|EMBL:AHI53142.1};
RX PubMed=24534435;
RA Chang T.H., Lo W.S., Ku C., Chen L.L., Kuo C.H.;
RT "Molecular evolution of the substrate utilization strategies and putative
RT virulence factors in mosquito-associated Spiroplasma species.";
RL Genome Biol. Evol. 6:500-509(2014).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00473}.
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DR EMBL; CP006681; AHI53142.1; -; Genomic_DNA.
DR RefSeq; WP_025363370.1; NZ_CP006681.1.
DR AlphaFoldDB; W6A826; -.
DR STRING; 1276246.SCULI_v1c08020; -.
DR KEGG; scq:SCULI_v1c08020; -.
DR PATRIC; fig|1276246.3.peg.798; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_037303_0_1_14; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000019267; 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 HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
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:UP000019267}.
FT ACT_SITE 277
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 414
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 426 AA; 47850 MW; A5C10CF51345EEDD CRC64;
MISINFSNSK IENDIKNFSK EKMKEIHDVI ENKTGLGNEF LGWLTWPEDF NKDEYQKMKE
VANKLRQEID VLLVVGIGGS YLGARAADEM IRGLYPNDKV ELIYIGNTIS STYTKQVLDY
IADKEFAIAN ISKSGTTTEP GIAFRVFEKH LIDKKGKEVA KNRIVAVTDK ARGALKQLAD
AEGYQTFTIP DDIGGRFSVF TPVGIFPLLV AGIDTDAMFR GAQKALNDLK SLDNQAYQYA
VARYIFHEQK GYKAETLVSY ELQMQMFTEW WKQLFGESEG KDGKGLFPTS VVFSTDLHSL
GQFIQEGTKN VLFETVIDVK NPTVDLNIPS TEEDLDGLNY LTTKTFHEIN ATALVGVIDA
HSNTGNVPNI ILEFDKMDAE MFGYAGYWFM KACAFSGYLL GVNPFNQPGV EVYKENMFKL
LKKPGY
//
