ID A0A0N9VMT7_9GAMM Unreviewed; 557 AA.
AC A0A0N9VMT7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=AOY20_03680 {ECO:0000313|EMBL:ALH94704.1};
OS Acinetobacter equi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1324350 {ECO:0000313|EMBL:ALH94704.1, ECO:0000313|Proteomes:UP000064939};
RN [1] {ECO:0000313|EMBL:ALH94704.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114 {ECO:0000313|EMBL:ALH94704.1};
RX PubMed=26620413;
RA Poppel M.T., Skiebe E., Laue M., Bergmann H., Ebersberger I., Garn T.,
RA Fruth A., Baumgardt S., Busse H.J., Wilharm G.;
RT "Acinetobacter equi sp. nov. isolated from horse faeces.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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; CP012808; ALH94704.1; -; Genomic_DNA.
DR RefSeq; WP_054580604.1; NZ_CP012808.1.
DR AlphaFoldDB; A0A0N9VMT7; -.
DR STRING; 1324350.AOY20_03680; -.
DR KEGG; aei:AOY20_03680; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000064939; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000064939}.
FT ACT_SITE 361
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 392
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 520
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 557 AA; 63089 MW; F09EFCDE85318E4D CRC64;
MENEFQRTSI EKQVKLIADL NKLKDEFKQK HLTELFEFNP ERFKEFSVSL NPIVCDFSKQ
RVDQKVIHSL SAWASVCNLS DEIKKLFSTE AINYTENRAA MHWALRLPKN DCKNQELSSL
VHEQLQRMFT LVNKIHAGQY RGMTGEVIQD VVNIGVGGSD LGPLMASYAL SDFKQETAKP
LNIHFVSTID GSQLSELLHK LRPETTLFII SSKSFGTIDT LSNAQTAKIW LEKALGEGSR
TLKHHFIGVS TKPEKMTAWG ISLENQFLLW DWVGGRYSLW SCIGLPIALT IGVEGFQQFL
NGAYEVDQHF QHAPFDKNIP VLMGLLGAWN NNFLDIQTHA VLPYDGRLKY FAPYLQQLEM
ESNGKSIQRN GQKVEFDTCP IIWGEVGPNA QHAFYQLLHQ GTHSVSSDFI APVYRYNSNQ
FTYVDSAEAL IEQHNLALSN CLAQSRLLAF GNEALDAEEV STLPEYKQYE GNQPSTTILL
QELNPYSLGM LIAMYEHKVF VQSVLWNINP FDQWGVEKGK EIANQLLPIL NGEQVNTSQL
DASTRGLLDI LLRAKHE
//
