G6PI_ACIBC
ID G6PI_ACIBC Reviewed; 556 AA.
AC B2I056;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=ACICU_00090;
OS Acinetobacter baumannii (strain ACICU).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=405416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACICU;
RX PubMed=18411315; DOI=10.1128/aac.01643-07;
RA Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT Acinetobacter baumannii strain belonging to the European clone II group.";
RL Antimicrob. Agents Chemother. 52:2616-2625(2008).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473}.
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DR EMBL; CP000863; ACC55402.1; -; Genomic_DNA.
DR RefSeq; WP_000045495.1; NZ_CP031380.1.
DR AlphaFoldDB; B2I056; -.
DR SMR; B2I056; -.
DR KEGG; abc:ACICU_00090; -.
DR HOGENOM; CLU_017947_3_1_6; -.
DR OMA; CPAYAYG; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008839; 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; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 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; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..556
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000125682"
FT ACT_SITE 360
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 391
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 519
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 556 AA; 62709 MW; 12B8A7DFD412D366 CRC64;
MSKSIEKFPK ELVSPIAQLH SLVEKNSKLH IKELFAAEQD RFQNYSVKFD QLVFDYSKHR
ITKSVLEQLF ALAKTKQLTH WIERLFSQDK VNCTEQRAAM HWALRLPSEY SKFPELTKQV
HNQLQRMYAL VEKIHAGQYR GATGEVIQDV VNIGVGGSDL GPQMVTHALC DFKVKTAKPL
NVHFVSTMDG SQLSDLLHQL RPETTLFIIS SKSFGTIDTL SNAQTVRQWL EKALGKHDRV
VKSHFIGVST KAEKMTEWGI APDNQLLLWD WVGGRYSLWS CIGFPIALTI GIDGFQQLLA
GAHAVDEHFQ NTGFEQNIPV LMALLGIWNN NFLNIQTHAV LPYDGRLKYF AAYLQQLEME
SNGKSVQRDG QKVELDTCPI VWGEVGPNAQ HAFYQLLHQG TQAVSCDFIA PIQRYNADHF
TYVENAEALI EQHHLALSNC LAQSRLLAFG NEALDSAELK NLPIYKQYEG NQPSSTLLLK
ELNPYSLGML IALYEHKVFV QSVIWNINPF DQWGVEKGKQ IADQLLPILN GAQNDLSTLD
ASTRGLIKIL LGKVDG