G6PI_CHLT2
ID G6PI_CHLT2 Reviewed; 525 AA.
AC B0B7U7; O84382; Q46402;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=CTL0633;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-525.
RX PubMed=7543468; DOI=10.1128/jb.177.15.4252-4260.1995;
RA Fahr M.J., Douglas A.L., Xia W., Hatch T.P.;
RT "Characterization of late gene promoters of Chlamydia trachomatis.";
RL J. Bacteriol. 177:4252-4260(1995).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA75628.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AM884176; CAP04073.1; -; Genomic_DNA.
DR EMBL; L40822; AAA75628.1; ALT_FRAME; Genomic_DNA.
DR PIR; F71521; F71521.
DR RefSeq; WP_009873769.1; NC_010287.1.
DR RefSeq; YP_001654706.1; NC_010287.1.
DR AlphaFoldDB; B0B7U7; -.
DR SMR; B0B7U7; -.
DR EnsemblBacteria; CAP04073; CAP04073; CTL0633.
DR KEGG; ctb:CTL0633; -.
DR PATRIC; fig|471472.4.peg.683; -.
DR HOGENOM; CLU_017947_3_1_0; -.
DR OMA; IGVWYIN; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000795; 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..525
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000125705"
FT ACT_SITE 347
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 378
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 493
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT CONFLICT 135..145
FT /note="YIARAKFSTLV -> ACLQVDSRGSP (in Ref. 2; AAA75628)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="G -> K (in Ref. 2; AAA75628)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="R -> L (in Ref. 2; AAA75628)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="R -> A (in Ref. 2; AAA75628)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="Missing (in Ref. 2; AAA75628)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="S -> T (in Ref. 2; AAA75628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 57700 MW; BF49762A614C6ADE CRC64;
MMGKGFLDCE SLVALQEMAL HPIDLTASGC LSEERIQKNS LSVEGFTYSY ATERVDDRCL
EALQGLTEER ELIKQMECMQ QGAIMNRIEG FQSESRPVLH TATRAWVRDQ DLHEEAAAIA
RHSKEEALRL AEFLYIARAK FSTLVQIGIG GSELGPKAMY FAMQGSCPSD KRIFFVSNID
PDNAAEVLRE IDLEQTLVVV VSKSGTTLEP AANEELFRQA YQNKGLSIAE HFVAVTSQGS
PMDDKSRYLE VFHLWDSIGG RFSATSMVGG VVLGFAFGYE AFIEFLQGAA AIDAHALTPK
MRENLPLLSA MLGVWNRNLL GYPTTAVIPY STGLKYFTAH LQQCGMESNG KSISREGKEI
SFRTSPIIWG DVGTNCQHSF FQSLHQGTDI VPVEFIGFLH NQRGLDCVLS GSSSSQKLFA
NLVAQSLALA QGRDNANPNK RFKGNSPSSI LVAQQLSPRI AGSLLAFYEH KFAFQGFCWG
INSFDQEGVS LGKELATQII GIMSGNAPVE FPEARGVLRL FNVLT
