ID G6PI_LEPCP Reviewed; 545 AA.
AC B1Y2Y7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 02-NOV-2016, entry version 57.
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};
GN OrderedLocusNames=Lcho_3385;
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Leptothrix.
OX NCBI_TaxID=395495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6-
CC phosphate. {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}.
DR EMBL; CP001013; ACB35643.1; -; Genomic_DNA.
DR RefSeq; WP_012348390.1; NC_010524.1.
DR ProteinModelPortal; B1Y2Y7; -.
DR STRING; 395495.Lcho_3385; -.
DR EnsemblBacteria; ACB35643; ACB35643; Lcho_3385.
DR KEGG; lch:Lcho_3385; -.
DR PATRIC; 22397185; VBILepCho83238_3415.
DR eggNOG; ENOG4107QP8; Bacteria.
DR eggNOG; COG0166; LUCA.
DR HOGENOM; HOG000261370; -.
DR KO; K01810; -.
DR OMA; HAYARHH; -.
DR OrthoDB; POG091H04C3; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001693; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP.
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 PANTHER; PTHR11469; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
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 Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW Reference proteome.
FT CHAIN 1 545 Glucose-6-phosphate isomerase.
FT /FTId=PRO_1000125738.
FT ACT_SITE 376 376 {ECO:0000255|HAMAP-Rule:MF_00473}.
FT ACT_SITE 514 514 {ECO:0000255|HAMAP-Rule:MF_00473}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 46 524 ihamap:G6P_isomerase [T]
FT MYHIT 9 545 iprf:P_GLUCOSE_ISOMERASE_3 [T]
FT MYHIT 497 514 ipat:P_GLUCOSE_ISOMERASE_2 [T]
FT MYHIT 255 268 ipat:P_GLUCOSE_ISOMERASE_1 [T]
FT MYHIT 52 540 ipfam:PGI [T]
SQ SEQUENCE 545 AA; 58306 MW; B78C22550CD49E22 CRC64;
MNTPRCDQTA AWAALAAHHQ GAGRQFDLRT AFGADAGRFD AFSLQAPEVF ADLSKNHWDA
TTRGLLLGLA RQCQIESRRD AMLAGEPINH TEGRAVLHTA LRAPRGAAPF SDDVHGVLDA
MLAYVEQVRD TATSGIKHVV NIGIGGSDLG PQMVVPALDA YAQRGLQLHF VSNVDGHDIA
PVLRDLNPRE TLVIVASKTF TTQETMANAQ VARTWFLAGY GEGGEAAIAK HFAASTTNVA
AAAKFGITTT FGFWDWVGGR YSLWSAIGLP IALAVGAENF RALLAGAHAM DRHFATAPLE
SNLPIQLGLL DVWYRNFLGY TSRSIAPYHQ GLRRLPAYLQ QLEMESNGKC VDLDGASLPY
GTCPVVWGEA GTNGQHAYFQ MLHQGTDVIP VEFIAVKTPN HGPDVADELK AGLADQHVKL
LANCLAQSQA LMLGKTTDDA LTDKAPTAST ALDALTVARH RTFPGNRPSS TLVLDRLSPA
SLGALIALYE HRVYTSGALW GINSFDQWGV ELGKALCNQL LPRFASGESA GLDASTAGLL
ARLRG
//
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