(data stored in ACNUC7421 zone)

SWISSPROT: C3MI91_SINFN

ID   C3MI91_SINFN            Unreviewed;       541 AA.
AC   C3MI91;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   30-AUG-2017, entry version 64.
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   OrderedLocusNames=NGR_c06460 {ECO:0000313|EMBL:ACP24439.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24439.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24439.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00473,
CC       ECO:0000256|RuleBase:RU000612, ECO:0000256|SAAS:SAAS00846235}.
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|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612,
CC       ECO:0000256|SAAS:SAAS00846231}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473,
CC       ECO:0000256|SAAS:SAAS00846238}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|HAMAP-
CC       Rule:MF_00473, ECO:0000256|RuleBase:RU000612,
CC       ECO:0000256|SAAS:SAAS00846234}.
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DR   EMBL; CP001389; ACP24439.1; -; Genomic_DNA.
DR   RefSeq; WP_012707224.1; NC_012587.1.
DR   RefSeq; YP_002825192.1; NC_012587.1.
DR   STRING; 394.NGR_c06460; -.
DR   EnsemblBacteria; ACP24439; ACP24439; NGR_c06460.
DR   GeneID; 7791872; -.
DR   KEGG; rhi:NGR_c06460; -.
DR   PATRIC; fig|394.7.peg.3459; -.
DR   eggNOG; ENOG4107QP8; Bacteria.
DR   eggNOG; COG0166; LUCA.
DR   HOGENOM; HOG000261370; -.
DR   KO; K01810; -.
DR   OMA; SFIIPDD; -.
DR   OrthoDB; POG091H04C3; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001054; 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   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; 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   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;
DR   PRODOM; C3MI91.
DR   SWISS-2DPAGE; C3MI91.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473,
KW   ECO:0000256|SAAS:SAAS00846240};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00473,
KW   ECO:0000256|RuleBase:RU000612, ECO:0000256|SAAS:SAAS00846233};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00473,
KW   ECO:0000256|RuleBase:RU000612, ECO:0000256|SAAS:SAAS00846229};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00473,
KW   ECO:0000256|RuleBase:RU000612, ECO:0000256|SAAS:SAAS00846230,
KW   ECO:0000313|EMBL:ACP24439.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   ACT_SITE    377    377       {ECO:0000256|HAMAP-Rule:MF_00473}.
FT   ACT_SITE    506    506       {ECO:0000256|HAMAP-Rule:MF_00473}.
SQ   SEQUENCE   541 AA;  58532 MW;  F3D6ADFE86F9E128 CRC64;
     MKTIVEQLKS VVSATNATDI RAAFAADPNR FSRFSTRLGD LLLDYSKCAA NDRVIDGLEA
     LAKAARIEEK RDAMFRGDII NITEERAVLH TALRNRSNRP VLVGGKDVMP DVNAVLDAMG
     AFADGIRSGA LKGATGKKIT DVINIGIGGS DLGPVMATLA LAPFHDGPRL HFVSNVDGAH
     IADTLKLLDP ETSLFIIASK TFTTIETMTN AQTARSFIAG KLGEAAVGHH FAAVSTALDK
     VAVFGIDQAR VFGFWDWVGG RYSIWSAIGL PLMIAIGKEN FGRFLDGGHA IDEHFRTAPI
     RENIPVLLGL LGFYHRNVLG YPSRAILPYD QHLSRFPAYL QQLDMESNGK GVTLDSTPVE
     FSTGPVVWGE PGTNGQHAFY QLIHQGTDII PAEFMIAANG HEKDLRHQHQ LLIANCLAQS
     EALMKGRTLD EAKAQLTSKG MDEAKADKIA PHRVFTGNRP SLTFVYDQLD PFALGRLIAL
     YEHRVFVEGA LFNINSFDQW GVELGKELAT GLLPVVEGKE SADGHDSSTA GLVAALLKAQ
     G
//

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