(data stored in SCRATCH zone)

SWISSPROT: C6AZC8_RHILS

ID   C6AZC8_RHILS            Unreviewed;       541 AA.
AC   C6AZC8;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   30-AUG-2017, entry version 63.
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=Rleg_0143 {ECO:0000313|EMBL:ACS54454.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54454.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54454.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54454.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001622; ACS54454.1; -; Genomic_DNA.
DR   RefSeq; WP_012755876.1; NC_012850.1.
DR   ProteinModelPortal; C6AZC8; -.
DR   EnsemblBacteria; ACS54454; ACS54454; Rleg_0143.
DR   KEGG; rlg:Rleg_0143; -.
DR   HOGENOM; HOG000261370; -.
DR   KO; K01810; -.
DR   OMA; TNSQHAF; -.
DR   OrthoDB; POG091H04C3; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002256; 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; C6AZC8.
DR   SWISS-2DPAGE; C6AZC8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
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:ACS54454.1}.
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;  58586 MW;  7D7DF7B98BFB7C7E CRC64;
     MNAIVEQLKS TADATKATDI RAAFATDSQR FSRFSVALDD LLMDFSKTAV NDDILKLLVK
     LAEDGGVETK REEMFSGKAI NFTEDRAVLH TALRNRSNTP VLVDGKDVMP DVNAVLAAMG
     KFADDVRSGT LKGATGKAIT DVINIGIGGS DLGPVMATLA LAPFHDGPRA HFVSNIDGAH
     IADILKLVQP ETTLFIVASK TFTTVETMTN AQTARNFIAK ALGEAAVQHH FAAVSTALDK
     VAAFGIDSAR VFGFWDWVGG RYSIWSAIGL PLMIAVGPEN FGKFLDGAHA VDNHFRKAPI
     TENLPVLLGL IGFYHRNVLG YPTRAILPYD QRLSRFPAYL QQLDMESNGK GVTIDGTPVE
     GNSGPVVWGE PGTNGQHAFY QLIHQGTSII PAEFMIAANA FEPELRHQHQ LLISNVLAQS
     EALMKGRTFA EAKKQLTDKG MDDKKADFIA PHRVFTGNRP SITFVYDKLT PYALGRLIAL
     YEHRVFVEGV LFRINSFDQW GVELGKELAT GLLPVVEGKE SAAAHDSSTQ GLVAALAKLA
     K
//

If you have problems or comments...

PBIL Back to PBIL home page