(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIZ3_GEOS0

ID   A0A0F6BIZ3_GEOS0        Unreviewed;       449 AA.
AC   A0A0F6BIZ3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 25.
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=GY4MC1_0562 {ECO:0000313|EMBL:ADP73394.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73394.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73394.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73394.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-glucose 6-phosphate = keto-D-fructose 6-
CC         phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57579,
CC         ChEBI:CHEBI:57584; EC=5.3.1.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00473, ECO:0000256|RuleBase:RU000612,
CC         ECO:0000256|SAAS:SAAS01116370};
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:SAAS00981160}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|HAMAP-
CC       Rule:MF_00473, ECO:0000256|RuleBase:RU000612,
CC       ECO:0000256|SAAS:SAAS00846234}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00473}.
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DR   EMBL; CP002293; ADP73394.1; -; Genomic_DNA.
DR   RefSeq; WP_003248364.1; NC_014650.1.
DR   EnsemblBacteria; ADP73394; ADP73394; GY4MC1_0562.
DR   GeneID; 29236784; -.
DR   KEGG; gmc:GY4MC1_0562; -.
DR   KO; K01810; -.
DR   OMA; KMTEWGI; -.
DR   OrthoDB; 417261at2; -.
DR   BioCyc; GSP581103:G1GOQ-611-MONOMER; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
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; 2.
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; A0A0F6BIZ3.
DR   SWISS-2DPAGE; A0A0F6BIZ3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473,
KW   ECO:0000256|SAAS:SAAS00981142};
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:ADP73394.1}.
FT   ACT_SITE    425    425       {ECO:0000256|HAMAP-Rule:MF_00473}.
SQ   SEQUENCE   449 AA;  50380 MW;  7DA5B81D912FFF31 CRC64;
     MTHIRFDYSK ALAFFGEHEL TYLRDAVKVA HHSLHEKTGV GNDFLGWIDL PVNYDKEEFA
     RIQKAAAKIQ ADSDVLLVIG IGGSYLGARA AIEMLHHSFY NALSKEKRRT PQIIFVGNNI
     SSTYMKDVMD LLEGKDFSIN VISKSGTTTE PAIAFRIFRK LLEEKYGKEE ARKRIYATTD
     RARGALKTLA TAEGYETFII PDDVGGRYSV LTAVGLLPIA VSGANIEEMM KGAAQAREDF
     SNSELEENAA YQYAAIRNIL YNKGKTIELL INYEPALQYF AEWWKQLFGE SEGKDQKGIF
     PASANFSTDL HSLGQYIQEG RRDLFETVLK VEKPRHELVI EAEENDLDGL NYLAGKTVDF
     VNTKAFEGTL LAHTDGGVPN LVITLPELNE YTFGYLVYFF EKACAMSGYL LGVNPFDQPG
     VEAYKVNMFA LLGKPGYEEK KAELEKRLK
//

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