(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIK6_GEOS0

ID   A0A0F6BIK6_GEOS0        Unreviewed;       253 AA.
AC   A0A0F6BIK6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 34.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728730};
DE            Short=TIM {ECO:0000256|HAMAP-Rule:MF_00147};
DE            Short=TPI {ECO:0000256|HAMAP-Rule:MF_00147};
DE            EC=5.3.1.1 {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728682};
DE   AltName: Full=Triose-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147};
GN   Name=tpiA {ECO:0000256|HAMAP-Rule:MF_00147};
GN   OrderedLocusNames=GY4MC1_0416 {ECO:0000313|EMBL:ADP73257.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73257.1};
RN   [1] {ECO:0000313|EMBL:ADP73257.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73257.1};
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., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   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   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically
CC       the conversion of dihydroxyacetone phosphate (DHAP) to D-
CC       glyceraldehyde-3-phosphate (G3P). {ECO:0000256|HAMAP-Rule:MF_00147}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate;
CC         Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
CC         EC=5.3.1.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00147,
CC         ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS01116239};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC       ECO:0000256|SAAS:SAAS00728615}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC       ECO:0000256|SAAS:SAAS00728661}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728692}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|RuleBase:RU363013}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC       ECO:0000256|SAAS:SAAS00728708}.
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DR   EMBL; CP002293; ADP73257.1; -; Genomic_DNA.
DR   RefSeq; WP_003248110.1; NC_014650.1.
DR   EnsemblBacteria; ADP73257; ADP73257; GY4MC1_0416.
DR   GeneID; 29236924; -.
DR   KEGG; gmc:GY4MC1_0416; -.
DR   KO; K01803; -.
DR   OMA; LCVGEGL; -.
DR   OrthoDB; 1266295at2; -.
DR   BioCyc; GSP581103:G1GOQ-463-MONOMER; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004807; F:triose-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; cd00311; TIM; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00147_B; TIM_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035990; TIM_sf.
DR   InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR   InterPro; IPR000652; Triosephosphate_isomerase.
DR   InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR   PANTHER; PTHR21139; PTHR21139; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; SSF51351; 1.
DR   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIK6.
DR   SWISS-2DPAGE; A0A0F6BIK6.
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728593};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
KW   ECO:0000256|SAAS:SAAS00728672};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
KW   ECO:0000256|SAAS:SAAS00498630, ECO:0000313|EMBL:ADP73257.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00147}.
FT   REGION          9..11
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT   REGION          234..235
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT   ACT_SITE        95
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT   BINDING         173
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT   BINDING         213
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00147"
SQ   SEQUENCE   253 AA;  27524 MW;  B82F396706AEAB85 CRC64;
     MRKRIIAGNW KMHKTLPEAV SFVEEVKRLV PPAEQVDSVI CAPFLFLDRL VQNVQGSDLK
     IGAQNMHFED KGAFTGEISP VALKDIGVAY VIIGHSERRE MFAETDETVN KKVHAAFKHG
     LIPIVCCGET LEQRESGKTN DIVGAQVEKA LAGLTAEQAK QVVIAYEPIW AIGTGKSSTA
     EDANEVCGHI RSVIAKIFSP EVAEAVRIQY GGSVKPENIR EFLAQEHIDG ALVGGASLDP
     KSFLQLVEAG QHE
//

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