(data stored in ACNUC7421 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   08-MAY-2019, entry version 30.
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.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73257.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73257.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73257.1,
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   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes
CC       stereospecifically the conversion of dihydroxyacetone phosphate
CC       (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000256|HAMAP-
CC       Rule:MF_00147}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone
CC         phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00147, ECO:0000256|RuleBase:RU363013,
CC         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   Proteomes; UP000002034; Chromosome.
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   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147,
KW   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,
KW   ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00728672};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00498630,
KW   ECO:0000313|EMBL:ADP73257.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00147}.
FT   REGION        9     11       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00147}.
FT   REGION      234    235       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00147}.
FT   ACT_SITE     95     95       Electrophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
FT   ACT_SITE    167    167       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
FT   BINDING     173    173       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00147}.
FT   BINDING     213    213       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
FT   MOD_RES     213    213       Phosphoserine. {ECO:0000256|HAMAP-Rule:
FT                                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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