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Database: UniProt/TrEMBL
Entry: G8LY95_CLOCD
LinkDB: G8LY95_CLOCD
Original site: G8LY95_CLOCD 
ID   G8LY95_CLOCD            Unreviewed;       251 AA.
AC   G8LY95;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   26-NOV-2014, entry version 21.
DE   RecName: Full=Triosephosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU000517};
DE            Short=TIM {ECO:0000256|HAMAP-Rule:MF_00147};
DE            EC=5.3.1.1 {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU000517};
DE   AltName: Full=Triose-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147};
GN   Name=tpiA {ECO:0000256|HAMAP-Rule:MF_00147};
GN   OrderedLocusNames=Clocl_1154 {ECO:0000313|EMBL:AEV67826.1};
OS   Clostridium clariflavum (strain DSM 19732 / NBRC 101661 / EBR45).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=720554 {ECO:0000313|EMBL:AEV67826.1, ECO:0000313|Proteomes:UP000005435};
RN   [1] {ECO:0000313|Proteomes:UP000005435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19732 / NBRC 101661 / EBR45
RC   {ECO:0000313|Proteomes:UP000005435};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Kitzmiller T., Lynd L.,
RA   Izquierdo J., Woyke T.;
RT   "Complete sequence of Clostridium clariflavum DSM 19732.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|RuleBase:RU000517, ECO:0000256|SAAS:SAAS00021144}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU003527,
CC       ECO:0000256|SAAS:SAAS00017448}.
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:RU003527,
CC       ECO:0000256|SAAS:SAAS00017428}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00147,
CC       ECO:0000256|SAAS:SAAS00017485}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU004162}.
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DR   EMBL; CP003065; AEV67826.1; -; Genomic_DNA.
DR   RefSeq; YP_005045750.1; NC_016627.1.
DR   ProteinModelPortal; G8LY95; -.
DR   EnsemblBacteria; AEV67826; AEV67826; Clocl_1154.
DR   GeneID; 11561523; -.
DR   KEGG; ccl:Clocl_1154; -.
DR   KO; K01803; -.
DR   BioCyc; CCLA720554:GI2T-1152-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-HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00147_B; TIM_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005435};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU003527};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU003527};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU000517};
KW   Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00147,
KW   ECO:0000256|RuleBase:RU003527};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005435}.
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      10     10       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
FT   BINDING      12     12       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00147}.
SQ   SEQUENCE   251 AA;  27131 MW;  742008FDECF0C3DE CRC64;
     MSRVKIAAGN WKMNKTAKEA VEFVEALKPR VADADAEVVV GVPFVCIPGV KKAVEGSNIK
     VAAQNIHWEE KGAFTGEVSG PMLADLGVDY VIIGHSERRQ YFAETDETVN KKAHAVFKYG
     MKPIICVGES LTQREQGVTA ELVRYQVKIA LLGLTAEQVK ETVIAYEPIW AIGTGKTATT
     EQAEEVCAII RNVVKELYGD DVAQAIRIQY GGSVNAANAA ELFAMPNIDG GLVGGASLKL
     DDFEKIAKYN K
//
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