(data stored in SCRATCH zone)

SWISSPROT: A8FPL1_SHESH

ID   A8FPL1_SHESH            Unreviewed;       599 AA.
AC   A8FPL1;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 60.
DE   SubName: Full=Thiamine pyrophosphate enzyme domain protein TPP-binding {ECO:0000313|EMBL:ABV34784.1};
GN   OrderedLocusNames=Ssed_0171 {ECO:0000313|EMBL:ABV34784.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34784.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34784.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34784.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP000821; ABV34784.1; -; Genomic_DNA.
DR   RefSeq; WP_012004310.1; NC_009831.1.
DR   ProteinModelPortal; A8FPL1; -.
DR   STRING; 425104.Ssed_0171; -.
DR   EnsemblBacteria; ABV34784; ABV34784; Ssed_0171.
DR   KEGG; sse:Ssed_0171; -.
DR   eggNOG; ENOG4107RA9; Bacteria.
DR   eggNOG; COG3961; LUCA.
DR   HOGENOM; HOG000223445; -.
DR   OMA; QLPNVYG; -.
DR   OrthoDB; POG091H0FS6; -.
DR   BioCyc; SSED425104:GH7Q-174-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
PE   3: Inferred from homology;
DR   PRODOM; A8FPL1.
DR   SWISS-2DPAGE; A8FPL1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN       21    199       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      230    355       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      430    559       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   599 AA;  65478 MW;  5F20A44B6331801F CRC64;
     MSPSIKDNFG SEYYNSLPLF GDCLGELLAF FGVKRAYGVG GDFVANLINS LEGHIEVLPS
     SNEMHAGFSA CAQAELNPLG MCLTTYTVGS LPCVTAAALA RTEGLPVVFI SGAPGEAEVN
     SHALHHSVHP HTAWHTDLDA ALNSFRALGV RAERLQGQRH SGQPNIAAEQ CLELLTYAYL
     NRQPVFIEIP RDLINQPTQS LSLPLSLEQI SQNQPLSLSG AELIAQDIES KLKLANKPLV
     FLGEKLRLNR PLLSKIISLC HQHSLPYATS WFGKGMLDES EPLCLGSYNG AFSELEGKHY
     IESQADYILE LGTAIFPSDT NNAFSSQTHA IDTHSHKTML RGTARWEKDI EAVIDLLVQK
     LPLNEGAEST LDPDEKVTPP LESVMLGYHN LAETINQAQR QLAKPYIFVP EVGSSLFASF
     ELETHGSDIG RSYLANPWYA AMGTCLPYAR AIADQLAESN SLQPVLVMIG DGGFNFQANE
     LINLQKQGAN VTILYMRNNI FHLGKAGDAP IYSCNDQGFN PRLLIQAYGG DGHLCETTEQ
     LTHCLIETAH KGGVHLIEVP TSVEAGHQSE TTKKLNTYIG FRNGDPQATE RWNELCGHF
//

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