(data stored in SCRATCH zone)

SWISSPROT: A0LEZ5_SYNFM

ID   A0LEZ5_SYNFM            Unreviewed;       568 AA.
AC   A0LEZ5;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   SubName: Full=Thiamine pyrophosphate enzyme TPP binding domain protein {ECO:0000313|EMBL:ABK15997.1};
GN   OrderedLocusNames=Sfum_0296 {ECO:0000313|EMBL:ABK15997.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15997.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15997.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) 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; CP000478; ABK15997.1; -; Genomic_DNA.
DR   STRING; 335543.Sfum_0296; -.
DR   PRIDE; A0LEZ5; -.
DR   EnsemblBacteria; ABK15997; ABK15997; Sfum_0296.
DR   KEGG; sfu:Sfum_0296; -.
DR   eggNOG; ENOG4105CFN; Bacteria.
DR   eggNOG; COG0028; LUCA.
DR   HOGENOM; HOG000010642; -.
DR   KO; K01652; -.
DR   OMA; IRIIDVR; -.
DR   BioCyc; SFUM335543:G1G7I-301-MONOMER; -.
DR   Proteomes; UP000001784; 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   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; IPR000399; TPP-bd_CS.
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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LEZ5.
DR   SWISS-2DPAGE; A0LEZ5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN       25    192       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      214    340       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      402    550       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   568 AA;  61384 MW;  DF3E8CE0F72E334F CRC64;
     MGSADPFFNN FRTHSKEETQ MAGLTGGKLV AKTLATEGVQ AIFTLCGAHV MDIYSGCLDE
     GIRIIDVRHE QTAAHAADAW TRLTGVPGVA VVTAGPGVTD AVTGVANAYR AQVPMLLIGG
     QAPIRNLLKG GLQEMNSVDM MRPITKFSGT VFDTVRIPEM IGLALREACN GRPGPSFLEI
     PQDVLDREVE ENEVRVPVQS RSQCRLTGDR KLMARAAGLL AKAQRPALIA GTQVWSCRAV
     EQLRLFVERA GIPTYLNGAA RGCLPVDSPH AFNRTRKFAL SKADVVLVIG TPFDFRLGYG
     SRIAEGAKII QVDLDYAELC HNRDVEVAIQ ADAGAFLEEL EGAVSPAGGT RKWLDELRTM
     ETELLERESR FLSSDAVPIH PLRLAREIDA FLRDDSILIA DGGDTVTMSA SVIRPRGPGQ
     WLDPGPLGTL GVGTPFAIAA KAAMPARDVV VLFGDGAFGL TGFDYDTLIR FNLPMVGIVA
     NNGAWNQVRY VQLLKYGPQK GNTANLLHSL RYDRIIEAMG GHGEHVTEPG EIRAALDRAR
     NSGKPACVNV LVDRETFSSS TRDLTIYK
//

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