(data stored in ACNUC7421 zone)

SWISSPROT: C3MFU8_SINFN

ID   C3MFU8_SINFN            Unreviewed;       537 AA.
AC   C3MFU8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 52.
DE   SubName: Full=Predicted thiamine pyrophosphate protein, TPP binding domain protein {ECO:0000313|EMBL:ACP23999.1};
GN   OrderedLocusNames=NGR_c01990 {ECO:0000313|EMBL:ACP23999.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23999.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23999.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP001389; ACP23999.1; -; Genomic_DNA.
DR   RefSeq; WP_012706784.1; NC_012587.1.
DR   RefSeq; YP_002824752.1; NC_012587.1.
DR   ProteinModelPortal; C3MFU8; -.
DR   STRING; 394.NGR_c01990; -.
DR   EnsemblBacteria; ACP23999; ACP23999; NGR_c01990.
DR   GeneID; 7790777; -.
DR   KEGG; rhi:NGR_c01990; -.
DR   PATRIC; fig|394.7.peg.2996; -.
DR   eggNOG; ENOG4105C7K; Bacteria.
DR   eggNOG; COG0028; LUCA.
DR   HOGENOM; HOG000258446; -.
DR   KO; K01652; -.
DR   OMA; IRIIDVR; -.
DR   OrthoDB; POG091H02KO; -.
DR   Proteomes; UP000001054; 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; C3MFU8.
DR   SWISS-2DPAGE; C3MFU8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN        7    176       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      195    322       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      388    527       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   537 AA;  55888 MW;  1B42002FFFE49037 CRC64;
     MSVETKTVGE VLVDLLEANG VEVVFGIPGV HTVELYRGLA ASKIRHVTPR HEQGAGFMAD
     GYARVSGKPG VALVITGPGL TNTITAMAQA RQDSIPMLVI SGVNRRDSLG HGRGLLHELP
     DQQGMMKTLA LYSHTLINPA DLPLVVDRAF AVLLSGRPGP VHIEIPTDVM AERIESRGTK
     PAAATRPRSD GETLQRAAIL CAEASRPVIL CGGGALTAEA EVRGLAEQIG APVVTTVNAR
     GMLAGHPLRV PASPSLKAVR ALLRDADLVL ALGTEMGQTD YDLYADGGFP MLRNLIRTDI
     DAAQLARGPQ AALSVLSGAR AATAGILGFL PGHTAARDGA SRADATRKAA LKELTPKMRA
     EVGIIDLIYK ALPDCTIVGD STQAVYAGNL YCDAPRQRAW FNSATGYGSL GYAPPAAVGA
     AVADRARPVV CLVGDGGFQF SLAEIGSAVD AGARVIFLVW NNDGYREIES HMVEAGVTPE
     GVKPSAPDFL LTAGAYGVPA ERLAKIGDLP RALADAASRS GPSLIEIHQE KTAGVGG
//

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