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Database: UniProt
Entry: A0A0Q5TBK2_9BACT
LinkDB: A0A0Q5TBK2_9BACT
Original site: A0A0Q5TBK2_9BACT 
ID   A0A0Q5TBK2_9BACT        Unreviewed;       568 AA.
AC   A0A0Q5TBK2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-FEB-2018, entry version 9.
DE   SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KQS28059.1};
GN   ORFNames=ASG33_16865 {ECO:0000313|EMBL:KQS28059.1};
OS   Dyadobacter sp. Leaf189.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Dyadobacter.
OX   NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS28059.1, ECO:0000313|Proteomes:UP000051810};
RN   [1] {ECO:0000313|EMBL:KQS28059.1, ECO:0000313|Proteomes:UP000051810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf189 {ECO:0000313|EMBL:KQS28059.1,
RC   ECO:0000313|Proteomes:UP000051810};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS28059.1, ECO:0000313|Proteomes:UP000051810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf189 {ECO:0000313|EMBL:KQS28059.1,
RC   ECO:0000313|Proteomes:UP000051810};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KQS28059.1}.
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DR   EMBL; LMPS01000005; KQS28059.1; -; Genomic_DNA.
DR   RefSeq; WP_056287709.1; NZ_LMPS01000005.1.
DR   EnsemblBacteria; KQS28059; KQS28059; ASG33_16865.
DR   Proteomes; UP000051810; Unassembled WGS sequence.
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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000051810};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051810};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN        5    172       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      191    327       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      403    550       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   568 AA;  62018 MW;  BAA863B1AE064F07 CRC64;
     MAGKTGNQKI IEQFLADGMD FMFGNPGTVE QGFLDALAEY PDMKYILTLQ ETIAVMMGDG
     YARATQKPTL VQLHSSPGIG NAVGAIYQAK RGHAPLVVIG SDAGVQYMNM DAQMANDLVA
     MMAPVTKYAT MATSSKSLLR TLRRAIKIAT TAPMGPVYVC LPMDVLDELN DEPVFPSCIP
     STRVLPHSDL IREAAEILLN AEKPMIFVGD GVAYSDAIPE LTKVAELLGA EVYGVEFGDV
     VMDNTHPLYQ GTTGHMFGSY SHPITTKGDV NLIVGTYMVP EVFPELGDIY APEAKVIHFD
     LNAYEIAKNH RVDLGVVSDP KLSLAELAEV LEAMISTDQM AEVIQRIEEI GTAKSEKIAK
     EKEADQQYSG SPLRMAQFSK VLAEKLNLDE TVIFDEALTS SPAVSRYIPQ KAAGQYFTTR
     GGSLGVGFPG AIGVKLANPE KTVIGFSGDG GSMYTIQTLW SAVRHNAGAK FVVCNNGSYK
     LLQLNIDQYW KEREIDKHPF PLPFDLSYPA IRFDILAQSM GVEAVRVEKE EDILPAIERM
     LADDKPFLID LVLEGDHKSD WVKVNCSQ
//
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