ID B4CX94_9BACT Unreviewed; 454 AA.
AC B4CX94;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Thiamine pyrophosphate protein central region {ECO:0000313|EMBL:EDY20892.1};
GN ORFNames=CfE428DRAFT_1185 {ECO:0000313|EMBL:EDY20892.1};
OS Chthoniobacter flavus Ellin428.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC Chthoniobacteraceae; Chthoniobacter.
OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY20892.1, ECO:0000313|Proteomes:UP000005824};
RN [1] {ECO:0000313|EMBL:EDY20892.1, ECO:0000313|Proteomes:UP000005824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY20892.1,
RC ECO:0000313|Proteomes:UP000005824};
RX PubMed=21460085; DOI=10.1128/JB.00295-11;
RA Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A.,
RA Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S.,
RA Larimer F.W., Land M.L., Hauser L., Sangwan P., de Vos W.M., Janssen P.H.,
RA Smidt H.;
RT "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic
RT heterotrophic soil bacterium.";
RL J. Bacteriol. 193:2902-2903(2011).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDY20892.1}.
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DR EMBL; ABVL01000003; EDY20892.1; -; Genomic_DNA.
DR AlphaFoldDB; B4CX94; -.
DR STRING; 497964.CfE428DRAFT_1185; -.
DR eggNOG; COG0028; Bacteria.
DR InParanoid; B4CX94; -.
DR Proteomes; UP000005824; 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 CDD; cd02014; TPP_POX; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR047211; POXB-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005824}.
FT DOMAIN 59..188
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 248..403
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 454 AA; 50011 MW; 353D80E508BFBAF1 CRC64;
MVDRSIRIAM AERTVTCIIL PNDLQELEAM ETPPRKHGTV HSGAGYSSPR IIPKDVDLHR
AADVLNAGEK VAMLVGAGAL GATDEVIQVA DLLGAGVSKA LLGKAVIPDD LPYCCGPIGL
LGSKPSWDLM MECDTLFMVG SSFPYSEFLP QEGKARGVQI EIDPKLVSIR FPMEVSLIGD
SAETLRALIP LLKRKTDRSW RERIEKGIKE WWEVLEARAM NDANPINPQR VFWELSKRLP
DRCILSSDSG SAANWYARDI KIRRGMMASL SGNLATMGPG VPYAIAAKFA FPDRVAIALV
GDGAMLMNGI NELVTIAHEW KNWSDPRLIV LVLANRDLNQ VTWEQRVMMG DPKYNPSQIV
PEFGFARYAE LLGLEGIRVE KPDQIGPAWD RALSANRPVV YEVLTDPEVP PLPPHITFEQ
AVKFSESLIR DTSAPAMIRG AFKDAVESLI PHKS
//