ID H0FBI9_9BURK Unreviewed; 590 AA.
AC H0FBI9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Thiamine pyrophosphate protein {ECO:0000313|EMBL:EHK64454.1};
GN ORFNames=KYC_20729 {ECO:0000313|EMBL:EHK64454.1};
OS Achromobacter arsenitoxydans SY8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK64454.1, ECO:0000313|Proteomes:UP000003113};
RN [1] {ECO:0000313|EMBL:EHK64454.1, ECO:0000313|Proteomes:UP000003113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8 {ECO:0000313|EMBL:EHK64454.1,
RC ECO:0000313|Proteomes:UP000003113};
RX PubMed=22328747; DOI=10.1128/JB.06667-11;
RA Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.;
RT "Genome sequence of the highly efficient arsenite-oxidizing bacterium
RT Achromobacter arsenitoxydans SY8.";
RL J. Bacteriol. 194:1243-1244(2012).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:EHK64454.1}.
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DR EMBL; AGUF01000064; EHK64454.1; -; Genomic_DNA.
DR RefSeq; WP_008165894.1; NZ_AGUF01000064.1.
DR AlphaFoldDB; H0FBI9; -.
DR STRING; 477184.KYC_20729; -.
DR PATRIC; fig|477184.5.peg.4075; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000003113; 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 CDD; cd07039; TPP_PYR_POX; 1.
DR Gene3D; 3.40.50.970; -; 2.
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; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_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 Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 590 AA; 63719 MW; D961E3E6807EF1E1 CRC64;
METVSDFVLK RLSQWGVQRV FGYPGDGING LIGAFGRTRE PLEFIQARHE ESAAFMACAH
AKFTGQVGVC LATSGPGAIH LLNGLYDAKL DHQPVVALVG QQARSALGGD YQQEVDLVSL
FKDVAHDFVQ MVTTAEQARH MVDRAMRIAM ERRSVTCVIF PNDVQDLPAV DAPPRAHGTV
HTGIGVTSHA AVPEPAALRN AADILNAGER VSILAGAGAL DAGQPLAEVA GLLGAGVAKA
LLGKAVLPDS LPYVTGAIGL LGTQPSWDMM NECDTLLMVG TSFPYAEFLP QEGQARAVQI
DRDGRKLSLR YPVEVGLVGD SRLTLQALIP LLEPKKSRRW RERIEKQVAG WRETVHARAM
VDAAPLNPQR PFLELSKRLP SHAIVTCDSG SAANWYARDI DLREGMMGSV SGGLATMGCG
VPYAVAAKLA YPDRPVIALV GDGAMQMLGI NELITIAHRW KDWRNPTLVV LVLNNGDLNL
VTWEQRVMGG DPRFADSQWL PKFSYADYGR LLGLEGIRVD SPDEVGPAWD RALSATRPVV
LEMVTDPEMP PLPPHIPAKQ IAAYFKSLRK EEAAAGGAAL RATIKQWWAG
//
