ID A0A0J1DAT9_9BURK Unreviewed; 594 AA.
AC A0A0J1DAT9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KLU36237.1};
GN ORFNames=AB595_13390 {ECO:0000313|EMBL:KLU36237.1};
OS Massilia sp. WF1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1406431 {ECO:0000313|EMBL:KLU36237.1, ECO:0000313|Proteomes:UP000036336};
RN [1] {ECO:0000313|Proteomes:UP000036336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF1 {ECO:0000313|Proteomes:UP000036336};
RA Lou J., Gu H., Wang H., Xu J.;
RT "High quality genome sequence of a efficient PHE-degrading Massilia sp.
RT strain WF1, isolated from a polycyclic aromatic hydrocarbons (PAHs)
RT contaminated soil.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KLU36237.1}.
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DR EMBL; LELH02000014; KLU36237.1; -; Genomic_DNA.
DR RefSeq; WP_047825462.1; NZ_LELH02000014.1.
DR AlphaFoldDB; A0A0J1DAT9; -.
DR PATRIC; fig|1406431.3.peg.1643; -.
DR Proteomes; UP000036336; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000036336};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..541
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 594 AA; 65157 MW; 747A6185566D16B5 CRC64;
MSKTVGDFFV ERLYDWGVRT IFGYPGDGIN GVLGALQRSK KKIEFIQVRH EEMAAFMASA
HAKFTGQPGV CLSTGGPGAS HMVTGLYDAK MDHMPVLAIC GQAPRTARGA HYTQELNLDR
LFQDVADYVY EAEAPSQVRH LVDRAMRTVL GRNGIGVLIL PGDLQELPYE EPPRKHGSVQ
SGIGYAKPRV VPHDIDLRRA AEVLNAGKKV AILVGAGALH ATDEVIAVAD RLQAGAAKAL
LGKAALPDDL PWVTGSIGIL GTKASWELMT HCDTLLMIGS GFPYAEFLPE EGKARAVQID
IDPTMLSIRY PAEVNLHGDS AETLRLLLPL LEQKSGDWRR QVESEVQDSW KLLENRALVR
ANPINPQRVA WELSPQLPVD AIVTSDSGSC ANWYARDLRV RRGQMYSLSG GLASMGAAVP
YAIAAKFAHS ERPVIAMVGD GAMQMNNMAE LITVSKYWRL WKDPRWIVCV FNNGDLNQVT
WEQRVMEGDP KFEATQKIPD VPYHKFGELI GLKGIYCDNP EEVAIAWREA LAADRPVVLE
FKTDPEVPPL PSHITLEQAK SFMETVVKGD PKEGSMLAGV ARQVLSGILP KDKS
//
