ID A0A031JAT2_9SPHN Unreviewed; 383 AA.
AC A0A031JAT2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:EZP70348.1};
GN ORFNames=BV97_05472 {ECO:0000313|EMBL:EZP70348.1};
OS Novosphingobium resinovorum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=158500 {ECO:0000313|EMBL:EZP70348.1, ECO:0000313|Proteomes:UP000024329};
RN [1] {ECO:0000313|EMBL:EZP70348.1, ECO:0000313|Proteomes:UP000024329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF1 {ECO:0000313|EMBL:EZP70348.1,
RC ECO:0000313|Proteomes:UP000024329};
RA Gan H.M., Gan H.Y., Chew T.H., Savka M.A.;
RT "Whole genome sequence of Novosphingobium resinovorum KF1.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:EZP70348.1}.
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DR EMBL; JFYZ01000068; EZP70348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A031JAT2; -.
DR PATRIC; fig|158500.4.peg.5546; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000024329; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR Gene3D; 3.40.50.970; -; 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 PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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); 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EZP70348.1}.
FT DOMAIN 6..53
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 159..273
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT REGION 281..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 40932 MW; F86E6F42FA4B6809 CRC64;
MPLSTRSAFG IVGDALPPFT DAIRRQNKVR WIGVRHEEGA ALAAAGQTKV TGALRSPQGP
WPVLAISGGV ATAKRGSDYL QEDDPVALFR NVGVYSEIIA SPDQAAAVIQ QAIAHAYGER
GVAHISIPPE VFAAKVPGPV PSIATLRPRL EVAPAAADIA TLAQMIGEAK TVAVLCGFGC
HAAAEELKAL SDRLNAPLMH TYRGKDILPY DDPRWIGGIG LIGGRPGVDA LHQADLMLML
GTDYPYSEFL PTKTRVVQID ERAFALGRRT PVARHRRIGA PGLAHAARRP AAAKRHRLSE
RGEGQPREVG RDAGRKGRAR SIARPAAPAG HRPRGQRSCR RGRGVGNGHR RGHAVGGELA
APERAPADHR LVQQCRRRHR HGA
//