ID W0V8E9_9BURK Unreviewed; 567 AA.
AC W0V8E9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Thiamine pyrophosphate enzyme, C-terminal TPP binding domain protein {ECO:0000313|EMBL:CDG85094.1};
GN ORFNames=GJA_4487 {ECO:0000313|EMBL:CDG85094.1};
OS Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG85094.1, ECO:0000313|Proteomes:UP000027604};
RN [1] {ECO:0000313|EMBL:CDG85094.1, ECO:0000313|Proteomes:UP000027604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604};
RX PubMed=25883287; DOI=10.1128/genomeA.00277-15;
RA Graupner K., Lackner G., Hertweck C.;
RT "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium
RT agaricidamnosum.";
RL Genome Announc. 3:e00277-e00277(2015).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; HG322949; CDG85094.1; -; Genomic_DNA.
DR RefSeq; WP_038496111.1; NZ_HG322949.1.
DR AlphaFoldDB; W0V8E9; -.
DR STRING; 1349767.GJA_4487; -.
DR KEGG; jag:GJA_4487; -.
DR PATRIC; fig|1349767.4.peg.1128; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_4; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000027604; Chromosome I.
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; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 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; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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:UP000027604};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 567 AA; 61082 MW; BFA75300E4AE8026 CRC64;
MTQPSRTGGQ ILVDALQVHG VDTAFGVPGE SYLDVLDALH DSGIRFIINR QEGGAAFMAE
AYGKLTGKPG ICFVTRGPGA TNASIGVHTA YQDSTPMILF IGQVGNDFMD REAFQEVDYR
RMYGQMAKWV TQIDRAERIP EYLARAFQVA TSGRPGPVVL ALPEDMLITL ASVADTRPYQ
PVQASPSAAQ IGQLRAMLAT AKNPLVLLGG TVWTERACAD LQRFAEANAL PVACAFRFQD
LLDNAHPNYV GDVGIGINPT LAARIRNADL ILAIGPRLGE MTTSGYTLIA APVPQQRLVH
FHADAEELGS VYQAELMINS GMPQAAAMLA AMEPVDAGAW RHTVAEARAE LAAWQQQPPV
FHDGAAPLNL WQVVQDIMAQ APRDTIITNG AGNYASWAHR FYRYGGMRTQ LAPTNGAMGY
GLPAGVAAKI AAPERTVITF AGDGEYMMNG QELATAVQYR AGLVVIVFNN QMYGTIRMHQ
ERDYPGRVSG TTLHNPDFAA LAQAYGGHGE VIDTTEQFAA ALARALAFAN EKQLPALIEL
RYDGNLITPN TTLDSIRRNA EAALAAR
//
