ID S9S9F7_9RHOB Unreviewed; 568 AA.
AC S9S9F7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Thiamine pyrophosphate-requiring enzyme {ECO:0000313|EMBL:EPX82899.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:EPX82899.1};
GN ORFNames=ruthe_03124 {ECO:0000313|EMBL:EPX82899.1};
OS Rubellimicrobium thermophilum DSM 16684.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX82899.1, ECO:0000313|Proteomes:UP000015346};
RN [1] {ECO:0000313|EMBL:EPX82899.1, ECO:0000313|Proteomes:UP000015346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX82899.1,
RC ECO:0000313|Proteomes:UP000015346};
RX PubMed=24501632; DOI=10.4056/sigs.4247911;
RA Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL Stand. Genomic Sci. 8:480-490(2013).
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:EPX82899.1}.
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DR EMBL; AOLV01000038; EPX82899.1; -; Genomic_DNA.
DR RefSeq; WP_021099181.1; NZ_KE557324.1.
DR AlphaFoldDB; S9S9F7; -.
DR STRING; 1123069.ruthe_03124; -.
DR PATRIC; fig|1123069.3.peg.3097; -.
DR HOGENOM; CLU_013748_4_0_5; -.
DR OrthoDB; 7534569at2; -.
DR Proteomes; UP000015346; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000015346};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:EPX82899.1}.
FT DOMAIN 6..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 208..336
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 426..563
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 568 AA; 60731 MW; A8876B83EC997C31 CRC64;
MTRYQDGGEA LLEAFRALGV EHVFCSSGSE WAPVWEAFTR QTVEGRKGPA YHDLMHETLA
VDMAIGYALV TGRMQAVLLH AVPGLLQGAC GLHGALLSEV PVLVLSSEAN SYGERLGLDP
GSQWYRNLSI VGGPHSVVDR IAKWSCQVPG IETLHEFVKR AGEIARRVPA GPVYLNVPVE
VLLQPWSPPD RRGPVAPPGR RMPPEEEIRA LVAAIRAARS PIIVTESIGR RPGGLAALLR
FAEAFGLPVY ESQATVSCNF PRSHPLFQGS AVEAQRGKAD LVLLVCARAP WYPPSQGFPG
ARVIVIDEVP QRPYMVYQVL QADAYLEGDV PATLQAAAAM AAASGLPGDA DPLAVRQASA
AEGHRRLVEG WARLEAEAAG EEGISPIHLA ACLRKALPAG SMILDETITH GRIVRDHVRP
EDEGSYSYVQ GGLGQGLGVA LGAKLAAPDR FVVLTVGDGS FLYNPIVQAL SASRQMGLPV
LTVVFNNRQY LSMKMNHLRF YPDGQSVEHG LFHGVDLSDQ PDLATVARAC GVEGLRIADP
AGLPGAIGDA IAHVRSGRSC VLDVHVNR
//