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Database: UniProt
Entry: S9S9F7_9RHOB
LinkDB: S9S9F7_9RHOB
Original site: S9S9F7_9RHOB 
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
//
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