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Database: UniProt
Entry: A0A0T5PDJ9_9RHOB
LinkDB: A0A0T5PDJ9_9RHOB
Original site: A0A0T5PDJ9_9RHOB 
ID   A0A0T5PDJ9_9RHOB        Unreviewed;       575 AA.
AC   A0A0T5PDJ9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acetolactate synthase isozyme 3 large subunit {ECO:0000313|EMBL:QEW25800.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:QEW25800.1};
GN   Name=ilvI_1 {ECO:0000313|EMBL:QEW25800.1};
GN   ORFNames=RIdsm_01589 {ECO:0000313|EMBL:QEW25800.1}, XM52_06155
GN   {ECO:0000313|EMBL:KRS19229.1};
OS   Roseovarius indicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS19229.1, ECO:0000313|Proteomes:UP000051401};
RN   [1] {ECO:0000313|EMBL:KRS19229.1, ECO:0000313|Proteomes:UP000051401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B108 {ECO:0000313|EMBL:KRS19229.1,
RC   ECO:0000313|Proteomes:UP000051401};
RA   Li G., Lai Q., Shao Z., Yan P.;
RT   "The draft genome sequence of Roseovarius indicus B108T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QEW25800.1, ECO:0000313|Proteomes:UP000325785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26383 {ECO:0000313|EMBL:QEW25800.1,
RC   ECO:0000313|Proteomes:UP000325785};
RA   Vollmers J., Petersen J.;
RT   "Genetic Globetrotter - A new plasmid hitch-hiking vast phylogenetic and
RT   geographic distances.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; LAXI01000002; KRS19229.1; -; Genomic_DNA.
DR   EMBL; CP031598; QEW25800.1; -; Genomic_DNA.
DR   RefSeq; WP_057814287.1; NZ_LAXI01000002.1.
DR   AlphaFoldDB; A0A0T5PDJ9; -.
DR   STRING; 540747.SAMN04488031_1033; -.
DR   KEGG; rid:RIdsm_01589; -.
DR   PATRIC; fig|540747.5.peg.2817; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000051401; Unassembled WGS sequence.
DR   Proteomes; UP000325785; Chromosome.
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   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; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF13; 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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051401};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:QEW25800.1}.
FT   DOMAIN          13..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          214..349
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          405..550
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   575 AA;  59977 MW;  CF513DBEDF824A10 CRC64;
     MTCQPLYDAP VAAADAIVDT LIAAGIKHVF GLSGGHTGRI FGALEKRQEK IRTILVREES
     LGAVMAETIG RITGAPSVLL GQGPWVLGNG LLGTIEAHLS ATPLLLLTDF SDTPGASLHA
     PYQSGTGEYG NWDARQAFGA VTKEVFTAED PNSAVVATQL AIKHACSGEP GPVAMLLGLR
     ALDGEARPEA APRIYPAEAF IAPPLRGVPE LTASLAALQG AARPLIIAGN GIRVGRAEAA
     LMRFAEACGI PVVTSPSGKG VFDEDHVLSC GVYGGYGNPL AHRAVAGADV ILAIGTKLSA
     SDTNNGDTGL IDPSRQTLIQ VDIEPRNLSW TIPVAHPLLG DAATILDALR TGWTAAAHET
     WTAALNTPRH VSLPASDAGA AAIHPHEIIA TMQEILPRET IYTCDAGENR IFMLHFLRPR
     GAGRFIQPAG AGPMGYALPS AMARKLLSPE NPVVAFSGDG GFSMTMNGLI TAIEAALPII
     SVVMNNDALG WSQHSRGPFA TQFSRVDYAA IARGMGCAGF HASGIEPLKE ALAAALRVTQ
     EEQRPAVIDV EASMEVSFAR LAYSETSETR GLAAD
//
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