ID X7FAR2_9RHOB Unreviewed; 539 AA.
AC X7FAR2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ETX29808.1};
GN ORFNames=RISW2_21395 {ECO:0000313|EMBL:ETX29808.1};
OS Roseivivax isoporae LMG 25204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX29808.1, ECO:0000313|Proteomes:UP000023430};
RN [1] {ECO:0000313|EMBL:ETX29808.1, ECO:0000313|Proteomes:UP000023430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX29808.1,
RC ECO:0000313|Proteomes:UP000023430};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:ETX29808.1}.
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DR EMBL; JAME01000007; ETX29808.1; -; Genomic_DNA.
DR RefSeq; WP_043768182.1; NZ_JAME01000007.1.
DR AlphaFoldDB; X7FAR2; -.
DR STRING; 1449351.RISW2_21395; -.
DR PATRIC; fig|1449351.3.peg.1315; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000023430; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:SF129; ACETOLACTATE SYNTHASE; 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:UP000023430};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 539 AA; 55719 MW; 8157DF93464E7573 CRC64;
MTEPVLRSAD VLARRLYDAG VRRAFGMPGG EVLTLVDALE AAGIGFVLVR HENSGGFMAE
GMHHATGAPA VLVATVGPGA LNAINAVENA RQDRVPMIVL TGCVDPETAA RYTHQVLDQG
RVFAAVAKAS FTLAAGAAEV TIDKALAIAT DGRPGPVHID VPISVADAPA EARPDLRRRP
ALPVAPARGP GLDAARAALA GAERPLIVAG VDAVNGGAAE ALRAAAEALG APVVTTYKAK
GLLPEDHPLA LGGAGLSPRA DAILLPLVRA ADAILLAGYD PIEMRTGWQD PWDPDAVPVV
DVTAEPNLHY MHQGSVNVVG AIGPSLAALT EGATPAAGWG GRVAETRAAL DAAFAPEEAW
GPAAVIETCR QVLPPETRAS ADSGAHRILL SQMWRCSYPR ALVQSSGLCT MGCAVPLAMG
AQLAEPDRPC VSFSGDAGFL MVAGELATAA DLGLRTIFVV FVDRSLALIE LKQRQRQMRN
AGVDFGRTDF AALGRAMGGA GHVVTSREAL RAALEAALEA ETFTVIAAEI DRRAYDGRI
//
