ID A0A150UA67_9BRAD Unreviewed; 542 AA.
AC A0A150UA67;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SE92_13360 {ECO:0000313|EMBL:KYG21128.1};
OS Bradyrhizobium sp. AT1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=574934 {ECO:0000313|EMBL:KYG21128.1, ECO:0000313|Proteomes:UP000075342};
RN [1] {ECO:0000313|EMBL:KYG21128.1, ECO:0000313|Proteomes:UP000075342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT1 {ECO:0000313|EMBL:KYG21128.1,
RC ECO:0000313|Proteomes:UP000075342};
RA Okubo T., Minamisawa K.;
RT "Evolution of nitrogen fixation genes.";
RL Submitted (JAN-2015) 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:KYG21128.1}.
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DR EMBL; JXDL01000001; KYG21128.1; -; Genomic_DNA.
DR RefSeq; WP_063196119.1; NZ_JXDL01000001.1.
DR AlphaFoldDB; A0A150UA67; -.
DR STRING; 574934.SE92_13360; -.
DR PATRIC; fig|574934.3.peg.2818; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000075342; Unassembled WGS sequence.
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 GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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:SF167; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVB2-RELATED; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..316
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..523
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 542 AA; 57795 MW; 99821C75A3E09F52 CRC64;
MTTLTGGEAI VSGLVAHGVD TVFGLPGAQV YGLFDAFHQA QLKVIGARHE QACGYMAFGY
ARSSGKPGVF SVVPGPGVLN ASAALLTAFG CNEPVLCVTG QVPTQFLGKG RGHLHEMPDQ
LATLRTYVKW ADRIEYPGNA PTIVARAFQE MMSGRRGPAS VEMPWDVFTQ RAATSAARVL
EPLPAPQPDP DLVKQAAALI KASKAPMIFV GSGAMEAGDE ILELAEMIDA PVVAFRSGRG
IVSNAHELGL TMAAAYKLWP KTDLMIAIGT RAELPASGFR WPYQPSGLKS IRIDIDPTEI
RRLAADAAIV ADARDGTADL VAAVKKAGYA RSHGRRGEIR EAAAAAQAEI QRIQPQMAYL
NILREVLPAN AIVTDELSQF GFASWYGFPV YEPRTFITSG YQGTLGSGFP TALGAKVANP
DKPVVAITGD GGFMFGVQEL ATAVQFNIGV VTLVFNNNAY GNVRRDQRER FDGRVVASDL
VNPDFVKLAE SFGVAAARVT APDQFKAAME KALSHGGPYL ISIEVTRDSE VSPWAFIHPP
KP
//