ID A0A1I3KSF6_9BRAD Unreviewed; 541 AA.
AC A0A1I3KSF6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acetolactate synthase, large subunit {ECO:0000313|EMBL:SFI75471.1};
GN ORFNames=SAMN05216525_11377 {ECO:0000313|EMBL:SFI75471.1};
OS Bradyrhizobium sp. Gha.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855318 {ECO:0000313|EMBL:SFI75471.1, ECO:0000313|Proteomes:UP000199284};
RN [1] {ECO:0000313|EMBL:SFI75471.1, ECO:0000313|Proteomes:UP000199284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gha {ECO:0000313|EMBL:SFI75471.1,
RC ECO:0000313|Proteomes:UP000199284};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FOQM01000013; SFI75471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3KSF6; -.
DR STRING; 1855318.SAMN05216525_11377; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000199284; 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..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..522
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 541 AA; 57720 MW; 4AD95644F12F0DD8 CRC64;
MTTLTGGEAI VSGLVAHGVD TVFGLPGAQV YGLFDAFHQA QLKVIGARHE QACGYMAFGY
ARSSGKPGVF SVVPGPGVLN ASAALLTAFG CNEPVLCVTG QVPTQFLGKG RGHLHEMPDQ
LATLRSYVKW ADRIEHPGNA PTTVARAFQE MTSGRRGPAS VEMPWDIFTQ RAETGAAQVL
APLPAPQPDP DMVKQAAALI KASKAPMIFV GSGAIEAREE ILELAEMIDA PVVAFRSGRG
IVSNAHELGL TMAAAYKLWP KTDLMIGIGT RLELPTMSRW PYRPDGLKSI RIDIDPVEMR
RYPSNAAIVA DAKAATADLA AAVSKAGYSK NPGRRAAIRE ASAGALAEIQ RVQPQMAYLN
ILREVLPANA IVTDELSQFG FASWYGFPVY QPRTFITSGY QGTLGSGFPT ALGAKVANPD
KPVVAITGDG GFMFGVQELA TAVQFNIGVV TLVFNNNAYG NVRRDQRERF DGRVVASDLV
NPDFVKLAES FGVASARVTA PDQFKVAMEK ALAHGGPYLI SVEVTRDSEV SPWAFIHPPK
P
//