ID A0A0P1IFR1_9RHOB Unreviewed; 593 AA.
AC A0A0P1IFR1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:CUK10568.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CUK10568.1};
GN Name=ilvB_2 {ECO:0000313|EMBL:CUK10568.1};
GN ORFNames=RUE5091_03331 {ECO:0000313|EMBL:CUK10568.1};
OS Ruegeria denitrificans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1715692 {ECO:0000313|EMBL:CUK10568.1, ECO:0000313|Proteomes:UP000051260};
RN [1] {ECO:0000313|EMBL:CUK10568.1, ECO:0000313|Proteomes:UP000051260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5091 {ECO:0000313|EMBL:CUK10568.1,
RC ECO:0000313|Proteomes:UP000051260};
RG Swine Surveillance;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CYUD01000010; CUK10568.1; -; Genomic_DNA.
DR RefSeq; WP_058282988.1; NZ_CYUD01000010.1.
DR AlphaFoldDB; A0A0P1IFR1; -.
DR STRING; 1715692.RUE5091_03331; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000051260; 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; 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: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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUK10568.1}.
FT DOMAIN 10..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 207..342
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 409..563
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 593 AA; 63739 MW; F49D5581BB804B03 CRC64;
MDGAKLEGKT VAEHIVDFLE RREVKHVFGL CGHTNIAVLA ALAESPIDFV TVRHEQIASH
AADAYARVTG TASVVLSHLS PGLTNCATGV ANAALDCIPM VVIAGDIPTH YYGKHPHQEV
NLHADAAQWE IYRPFVKRAW RVDRADLMAE ILEKAFHLAE SGQPGPVLVN VPMDIFSEVI
SSDSFDRIRD NTRALKKPSI DDETACEIVE ALAKAKNPVA YVGGGILLAQ ASEELREFVE
HMGLPVAHSL MGKGALRDDH PLVLGMTGFW GTELVNQSCL NADYIFAVGT RFKEADCSSW
YPGYTFNIPG SKVIHIDIEP QEIGRNYPTE IGVVADAKAA FRVLNRVARE MYPDGFKRPA
LEQQITNFRT EFKARNVEMA TSSAFPMMPE RILADTRKAL PKDAIITTDV GWNKNGVGQQ
FDILTPGSIL TPGGFATMGF GPPGAIGAKL AAPDRVVLSL VGDGGFGQNP SMLATAVELD
LGIIWLVMNN NAFGTIAGLQ KAHYGLTYGT TFPGSAAAPA NGPGYSDIAR AYGAEGHRLS
AADELLPALE AAIASGKPTV LDVPMINNPT PTTGHWNILD IYSPDRDVSH VAT
//