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Database: UniProt
Entry: A0A0P1IFR1_9RHOB
LinkDB: A0A0P1IFR1_9RHOB
Original site: A0A0P1IFR1_9RHOB 
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
//
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