ID A0A0T5NPY9_9RHOB Unreviewed; 563 AA.
AC A0A0T5NPY9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KRS10828.1};
GN ORFNames=XM53_18985 {ECO:0000313|EMBL:KRS10828.1};
OS Roseovarius atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1641875 {ECO:0000313|EMBL:KRS10828.1, ECO:0000313|Proteomes:UP000051295};
RN [1] {ECO:0000313|EMBL:KRS10828.1, ECO:0000313|Proteomes:UP000051295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R12B {ECO:0000313|EMBL:KRS10828.1,
RC ECO:0000313|Proteomes:UP000051295};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius sp.R12b.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KRS10828.1}.
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DR EMBL; LAXJ01000026; KRS10828.1; -; Genomic_DNA.
DR RefSeq; WP_057796360.1; NZ_LAXJ01000026.1.
DR AlphaFoldDB; A0A0T5NPY9; -.
DR STRING; 1641875.XM53_18985; -.
DR PATRIC; fig|1641875.4.peg.2328; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000051295; 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; 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:SF13; 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}.
FT DOMAIN 5..123
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 400..546
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 563 AA; 60185 MW; 83EC32DC7A4F4FD6 CRC64;
MSNSMTGAQA MVRSLEAHGV RHIFGLCGDT TLPFYDAMLQ LDHPISHVLT RDERSATYMA
DAYSRVTGRV GVCEGPSGGG ATYILPGLIE ASESSYAVLG ITTDVSVASY GRYPLTEVDQ
EALMRPLTKW NTVIKRADHI PRMVRQAFRA MTTGRSGAAH LGLPYDIQYD DVPADDVWAD
PQLASYPAYR TGPEQGAVEA ALDAILSAKS PLIVCGGGVV ISGGMEELDR LATRLDITVA
TSISGQGSLA ETHPNCLGVV GSNGGTDETW EAMANADLVV FMGCRAGSTT TSRWEAPKPG
TRVVHCDVDP MVIGAVLPTE VGVVGDLRMT LAAMNAELDR RGQGADTFGG AAAIADIHKR
KFDKFRALAQ SDATPIKPER VIATLQAVLP EDATVVSDPG TSCPYFSSYY QLPKPGRHFI
TNRAHGALGY ALSASLGAWF GRPTSKVVGL MGDGSFGFTC GELETVTRCR APITYIVFSN
ANFGWIKASQ HDDCGARYYN VDFNRVDQAA VAAAYGVKSW RVEDPAKLEG VLREAIAHDG
PTLVDIVCQP LEEAKAPVRR WMG
//
