ID A0A3N1CXN4_9ACTN Unreviewed; 568 AA.
AC A0A3N1CXN4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:ROO86053.1};
GN ORFNames=EDD29_3614 {ECO:0000313|EMBL:ROO86053.1};
OS Actinocorallia herbida.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinocorallia.
OX NCBI_TaxID=58109 {ECO:0000313|EMBL:ROO86053.1, ECO:0000313|Proteomes:UP000272400};
RN [1] {ECO:0000313|EMBL:ROO86053.1, ECO:0000313|Proteomes:UP000272400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44254 {ECO:0000313|EMBL:ROO86053.1,
RC ECO:0000313|Proteomes:UP000272400};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) 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:ROO86053.1}.
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DR EMBL; RJKE01000001; ROO86053.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1CXN4; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000272400; 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 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000272400};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..111
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 202..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 568 AA; 61270 MW; 5C9276E4DB6A4642 CRC64;
MQVYEALVKG LESAGVDTAF GGNGENIASL AVALSRSRRI RPIMTRHEQG ASFMACGYAM
YTDRLGVCFA TVGPGAFNLF TGLAVALSDS YPVLALTGYV ALDWQGRGAV NDTSGRNGTP
DSQAMFAATT KRSYLLTDPA DTCDVLEEAI NVAFEGRPGP VHLHVPQNLA EHGVRVDYRD
PVIEVKPVRP DPARVEEIAD VLADALREGR RIVVLAGFGT IRAHAEAAML RFVERFQIPL
LTTLDGKGVI AETHPLAVGV FAESGHASAW KAFREADVVL AVGNSLSQHA TFGLREDLFE
GKKLLQVNIA ASEIGRFYAP DLSLVSDARL AVEAITGALE PRVGPVAPSP VVGQDYEARH
IVRLPGEIHP GLLAQTIGRM LPDRAILLAD AGAHLAWLGY HVDLEAGQNF RKTGAFGPMA
AHVNGAIGVK LAHPDRTVVV GCGDGCYSLA GFELMTAVEN DVPVIWVIFN DDEYKLVKLY
QLATYGESAL VEFKNPDFAA YARVCGADGF RVETLEEFED AFRTALGSGR PTVIDAKITR
WALPRYSTSP KGMVHGIWET LEKRLRHD
//