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Database: UniProt
Entry: A0A3N1CXN4_9ACTN
LinkDB: A0A3N1CXN4_9ACTN
Original site: A0A3N1CXN4_9ACTN 
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
//
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