ID   B0CDG0_ACAM1            Unreviewed;       545 AA.
AC   B0CDG0;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   02-SEP-2026, entry version 82.
DE   SubName: Full=Acetolactate synthase, large subunit, biosynthetic type {ECO:0000313|EMBL:ABW26885.1};
GN   Name=ilvB {ECO:0000313|EMBL:ABW26885.1};
GN   OrderedLocusNames=AM1_1865 {ECO:0000313|EMBL:ABW26885.1};
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC   Acaryochloridaceae; Acaryochloris.
OX   NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW26885.1, ECO:0000313|Proteomes:UP000000268};
RN   [1] {ECO:0000313|EMBL:ABW26885.1, ECO:0000313|Proteomes:UP000000268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP000828; ABW26885.1; -; Genomic_DNA.
DR   RefSeq; WP_012162388.1; NC_009925.1.
DR   AlphaFoldDB; B0CDG0; -.
DR   STRING; 329726.AM1_1865; -.
DR   KEGG; amr:AM1_1865; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_2_3; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000000268; Chromosome.
DR   GO; GO:0005948; C:acetolactate synthase complex; IEA:TreeGrafter.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:TreeGrafter.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:TreeGrafter.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0009099; P:L-valine biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd02010; TPP_ALS; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   FunFam; 3.40.50.970:FF:000007; Acetolactate synthase; 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   NCBIfam; NF006187; PRK08322.1; 1.
DR   NCBIfam; NF006378; PRK08617.1; 1.
DR   PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000000268};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..116
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          186..318
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          378..524
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   545 AA;  59954 MW;  BBDAD4CE535582DE CRC64;
     MNTAELLVKC LENEGVEYIF GLPGEENLQV LEALRDSSIQ FITTRHEQGA AFMADVYGRL
     TGRAGVCLST LGPGATNLMT GVADANLDGA PLVAITGQVG TDRMHIESHQ YLDLVAMFNP
     VTKWNSQIVR PSNTPEIVRR AFKRAQTEKP GAVHIDLPEN IAAMPAEGMP LQQDSLKRSF
     ASPRNLEQAA EIISQATNPL ILVGNGAIRA NASEALTQFA TELNIPVANT FMGKGVIRYT
     HPLALWTVGL QQRDYISCGF DRTDLVIAVG YDLIEFSPKK WNPDGTIPIV HVGAEPAEID
     SSYIPKTEVV GDISDSLIEI LRRADRQGKP DPYGVELRPQ IRADYEEYAK DEHFPLRPQK
     LIYDLREVLA SEDIVISDVG AHKMWMARHY HCDRPNTCLI SNGFAAMGIA IPGALAAKLV
     YPDRHVVAVT GDGGFMINMQ ELETALRLGV AFTTIIFNDG GYGLIEWKQQ QYYGEASFIK
     FGNPDFVRLA ESMGLKGYRV ESSADFMPCL KTALAQDVPT IVDCPIDYKE NLMFSQKSGE
     IACIN
//