ID A0A0F5YB94_9CYAN Unreviewed; 612 AA.
AC A0A0F5YB94;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Acetolactate synthase {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
GN ORFNames=WN50_22100 {ECO:0000313|EMBL:KKD36013.1};
OS Limnoraphis robusta CS-951.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Sirenicapillariaceae; Limnoraphis.
OX NCBI_TaxID=1637645 {ECO:0000313|EMBL:KKD36013.1, ECO:0000313|Proteomes:UP000033607};
RN [1] {ECO:0000313|EMBL:KKD36013.1, ECO:0000313|Proteomes:UP000033607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-951 {ECO:0000313|EMBL:KKD36013.1,
RC ECO:0000313|Proteomes:UP000033607};
RA Willis A., Parks M., Burford M.A.;
RT "Draft genome assembly of filamentous brackish cyanobacterium Limnoraphis
RT robusta strain CS-951.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU003591};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU003591}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC ECO:0000256|RuleBase:RU003591}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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:KKD36013.1}.
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DR EMBL; LATL02000006; KKD36013.1; -; Genomic_DNA.
DR RefSeq; WP_046280759.1; NZ_LATL02000006.1.
DR AlphaFoldDB; A0A0F5YB94; -.
DR PATRIC; fig|1637645.4.peg.100; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000033607; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02015; TPP_AHAS; 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; IPR012846; Acetolactate_synth_lsu.
DR InterPro; IPR039368; AHAS_TPP.
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 InterPro; IPR026870; Zinc_ribbon_dom.
DR NCBIfam; TIGR00118; acolac_lg; 1.
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 Pfam; PF13240; zinc_ribbon_2; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU003591};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU003591}; Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Reference proteome {ECO:0000313|Proteomes:UP000033607};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:KKD36013.1}.
FT DOMAIN 13..130
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 207..341
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 404..552
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 590..612
FT /note="Zinc-ribbon"
FT /evidence="ECO:0000259|Pfam:PF13240"
SQ SEQUENCE 612 AA; 66734 MW; A6A1D190D9587038 CRC64;
MQLRTQVAAK RATGAFALMD SLKRHGVEHI FGYPGGAILP IYDELYRFEA GGDLKHILVR
HEQGAAHAAD AYARATGRVG VCFGTSGPGA TNLVTGIATA HMDSIPLVVV TGQVSRKAIG
TDAFQETDIF GITLPIVKHS YLVRDPKKMA AIVAEAFHIA STGRPGPVLI DVPKDVGLEE
FDYIPVNPGE VSLTGYRPTV KGNMRQINQA IALIRKAERP LLYIGGGGIS ANAHAEIHEL
AELFQIPVTT TLMGKGAFDE NHPLSVGMLG MHGTAYANFA VSECDLLIAV GARFDDRVTG
KLEEFASRAE VIHIDIDPAE VGKNRAPEVP IVGDVRQVLV DLLRRCRETG EPAPQTQTQA
WLDRINRWRE DYPLEVPLYP DSLSPQEVIS ELGKMAPDAY YTTDVGQHQM WAAQYLKNGP
RQWISSAGLG TMGYGLPAAM GAKVALPDHE VICIAGDASI QMNIQELGTL MQYGIHAKTV
IINNGWQGMV RQWQQTFYGE RYSSSNMELG MPNFVKLAEA YGVKGMSVTH RDQLHEALAE
MLAYDGPVLM DVRVRRDENC YPMVAPGKSN AQMLGLPERK KLEQAAELVY CSNCGTKNVA
SNHFCPECGT KL
//
