ID D4MZK3_ANAHA Unreviewed; 581 AA.
AC D4MZK3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 83.
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 Name=ilvB_2 {ECO:0000313|EMBL:CUN49565.1};
GN Synonyms=ilvB_1 {ECO:0000313|EMBL:CUM80042.1};
GN ORFNames=CL2_10500 {ECO:0000313|EMBL:CBL38048.1}, DO83_12995
GN {ECO:0000313|EMBL:AQP40406.1}, ERS852425_01095
GN {ECO:0000313|EMBL:CUM86508.1}, ERS852475_00246
GN {ECO:0000313|EMBL:CUN49565.1}, ERS852520_00678
GN {ECO:0000313|EMBL:CUP13290.1}, ERS852571_00650
GN {ECO:0000313|EMBL:CUM80042.1};
OS Anaerostipes hadrus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL38048.1, ECO:0000313|Proteomes:UP000008960};
RN [1] {ECO:0000313|EMBL:CBL38048.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38048.1,
RC ECO:0000313|Proteomes:UP000008960};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SSC/2.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL38048.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38048.1,
RC ECO:0000313|Proteomes:UP000008960};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000095553, ECO:0000313|Proteomes:UP000095564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608868 {ECO:0000313|EMBL:CUM86508.1,
RC ECO:0000313|Proteomes:UP000095598}, 2789STDY5834860
RC {ECO:0000313|EMBL:CUN49565.1, ECO:0000313|Proteomes:UP000095611},
RC 2789STDY5834908 {ECO:0000313|EMBL:CUP13290.1,
RC ECO:0000313|Proteomes:UP000095564}, and 2789STDY5834959
RC {ECO:0000313|EMBL:CUM80042.1, ECO:0000313|Proteomes:UP000095553};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AQP40406.1, ECO:0000313|Proteomes:UP000188159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPB5 {ECO:0000313|EMBL:AQP40406.1,
RC ECO:0000313|Proteomes:UP000188159};
RX PubMed=27264309; DOI=10.1038/srep27572;
RA Zhang Q., Wu Y., Wang J., Wu G., Long W., Xue Z., Wang L., Zhang X.,
RA Pang X., Zhao Y., Zhao L., Zhang C.;
RT "Accelerated dysbiosis of gut microbiota during aggravation of DSS-induced
RT colitis by a butyrate-producing bacterium.";
RL Sci. Rep. 6:27572-27572(2016).
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|ARBA:ARBA00000673,
CC 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}.
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DR EMBL; CP012098; AQP40406.1; -; Genomic_DNA.
DR EMBL; FP929061; CBL38048.1; -; Genomic_DNA.
DR EMBL; CYXY01000003; CUM80042.1; -; Genomic_DNA.
DR EMBL; CYXT01000006; CUM86508.1; -; Genomic_DNA.
DR EMBL; CYZM01000001; CUN49565.1; -; Genomic_DNA.
DR EMBL; CZAU01000004; CUP13290.1; -; Genomic_DNA.
DR RefSeq; WP_015530384.1; NZ_WQRA01000055.1.
DR AlphaFoldDB; D4MZK3; -.
DR STRING; 649756.ERS852387_00950; -.
DR GeneID; 15231139; -.
DR KEGG; bprl:CL2_10500; -.
DR PATRIC; fig|245018.3.peg.1290; -.
DR OMA; FILTHHE; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000008960; Chromosome.
DR Proteomes; UP000095553; Unassembled WGS sequence.
DR Proteomes; UP000095564; Unassembled WGS sequence.
DR Proteomes; UP000095598; Unassembled WGS sequence.
DR Proteomes; UP000095611; Unassembled WGS sequence.
DR Proteomes; UP000188159; Chromosome.
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 NCBIfam; TIGR00118; acolac_lg; 1.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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 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}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:CBL38048.1}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..553
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 581 AA; 63965 MW; FB9B10CE68ADB8DF CRC64;
MGKMTGNEFL VKALQEEGVE KIFGYPGACV IDIFDEIYKQ DQVELILPRH EQGLIHAADG
YARATGKVGV CLATSGPGAT NLVTGIATAN YDSVPLVCFT GQVATNLIGN DTFQEIDIVG
VTRNIAKFVI VVRKREDLNR LIKEAFYIAR TGKPGPVLLD LPKDVMAELG SDEYPEEVNI
RGYKPNTKPH HGQILRAMNM IYDAKRPLFL IGGGAKIAGA QEEMCKLMET LKVPVVTTIM
GRGIVPTNHE LYYGNIGMHG NYAANQAVND CDLLISIGTR FNDRITGKLG TFASDAKIIH
IDIDTAAISK NVTVDVPLVG DAKEAIALML SIAENEEPCK VDEWLSRMNE WHEQKPLVME
EKEKLVPKQV IDAINEYFDE PIVTTDVGQN QMWTTQFLEL YGRRQMLTSG GLGTMGYGLP
AAIGAAIGNP GREVVCVSGD GGFQMNSQEI ATAVIQELPI TICILNNGYL GMVRQWQDLF
YDKAYAGTCL RRRKSCEHHC DGDFSKCPPY TPDFVKLAES YGAQGIRVFK KEEIIPAFEK
AKAKTDGPTI IEFIIENEEL VMPMVKPNGS ITDLIMERGE E
//