ID A0A166BER8_9EURY Unreviewed; 510 AA.
AC A0A166BER8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acetolactate synthase isozyme 2 large subunit {ECO:0000313|EMBL:KZX13244.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KZX13244.1};
GN Name=ilvG {ECO:0000313|EMBL:KZX13244.1};
GN ORFNames=MBORA_07940 {ECO:0000313|EMBL:KZX13244.1};
OS Methanobrevibacter oralis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=66851 {ECO:0000313|EMBL:KZX13244.1, ECO:0000313|Proteomes:UP000077428};
RN [1] {ECO:0000313|EMBL:KZX13244.1, ECO:0000313|Proteomes:UP000077428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7256 {ECO:0000313|EMBL:KZX13244.1,
RC ECO:0000313|Proteomes:UP000077428};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter oralis DSM 7256.";
RL Submitted (APR-2016) 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:KZX13244.1}.
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DR EMBL; LWMU01000055; KZX13244.1; -; Genomic_DNA.
DR RefSeq; WP_042693586.1; NZ_LWMU01000055.1.
DR AlphaFoldDB; A0A166BER8; -.
DR STRING; 66851.MBORA_07940; -.
DR PATRIC; fig|66851.6.peg.873; -.
DR OrthoDB; 6837at2157; -.
DR Proteomes; UP000077428; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
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: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 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KZX13244.1}.
FT DOMAIN 1..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 185..304
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 355..500
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 510 AA; 56691 MW; 98DBC6792A0CC601 CRC64;
MNVAEKLVEI LEEEKIEHIF GIPGEQIMPM YKALSESEIQ HILTRHEQAA AHAADAYYRS
SGKVGVCIST AAPGALNFTM ALATAFKDSI PILVLTGDND LDKRNTDYFQ SIPQFEMFKH
ITSESFSPLN GTEAVFCLRV ALFYLKNNPK GPIHINLSKD VLLSEEFEDH DLCTLCENDL
SKIVDAQKLI DKAQKPLFIL GAGAVSQKIA IRAFAEMYKI PVVTTFHGRG ILDESDDLNL
GMIGIRSTPR AKFAYENSDC IIALGIKASE RTLQEIPDYL IHVNINKDVL VGKYPIHGKV
EDFLLEINLK KADWLDEILK IPNEIEIEGI YDDLKPQAAI NSILNKYPNN IVVSDAGSHT
TWTTLLKKCN DSGKLIFSGG FAPMGYAIPA AIGVAIANLD EKIIVINGDG DFQMNLQELA
TIKDNNLNII IFIIDNSEFS ILRQWQESFY DMDPYQVELN NPDFLKLASS YGIDAVCVDN
IEDLELVLNK EVKGPLVVDV KVLSEDIPLP
//
