ID U6EES5_9EURY Unreviewed; 530 AA.
AC U6EES5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:CDG65569.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CDG65569.1};
GN ORFNames=MBMB1_1471 {ECO:0000313|EMBL:CDG65569.1};
OS Methanobacterium sp. MB1.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=1379702 {ECO:0000313|EMBL:CDG65569.1, ECO:0000313|Proteomes:UP000017867};
RN [1] {ECO:0000313|EMBL:CDG65569.1, ECO:0000313|Proteomes:UP000017867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB1 {ECO:0000313|Proteomes:UP000017867};
RA Maus I., Wibberg D., Stantscheff R., Cibis K., Eikmeyer F.G., Puehler A.,
RA Koenig H., Schlueter A.;
RT "Methanobacterium sp. Mb1.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; HG425166; CDG65569.1; -; Genomic_DNA.
DR AlphaFoldDB; U6EES5; -.
DR STRING; 1379702.MBMB1_1471; -.
DR KEGG; meth:MBMB1_1471; -.
DR PATRIC; fig|1379702.4.peg.1466; -.
DR HOGENOM; CLU_013748_3_1_2; -.
DR BioCyc; MSP1379702:MBMB1_RS07130-MONOMER; -.
DR Proteomes; UP000017867; Chromosome.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000017867};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:CDG65569.1}.
FT DOMAIN 7..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 372..518
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 530 AA; 58128 MW; 8952B55514E99B6A CRC64;
MEALEITLAD ALVKILENEH LEFIFGYPGE QILPFYQALQ KSNIRHILTR HEQGAVHAAD
GYARASHHMG VCVATAGPGA LNMVMGVATA YKDSIPMLVI TGDVPLQLKG ENVFQDVDLN
LVFAHITLQS HLVTDPERGI FITKKAISDL KTGKTGPIHL NFPKDVLQMK VDSIILENEV
ETSPNTDWGG IDRIKMMVER SYKPLILAGA GVIWSHATTY LQEFAEKNQI PVATTYPARG
ILSEEHPLSL GLIGLRGTEA ANFAGKNSDL ILALGCRLSE RTRKGLGSGT LIQVNLDKGV
LDGDVNIKGD VKEFLDKIKE SNLNNTEQWL KEIQSLRKIH QVETNFKETP IRPQRAIKEI
LDAMGDSILV NDAGSHTTWV NLIFKAREPS SLLFSGGFGP MGYGVPAAIG VSLAHPSRSV
VVVVGDGGLQ MNIQELATIA ELDLPITICL LNNQSLGIIR QWQDLYYSGS FQVELENPDF
VQLAEAYHIK ALRVDSPGDV FEAVQKAVKL NKPVFIEIEI NENEDIPLPG
//