ID R6YI98_9FIRM Unreviewed; 445 AA.
AC R6YI98;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:CDD35683.1};
GN ORFNames=BN600_01913 {ECO:0000313|EMBL:CDD35683.1};
OS Roseburia sp. CAG:309.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1262945 {ECO:0000313|EMBL:CDD35683.1, ECO:0000313|Proteomes:UP000018292};
RN [1] {ECO:0000313|EMBL:CDD35683.1, ECO:0000313|Proteomes:UP000018292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:309 {ECO:0000313|Proteomes:UP000018292};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:CDD35683.1}.
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DR EMBL; CBGX010000249; CDD35683.1; -; Genomic_DNA.
DR AlphaFoldDB; R6YI98; -.
DR STRING; 1262945.BN600_01913; -.
DR Proteomes; UP000018292; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02010; TPP_ALS; 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; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000018292}.
FT DOMAIN 85..219
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 276..422
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 445 AA; 50040 MW; 434E9BC4F3900EAF CRC64;
MHITAHQFLD LVQLFEPITK RSKQIVEPAS VNEIIRLAFK YAESEKPGAC HIDLPVNIAK
LPVEESEKPL IRRQLPVELP SENAIKVAVD TINKAKRPVI LAGNGAVRAH AEKALTLFSN
LLKIPVINTM MAKGIVPCDN AYSLLTIGTP QKDYVNKYIE SADVVITVGY DIIEYSPDKW
NYQNKASIVH IDARPAHINK HYQPVIDVVG DISISLQKLV SLCTDKEDPT LAFHLRRKME
QEYVQYAKDN AFPMKPQKIL FDIHRIMGKD GILISDVGAH KMWIARHYNS YQPNTCIISN
GFASMGIALP GAIVSKMIYP DRKILAVTGD GGFLMNVQEL ETAVRLKLAF VVLIFNDSSY
GLIKWKQEDY FGKSRYVDFD NPDFLKLAES FGCKGYRIQA ADELLPTLKE AFSQKVPTVI
DCAVDYGENP KLTKHLEDIH HLPLE
//