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Database: UniProt
Entry: E7GTU8_CLOSY
LinkDB: E7GTU8_CLOSY
Original site: E7GTU8_CLOSY 
ID   E7GTU8_CLOSY            Unreviewed;       613 AA.
AC   E7GTU8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:EGA91735.1};
GN   ORFNames=HMPREF9474_04343 {ECO:0000313|EMBL:EGA91735.1};
OS   [Clostridium] symbiosum WAL-14163.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=742740 {ECO:0000313|EMBL:EGA91735.1, ECO:0000313|Proteomes:UP000002970};
RN   [1] {ECO:0000313|EMBL:EGA91735.1, ECO:0000313|Proteomes:UP000002970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL-14163 {ECO:0000313|EMBL:EGA91735.1,
RC   ECO:0000313|Proteomes:UP000002970};
RA   Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA   Molitoris D.R., Vaisanen M.L., Daigneault M., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA   Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   White J., Yandava C., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium symbiosum strain WAL-14163.";
RL   Submitted (DEC-2010) 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}.
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:EGA91735.1}.
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DR   EMBL; ADLQ01000102; EGA91735.1; -; Genomic_DNA.
DR   RefSeq; WP_003504768.1; NZ_GL834321.1.
DR   AlphaFoldDB; E7GTU8; -.
DR   STRING; 1512.GCA_900049235_04697; -.
DR   GeneID; 57968737; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_9; -.
DR   Proteomes; UP000002970; 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; cd00568; TPP_enzymes; 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; 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:UP000002970};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          6..116
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          202..337
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          405..560
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   613 AA;  66376 MW;  356D6319A9758D30 CRC64;
     MSKKLVSDLL VDYLERRGVT KLFGLCGHTV IGMLDALSRS EKIEYIGTRH ESVASTAADG
     YARVTHKASV VMCHLGPGLT NVITGVANAS LDSIPMVVIA GDVPSYYYGR HPHQEVQMHA
     DGDQYKLLEP VVKRAWRVDD VEAFPDILDK AFRLAESGRP GPVLVDVPMD MFSREMDEDL
     WARTHKGNLV TMRPALDPAA AKAIAKRLAR AKNPVLHAGG GILLSQASEE LAALAEYLDI
     PVSRTLAGQG CLSDLHPLMI GQTGFWGLEF THSLTTNADV ILGLGTRFGE ADSSSWYQGV
     TFDPDKTTFL QIDIDPMEIG RNYPVEIGAM GDLKIGLGQI LEEVKKLCPE GRNNPELRAR
     IARAKADFKQ SNAAISSDSR FPMTPQRILK DVKEVIPEDA VIFTDVGWNK NGVAQEFDIT
     IPGTIHHSSG LATMGFGPSA VLGGKVAAPD KIVINLTGDG GFGINPSCLA TAVEHGIACT
     WVVMNNSAFG TIAGLENANY KTKFGTVFYK PDGERYTICW ADVAKSYGIE SICVNSAEEF
     KPALEKAIAA NKEGRPFLVE APMENIVVPT PGCWNINDIY TPNALVKEGK LVKKENGRYV
     APSHSKSHDG CLN
//
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