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Database: UniProt
Entry: Q7D456_CLOAB
LinkDB: Q7D456_CLOAB
Original site: Q7D456_CLOAB 
ID   Q7D456_CLOAB            Unreviewed;       563 AA.
AC   Q7D456;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AAK81574.1};
GN   Name=alsS {ECO:0000313|EMBL:AAK81574.1};
GN   OrderedLocusNames=CA_C3652 {ECO:0000313|EMBL:AAK81574.1};
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK81574.1, ECO:0000313|Proteomes:UP000000814};
RN   [1] {ECO:0000313|EMBL:AAK81574.1, ECO:0000313|Proteomes:UP000000814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC   {ECO:0000313|Proteomes:UP000000814};
RX   PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; AE001437; AAK81574.1; -; Genomic_DNA.
DR   PIR; C97348; C97348.
DR   RefSeq; NP_350234.1; NC_003030.1.
DR   RefSeq; WP_010966914.1; NC_003030.1.
DR   AlphaFoldDB; Q7D456; -.
DR   STRING; 272562.CA_C3652; -.
DR   GeneID; 45000150; -.
DR   KEGG; cac:CA_C3652; -.
DR   PATRIC; fig|272562.8.peg.3841; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_2_9; -.
DR   OMA; GFPIKPQ; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000000814; Chromosome.
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; 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: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   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:UP000000814};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          23..139
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          208..341
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          399..545
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  62563 MW;  65A48C17ED327256 CRC64;
     MNENLKQDKD SEISKTEDEE SSMNTAELVV KCLENENVEY IFGIPGEENL ALIKALTKSP
     IKFITTRHEQ GAAFMADVYG RLTGRPGVCL STLGPGATNL MTGVADANLD GAPLIAITGQ
     VGTDRMHIES HQHLDLVAMF APVTKWNKQI VRPDTAPEIV RKAFKTAVDE KPGACHIDLP
     QNIADMPVQG KPLRHTVTDK SFAAYSSIEK AAIAISRAKS PLILSGNGAI RSKASKAVLD
     MAERLNIPVA NTFMGKGIIP FNHPLSLWSM GLAQKDYINR IFEKTDLVIA IGYDIVEYSP
     KKWNSKGEIR IIHIGEKKAE VNNSYLPEVE VIGDISDSIQ EIIRRSDRIE TPKQALKIKE
     DMHKNYEEYS DDQSFPMKPQ KVLYDLRRVM GEDDIVISDV GAHKMWIARN YHCYKPNTCI
     ISNGFASMGI AIPGALAAKL VNPDKKVVAV TGDGGFMMNS QELETALRIG TPFVTLIFND
     SNYGLIKWKQ EERYGESAYI NFTNPDFKMY AESMGLKGYR ITKAEELIPT LEEAFSQKVP
     SVIDCAVDYS ENLKLSHKLE ELK
//
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