ID   G9WZY1_9FIRM            Unreviewed;       577 AA.
AC   G9WZY1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF9629_01737 {ECO:0000313|EMBL:EHL15613.1};
OS   Peptoanaerobacter stomatis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoanaerobacter.
OX   NCBI_TaxID=796937 {ECO:0000313|EMBL:EHL15613.1, ECO:0000313|Proteomes:UP000006437};
RN   [1] {ECO:0000313|EMBL:EHL15613.1, ECO:0000313|Proteomes:UP000006437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACC19a {ECO:0000313|EMBL:EHL15613.1,
RC   ECO:0000313|Proteomes:UP000006437};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A.,
RA   Epstein S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Eubacteriaceae bacterium ACC19a.";
RL   Submitted (AUG-2011) 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:EHL15613.1}.
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DR   EMBL; AFZE01000010; EHL15613.1; -; Genomic_DNA.
DR   RefSeq; WP_009525966.1; NZ_JH414559.1.
DR   AlphaFoldDB; G9WZY1; -.
DR   PATRIC; fig|796937.3.peg.932; -.
DR   HOGENOM; CLU_013748_1_3_9; -.
DR   BioCyc; EBAC796937-HMP:GMGH-1745-MONOMER; -.
DR   Proteomes; UP000006437; 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; 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:SF142; 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.
PE   3: Inferred from homology;
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..125
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          201..335
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          391..541
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   577 AA;  65750 MW;  5A11B2BBC733DC1C CRC64;
     MKISDFIVNF FIDKGIIDVF GYPGGMVTHL MDSFEKYNKY IKVHVNYHEQ ASAFSACGYA
     QCSLKPGLAF ATSGPGATNL ITGICNAYFD SIPCVFITGQ VNTYESKGDS LVRQKGFQET
     DIVSMVKNVT KDSIYINSSK ELPEILYNLY CLSISGRPGP VLIDIPMNIQ REEIEDEIAY
     FYIKKEVKKL NTKNIDDFQI EYITKSLKNS NRPCIIVGAG IRQSGQIEKF REIVNKFKIP
     VITSMVSIDV LERDNPYNYG FIGSYGNRVA NFITSKSDLI ISIGTRLDCR QTGNNLLFFA
     PNAKLIRIDI DSDEMTNKIK KNEVQYNIDL KDFLSYMKYM SFEGCHEKFL KWNEICLQIS
     KYLKSMDELL PNNIIKRLSD LFPNECVITT DVGQNQVWVA QSINNKSTQK VLFSGGHGSM
     GYSLPAAIGA YYAVKLPIIC IVGDGGIQMN IQELEFIRRE KLPIKIILIN NHSLGMIRHF
     QEMYFNSIFA QTIEEKGYST PNFSKIALAY DLNYYNINNL DDINDNIKEI LCNDIPQFIE
     IGIKQKTYVY PKLAINKPIE DQEPLMDRDL FETIKKL
//