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Database: UniProt
Entry: E6QI57_9ZZZZ
LinkDB: E6QI57_9ZZZZ
Original site: E6QI57_9ZZZZ 
ID   E6QI57_9ZZZZ            Unreviewed;       387 AA.
AC   E6QI57;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Acetolactate synthase (Acetohydroxy-acid synthase) (Large subunit) {ECO:0000313|EMBL:CBI06922.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:CBI06922.1};
GN   ORFNames=CARN6_0216 {ECO:0000313|EMBL:CBI06922.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI06922.1};
RN   [1] {ECO:0000313|EMBL:CBI06922.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA   Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA   Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA   Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA   Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA   Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA   Le Paslier D.;
RT   "Diversity of trophic interactions inside an arsenic-rich microbial
RT   ecosystem.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:CBI06922.1}.
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DR   EMBL; CABQ01000039; CBI06922.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6QI57; -.
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   CDD; cd02015; TPP_AHAS; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR039368; AHAS_TPP.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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); 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:CBI06922.1}.
FT   DOMAIN          10..144
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          203..349
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   387 AA;  42284 MW;  022C0336DA37AD05 CRC64;
     MLHCTNSHLH DAAELIRNAK RPVILAGHGI MKAQAGEQIT TLAERMQIPV AMTLLGLGGF
     PASHPLNMGM MGMHGESWVN HAIQEADLLI ACGMRFDDRV IGTPATYAPN AKKIHIEIDP
     AEINKNIKVD VALVGDLREV LEQLLPLLPG RDGAAWLKAI EESKGTAAVR DIRNLPDSGH
     LYAAHVMHDL WRITEGRAIV ATDVGQHQMW EAQYYHHDLP RTLITSGGLG TMGFALPAGI
     GAKVARPESE VWVIAGDGGF QMTASELATI VQEKLKINIA IINNGYLGMV RQWQEFFYER
     NYESTPLVSP DFVKLADAHG IAGAAVRTRS ELESAVAAAR NHPGPYLLNF MVEKEDSVYP
     MIPAGSALHE MIRRPGENPL VETSEDN
//
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