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
//