ID A0A3N4H059_9BACT Unreviewed; 546 AA.
AC A0A3N4H059;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:RPA66398.1};
GN ORFNames=EF405_20885 {ECO:0000313|EMBL:RPA66398.1};
OS Cyclobacteriaceae bacterium YHN15.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae.
OX NCBI_TaxID=2487897 {ECO:0000313|EMBL:RPA66398.1, ECO:0000313|Proteomes:UP000274029};
RN [1] {ECO:0000313|EMBL:RPA66398.1, ECO:0000313|Proteomes:UP000274029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YHN15 {ECO:0000313|EMBL:RPA66398.1,
RC ECO:0000313|Proteomes:UP000274029};
RA Chen Z.;
RT "Cecembia caeni sp. nov.,isolated from a lake.";
RL Submitted (NOV-2018) 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:RPA66398.1}.
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DR EMBL; RKQB01000015; RPA66398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4H059; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000274029; 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: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.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..523
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 546 AA; 60990 MW; F19D5D66EC1B3ABD CRC64;
MKASDLFVSA LENEGVVYIF AVPGEENLDF LQSLKNSNIK LIVTRHEQGA GFMAATYGRL
TGKPGVCLST LGPGATNLVT PAAYAQLGGM PMMMITGQKP IKKSKQARFQ IIDVVDMMRP
VTKYTKQIVN SNNIASQVRE AFRLAMEEKP GTVHLELPED IAQEDCTSDL FEPIGHIIPK
PDDTAIKESV KMIQEAKMPL LLIGAGANRK VTCDALKSFV DATGIYFFTT QMGKGAIDER
HDQYLGTAAL SSHDFLHAGI DKADLIINIG HDVIEKPPFF MKKGGKKVIH INFSPAQVDP
VYFPQLNVVG DITHSIRKLT AKLEKQAHWD FSFFQKVKLE VEGHLGKYFK DERFPMLPQR
LVNLLRENLR SEDIITLDNG IYKIWFARNY TCHLPNTLLL DNALASMGAG LPSAMMVNML
YPDRKVVAVC GDGGFMMNSQ EMETAVRLKL NLTVVILNDH AFGMIKWKQQ DMGFEDFGLD
YNNPDFVKYA ESYGAKGFRP KSDSDFQEIL KICLESDGVK LIDLPVDYSL NHPILNVMLK
EKVEKL
//
