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Database: UniProt
Entry: K7AD79_9ALTE
LinkDB: K7AD79_9ALTE
Original site: K7AD79_9ALTE 
ID   K7AD79_9ALTE            Unreviewed;       546 AA.
AC   K7AD79;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AGH47046.1};
GN   ORFNames=C427_4947 {ECO:0000313|EMBL:AGH47046.1};
OS   Paraglaciecola psychrophila 170.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH47046.1, ECO:0000313|Proteomes:UP000011864};
RN   [1] {ECO:0000313|EMBL:AGH47046.1, ECO:0000313|Proteomes:UP000011864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:AGH47046.1,
RC   ECO:0000313|Proteomes:UP000011864};
RX   PubMed=23640379;
RA   Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT   "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL   Genome Announc. 1:E00199-13(2013).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP003837; AGH47046.1; -; Genomic_DNA.
DR   RefSeq; WP_007643025.1; NZ_BAES01000095.1.
DR   AlphaFoldDB; K7AD79; -.
DR   STRING; 1129794.C427_4947; -.
DR   KEGG; gps:C427_4947; -.
DR   PATRIC; fig|1129794.4.peg.4934; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_2_6; -.
DR   OrthoDB; 9785953at2; -.
DR   Proteomes; UP000011864; 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   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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:UP000011864};
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..318
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          378..524
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   546 AA;  60409 MW;  3A05669076099A38 CRC64;
     MKASDLFVKA LEAEGVEYIF GIPGEENLDL LESLRESPIK LILTRHEQGA GFMAATYGRL
     TGKVGVCLST LGPGATNLVT PAAYAQLGAM PMLMITGQKP VKTSKQGRFQ VIDVVDMMRP
     ITKYTTQLVS GDRIPSAVRE AFRLAHDERP GATHIELPED IAAEDTSAYL LTPSVSRRPI
     AEYKAINRAV EMIETAKSPL LLIGAAANRK LTSKMLKELV SKTGIPYVTT QMGKGVLDER
     DDLFMGNTAL SAGDFVHRVI DRADLIINVG HDVVEKPPFF MNNDGQQVIH INFEPAAVDP
     VYFPQLEVIG DIANTIWQMK EQIVASANWD FSFFFKAHNA YLTHKAESEN DDRFPILPER
     FVRDIRRAMP DEGIVTLDNG VYKIWFARNY PAALPNTLLL DNALATMGAG LPSAMAAKLV
     YPDRPVISVC GDGGFMMNSQ ELETAVRLKL HIVVIILRDD AYGMIKWKQA NMEFENYGLD
     YGNPDFVKYV ESYGGKGWRI AAADELLPQV QKCLAEPGVH LIDVPVDYSL NDKTLNQTLR
     IRSASI
//
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