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
//