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Database: UniProt
Entry: A6TA67_KLEP7
LinkDB: A6TA67_KLEP7
Original site: A6TA67_KLEP7 
ID   A6TA67_KLEP7            Unreviewed;       559 AA.
AC   A6TA67;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:ABR77488.1};
GN   ORFNames=KPN_02060 {ECO:0000313|EMBL:ABR77488.1};
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR77488.1, ECO:0000313|Proteomes:UP000000265};
RN   [1] {ECO:0000313|EMBL:ABR77488.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2] {ECO:0000313|EMBL:ABR77488.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP000647; ABR77488.1; -; Genomic_DNA.
DR   RefSeq; WP_015958557.1; NC_009648.1.
DR   AlphaFoldDB; A6TA67; -.
DR   STRING; 272620.KPN_02060; -.
DR   PaxDb; 272620-KPN_02060; -.
DR   EnsemblBacteria; ABR77488; ABR77488; KPN_02060.
DR   KEGG; kpn:KPN_02060; -.
DR   HOGENOM; CLU_013748_3_2_6; -.
DR   OMA; DIGSHYI; -.
DR   Proteomes; UP000000265; Chromosome.
DR   GO; GO:0003984; F:acetolactate synthase 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:0034077; P:butanediol metabolic process; 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; 1.20.5.740; Single helix bin; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR012782; Acetolactate_synth_catblc.
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   NCBIfam; TIGR02418; acolac_catab; 1.
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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          12..127
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          197..331
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          393..538
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   559 AA;  60326 MW;  976EFA78F2E9BB86 CRC64;
     MDKQYPVRQW AHGADLVVSQ LEAQGVRQVF GIPGAKIDKV FDSLLDSSIR IIPVRHEANA
     AFMAAAVGRI TGKAGVALVT SGPGCSNLIT GMATANSEGD PVVALGGAVK RADKAKQVHQ
     SMDTVAMFSP VTKYAVEVTA PDALAEVVSN AFRAAEQGRP GSSFVSLPQD VVDGPVSGKV
     LPASGAPQMG AAPDDAIDQV AKLIAQAKNP IFLLGLMASQ PENSKALRRL LETSHIPVTS
     TYQAAGAVNQ DNFSRFAGRV GLFNNQAGDR LLQLADLVIC IGYSPVEYEP AMWNSGNATL
     VHIDVLPAYE ERNYTPDVEL VGDIAGTLNK LAQNIDHRLV LSPQAAEILR DRQHQRELLD
     RRGAQLNQFA LHPLRIVRAM QDIVNSDVTL TVDMGSFHIW IARYLYSFRA RQVMISNGQQ
     TMGVALPWAI GAWLVNPERK VVSVSGDGGF LQSSMELETA VRLKANVLHL IWVDNGYNMV
     AIQEEKKYQR LSGVEFGPMD FKAYAESFGA KGFAVESAEA LEPTLRAAMD VDGPAVVAIP
     VDYRDNPLLM GQLHLSQIL
//
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