ID D8MK89_ERWBE Unreviewed; 559 AA.
AC D8MK89;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:CAX57545.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CAX57545.1};
GN Name=budB {ECO:0000313|EMBL:CAX57545.1};
GN OrderedLocusNames=EbC_00140 {ECO:0000313|EMBL:CAX57545.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX57545.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX57545.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FP236843; CAX57545.1; -; Genomic_DNA.
DR RefSeq; WP_013200054.1; NC_014306.1.
DR AlphaFoldDB; D8MK89; -.
DR STRING; 634500.EbC_00140; -.
DR KEGG; ebi:EbC_00140; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_6; -.
DR Proteomes; UP000008793; Chromosome.
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 GO; GO:0034077; P:butanediol metabolic process; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:CAX57545.1}.
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..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 559 AA; 59833 MW; 21960127E7825B33 CRC64;
MKNPTDTQLW QHGADLVVAQ LEAQGVKQVF GIPGAKIDKV FDSLVDSTIQ TIPVRHEANA
AFMAAAVGRL TGNAGVALVT SGPGCSNLIT GMATATSEGD PVVALGGAVK RADSAKQVHQ
SMDTVAMFRP VTKYAVEVTD ANALSEVISN AFRQAEHGRG GGAFVSLPQD IVDQPARGNL
LSSKGQVLLG AAPDVAIEAV AAQIAQAKNP VLLLGLMASQ PQNSDALHRL LERSHIPVTS
TYQAAGAVRQ GHFSRFAGRV GLFNNQAGDR LLRQADLIIT IGYSPVEYEP AMWNSGTATL
VHIDVLPAEA DNCYLPDAEL VGDIAATLDK LAARIASPLQ LSSQAASILH DRQQQRELLT
LQGQNLNQFA LHPLRIVRAM QDIINSDVTL TVDMGSFHIW IARYLYSFRA RQIMISNGQQ
TMGVALPWAI GAWLVDPSRK VVSVSGDGGF LQSSMELETA VRLKANILHI IWVDEEYNMV
AMQEQKKYQR VSGVKFGPVD FKAYAEAFGA AGFAVDSAAA LEPTLRKAMD VQGPAVVAVP
VDYADNHLLM GQLHLSQIL
//
