ID V9W0D7_9RHOB Unreviewed; 557 AA.
AC V9W0D7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AHD03479.1};
GN ORFNames=METH_21880 {ECO:0000313|EMBL:AHD03479.1};
OS Leisingera methylohalidivorans DSM 14336.
OG Plasmid unnamed {ECO:0000313|EMBL:AHD03479.1,
OG ECO:0000313|Proteomes:UP000018780}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD03479.1, ECO:0000313|Proteomes:UP000018780};
RN [1] {ECO:0000313|EMBL:AHD03479.1, ECO:0000313|Proteomes:UP000018780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD03479.1,
RC ECO:0000313|Proteomes:UP000018780};
RC PLASMID=1 {ECO:0000313|Proteomes:UP000018780};
RG DOE Joint Genome Institute;
RA Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (SEP-2013) 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; CP006774; AHD03479.1; -; Genomic_DNA.
DR RefSeq; WP_024092775.1; NC_023146.1.
DR AlphaFoldDB; V9W0D7; -.
DR KEGG; lmd:METH_21880; -.
DR PATRIC; fig|999552.6.peg.4325; -.
DR HOGENOM; CLU_013748_3_2_5; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000018780; Plasmid 1.
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; 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; 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 Plasmid {ECO:0000313|EMBL:AHD03479.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 13..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 557 AA; 60943 MW; C8DF5E8F73BF4FC3 CRC64;
MHETRSVPHS PAKASDLLVD ALEAEGVEYV FAVPGEENLD LLESLRTSKI ELVLTRHEQG
AAFMAATYGR LTGKAGVCMA TLGPGATNFA TPAAYAHLGG MPLIMITGQK PIKKSKQGRF
QIIDVVGLFE PICKMSKQIV HGNTIPALIR EAFRTAEEER PGAVLLELPE DIAAEETDAS
VIPPHPRHYA VAGDEVLNEA AEMIRSARMP LLLLGAGANR RKARSALCGF TDLIQIPFFN
TQMGKGVVDE RSDLFLGTAA LSDGDYLHCA IERADLIINV GHDVVEKPPF FMEEGGTKVI
HVNYKAAQVD QVYFPQLEVV GDLAQSITRL GKMLGGPLDF DRSYFQRIKQ ETEKHLSNRA
GDARFPVIPQ RLVADTRKVM DDCDIIALDN GIYKIWYARN YKAYDSNTVL LDNALATMGA
GLSSAMMAAK LNPGRRVMAI CGDGGFMMNS QELETAVRLG LNLVVTVLND SSYGMIRWKQ
SHAGFADWGL EFGNPDFVQY ANSYGATGHR IERTEDLVPT FEKAFAAGGV HLIDVPVDYS
ENQRVLIDEL AEKVCLI
//
