ID A0A1W1Y0Z6_9NEIS Unreviewed; 603 AA.
AC A0A1W1Y0Z6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SMC29805.1};
GN ORFNames=SAMN02745857_04146 {ECO:0000313|EMBL:SMC29805.1};
OS Andreprevotia lacus DSM 23236.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Andreprevotia.
OX NCBI_TaxID=1121001 {ECO:0000313|EMBL:SMC29805.1, ECO:0000313|Proteomes:UP000192761};
RN [1] {ECO:0000313|EMBL:SMC29805.1, ECO:0000313|Proteomes:UP000192761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23236 {ECO:0000313|EMBL:SMC29805.1,
RC ECO:0000313|Proteomes:UP000192761};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWXD01000045; SMC29805.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1Y0Z6; -.
DR STRING; 1121001.SAMN02745857_04146; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000192761; Unassembled WGS sequence.
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; cd00568; TPP_enzymes; 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:SF142; 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:UP000192761};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..107
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 408..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 603 AA; 65295 MW; EF5E3BFBFDC0A6C1 CRC64;
MQRVAEQIAD WLVEQGIEQV FAVTGGGAMF LNQAFASHPK LKCTYMHHEQ ACAMAAEGYA
RISGKPAVVN VTTGPGGINA LNGVFGAYTD SIPMLVISGQ VKRDTLLDYK QVEGLRQLGD
QEAPVAAMAR PVTKSANVVL STAELAVLLP KALHECRTGR PGPVWLDIPL DIQSATEPVA
FQPAEIVPEP KIELPLAHIH ELLSQAQRPV LLGGTGVRLA GAQDALLALA ERRGIPLATA
WTHDLIASDH PLFAGRPGTI GTRAGNFAVQ NADLVIVIGS RLNIRQVSYN WPAFAKNATV
VHVDIDPAEL SKPIFNAHVP VAADARDFVL AFDAYLATCP ALPDYSPWAQ WCVGLRTRYP
VLQPHHLTGE RINPYQAIDF VFRHLRHDDI VVCGNASACI IPFQTGHLTS GQRMFSNSGS
ASMGYDLPAA LGAAIAAPQR RVICFAGDGS LQMNIQELQT LRTLQLNVIV VVIDNNGYLS
IKQTHENFFG QIVGAHPDSG VDFPDFTAIA GAYGLPAQRI AVREQFDALH TMLQQDGPQL
IQLEVDSEQS FEPRLKSRMG SDGTFHTPEL DDMFPFIAEA ELEAVRAEAL AIHAIPRKET
HHA
//
