ID A0A258BYX3_9GAMM Unreviewed; 357 AA.
AC A0A258BYX3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Acetolactate synthase 3 large subunit {ECO:0000313|EMBL:OYW88041.1};
DE Flags: Fragment;
GN ORFNames=B7Z23_13195 {ECO:0000313|EMBL:OYW88041.1};
OS Pseudomonadales bacterium 32-61-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales.
OX NCBI_TaxID=1970544 {ECO:0000313|EMBL:OYW88041.1, ECO:0000313|Proteomes:UP000215582};
RN [1] {ECO:0000313|EMBL:OYW88041.1, ECO:0000313|Proteomes:UP000215582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-61-5 {ECO:0000313|EMBL:OYW88041.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYW88041.1}.
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DR EMBL; NCDF01001036; OYW88041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258BYX3; -.
DR Proteomes; UP000215582; 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 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; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..48
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 126..260
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 326..357
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OYW88041.1"
FT NON_TER 357
FT /evidence="ECO:0000313|EMBL:OYW88041.1"
SQ SEQUENCE 357 AA; 38321 MW; 4CA82F1DEE0A2F6C CRC64;
VLVTSGPGAT NAITGIATAF MDSIPMVVIS GQVPSNMVGT DAFQETDMIG ISRPIVKHSF
MIKHPSEIPE VMKKAFYLAE SGRPGPVVVD IPKDMTNPAE KFEYVYPKKA KLRSYGPALR
GHSGQIRKAA ELLLAAKRPI IYAGGGVILG GASAQLTELA KMLNLPVTNT LMGLGCYPGS
DRQFVGMLGM HGSYTANLAM HHADVILAVG ARFDDRVING AAKFCPNAKI IHIDIDPASI
SKTIKADIPI VGPVGSVLTE MVAIVKEIGQ APNAETVASW WKQIDEWRGN RGLFPYDKGD
GSIIKPQAAI EMLCEVTKGE AYVASDVGQH QMFACQYYKF DKPNRWLNSG GLGTMGF
//
