ID A0A3N1WQS6_9BURK Unreviewed; 557 AA.
AC A0A3N1WQS6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:ROR17036.1};
GN ORFNames=EC845_4077 {ECO:0000313|EMBL:ROR17036.1};
OS Comamonas sp. BIGb0124.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=2485130 {ECO:0000313|EMBL:ROR17036.1, ECO:0000313|Proteomes:UP000267274};
RN [1] {ECO:0000313|EMBL:ROR17036.1, ECO:0000313|Proteomes:UP000267274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIGb0124 {ECO:0000313|EMBL:ROR17036.1,
RC ECO:0000313|Proteomes:UP000267274};
RA Samuel B.;
RT "Genomic analyses of the natural microbiome of Caenorhabditis elegans.";
RL Submitted (NOV-2018) 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:ROR17036.1}.
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DR EMBL; RJVF01000015; ROR17036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1WQS6; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000267274; 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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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:UP000267274};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 12..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..335
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 395..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 557 AA; 59561 MW; 3817245022011309 CRC64;
MSETTPGAVA RSGGRALVDA LRLHGVDRVF CVPGESYLEV LDALHDTPEI ALVVAKHEGG
AANMAEADGK LTGRPGICMV TRGPGATHAS VGVHIAQQDS TPMILFVGQI ARSHRGREAF
QEVDYQALFG SLAKWVVEID DAARVPEIVA RAFQAACSGR PGPVVVSLPE DMLLEPCTRA
DCAAVLPAPM VPAAGLVDGI VQRLARAQRP LVVVGGPDWD DAGRQALSRF AARWSLPVAC
AFRRQDVLDN LDEHYVGHMS LGMNPKLAQR VRDADLILAI GTRLGDIVTD GYTLIEPPRP
AQPLIHIHAD AGELGRVYQP ELAVVAHAGA AVAALADRPP PGTLPWQDWT RQARTEHEAF
SLPPEPAAGH RGVDLGSVVA HLGRTLPPDS ILTNGAGNYS VWLHRFYAYR RGRTELAPTC
GAMGYGLPAA VAASLRHPGR QVVCMAGDGC FLMYPQELAT AAEYGARLIV LVANNGMYGT
IRMHQERRHP GRVSGTRLQG PDYVMLARSF GAHAERIEQT EDFAAAFARA QAAQGLALLE
LVTDPLQITP QMRLAEA
//
