ID A0A0B1ZUX2_9SPHN Unreviewed; 559 AA.
AC A0A0B1ZUX2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=LK12_00585 {ECO:0000313|EMBL:KHK92927.1};
OS Novosphingobium malaysiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1348853 {ECO:0000313|EMBL:KHK92927.1, ECO:0000313|Proteomes:UP000031057};
RN [1] {ECO:0000313|EMBL:KHK92927.1, ECO:0000313|Proteomes:UP000031057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 273 {ECO:0000313|EMBL:KHK92927.1,
RC ECO:0000313|Proteomes:UP000031057};
RA Lee L.-H.;
RT "Genome sequence of Novosphingobium malaysiense MUSC 273(T).";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KHK92927.1}.
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DR EMBL; JTDI01000001; KHK92927.1; -; Genomic_DNA.
DR RefSeq; WP_039278109.1; NZ_JTDI01000001.1.
DR AlphaFoldDB; A0A0B1ZUX2; -.
DR STRING; 1348853.LK12_00585; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000031057; 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:0044281; P:small molecule metabolic process; IEA:UniProt.
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:SF169; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000031057};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..112
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 394..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 559 AA; 58994 MW; E959E1B507724B74 CRC64;
MAADKIPVYE ALAGDIRDLG IECVFGLMSD DTAQFVTTLD AYGVRFFGAR HENNAVCMAE
GYAAASGKLG IVILGRGPAT ANGMHGMGYA KRAGTPVLMI MGADPVGTRP ANGVGPDRKS
FNAEDALKAA GIPVVVADDP ATARRTLVKA MADAERGGHA LLLPTNVQLA RIDPEATAPQ
EAVSAKPASA PARDTAIATA VAVLEKASRP LFLVGRGAYD TGAKDAIIAL ADHVGAALVT
TMKAKDMFTG HPFNCGVLGS FSNVGGRRLI EQADCVVSFG ASLNQQTTSY ATALPADIPV
IHVDSVRENV GRWFTADVGV VGDARLVAEQ LLAALPVRPD DAKAMRSEEN ARWLAEFDMK
DDFQPMNTPR TMDVRSAALV LDEILPKDRN LVFDSGNNLM ASSYITVPGP AQFKLTTDFA
SIGMGFGTAM GFAVGAPERQ TVFVLGDGSF LMTLGELETV AREGIPLIII LMNDCAYGAE
LHFLKEREAP VNLSVFPDID YAPVAEAFGF ETATVRTLDE LRELAPLFED PDGPVFVECK
INASVVAPFL LETASVAGK
//