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Database: UniProt
Entry: A0A0A0DNS6_9BURK
LinkDB: A0A0A0DNS6_9BURK
Original site: A0A0A0DNS6_9BURK 
ID   A0A0A0DNS6_9BURK        Unreviewed;       596 AA.
AC   A0A0A0DNS6;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=JY96_05455 {ECO:0000313|EMBL:KGM39655.1};
OS   Aquabacterium sp. NJ1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Aquabacterium.
OX   NCBI_TaxID=1538295 {ECO:0000313|EMBL:KGM39655.1, ECO:0000313|Proteomes:UP000029993};
RN   [1] {ECO:0000313|EMBL:KGM39655.1, ECO:0000313|Proteomes:UP000029993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJ1 {ECO:0000313|EMBL:KGM39655.1,
RC   ECO:0000313|Proteomes:UP000029993};
RA   Masuda H.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGM39655.1, ECO:0000313|Proteomes:UP000029993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJ1 {ECO:0000313|EMBL:KGM39655.1,
RC   ECO:0000313|Proteomes:UP000029993};
RA   Shiwa Y., Yoshikawa H., Zylstra G.J.;
RT   "The draft genome sequence of a soil bacterium, Aquabacterium sp. strain
RT   NJ1, capable of utilizing both liquid and solid n-alkanes.";
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:KGM39655.1}.
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DR   EMBL; JRKM01000001; KGM39655.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0DNS6; -.
DR   STRING; 1538295.JY96_05455; -.
DR   eggNOG; COG0028; Bacteria.
DR   Proteomes; UP000029993; 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:UP000029993};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          3..115
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          202..333
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          454..575
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   596 AA;  64439 MW;  3909E9C1696FD181 CRC64;
     MGAASLIVSY LEALGVDFVF GVPGGAIEPL YNAMAVSMRR GGLRPVVARH EAGAAFMADG
     YARETGKIGV CVATSGPGAT NLITGVACAY DNKVPMLVIT GQPSLPVFGK GALQESACTG
     INTVGMFGHC TRYNTLVSHV DQLETKLVQA LMRASQPPHG PVHLSIPLDL MRSPVEQRLS
     PQSLQALLRK PSLIDEDMVH SLFTSLQASR KVALIVGGDC GEAIDAITHF AEMTNSSFVT
     TPDAKGLINP HHVLYRGVFG FAGHSSAQDA LNDDVDLILA IGTSLGEWTS GAWSQSVLNS
     KLIHIDAMDE HLRHSPMARQ HVRGRIRTVF ERLLDMMHIE QESLGMPWSP TDFKHTKHNA
     VTLREPEKVH SDATPIKPQR LMVELSKRLP PTTRFLADAG NATAWAIHYL ESRNNRRLGL
     VPPYGGSQDL AANRAWHGER RHDHAGWLRV LMDFAPMGWA IGAAVGVARG KPDCPVVCIT
     GDGSYLMNGQ EITVAAQEGL TVIFVILNDS ALGMVKHGQR LAGAEQVAFE LPTVNYALMA
     EAMGVRGHVI ESPDDFNQLD MAEILNRPGP TLLDIRIDAE EVPPMSLRMQ TLEGSV
//
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