GenomeNet

Database: UniProt
Entry: A0A081FWP7_9GAMM
LinkDB: A0A081FWP7_9GAMM
Original site: A0A081FWP7_9GAMM 
ID   A0A081FWP7_9GAMM        Unreviewed;       565 AA.
AC   A0A081FWP7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   20-DEC-2017, entry version 21.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   ORFNames=ADIMK_2922 {ECO:0000313|EMBL:KEA62952.1};
OS   Marinobacterium sp. AK27.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Marinobacterium.
OX   NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA62952.1, ECO:0000313|Proteomes:UP000028252};
RN   [1] {ECO:0000313|EMBL:KEA62952.1, ECO:0000313|Proteomes:UP000028252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK27 {ECO:0000313|EMBL:KEA62952.1,
RC   ECO:0000313|Proteomes:UP000028252};
RA   Singh A., Pinnaka A.K.;
RT   "Marinobacterium kochiensis sp. nov., isolated from sediment sample
RT   collected from Kochi backwaters in Kerala, India.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 Mg(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 1/4. {ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KEA62952.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; JMQN01000043; KEA62952.1; -; Genomic_DNA.
DR   EnsemblBacteria; KEA62952; KEA62952; ADIMK_2922.
DR   PATRIC; fig|1232683.4.peg.2873; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000028252; Unassembled WGS sequence.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
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; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00118; acolac_lg; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU003591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028252};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028252};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591,
KW   ECO:0000313|EMBL:KEA62952.1}.
FT   DOMAIN        2    159       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      188    322       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      387    535       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   565 AA;  62517 MW;  32DE729E3AE17675 CRC64;
     MVVRALRDEG VKYIYGYPGG ALLHVYDALF QQDDVQHVLV RHEQAATHMA DAYARATGKA
     GVALVTSGPG ATNAVTGIAT AFTDSIPMVV ITGQVMSHLI GEDAFQETDM LGISRPIVKH
     NFSVQRAEDI PSTIKKAFYI AQSGRPGPVV VDIPKDMTTP TDRFPYEYPK SVKLRSYNPI
     SRGHSGQIRK AVDMLLQARR PVIYTGGGIV IGDASAELTE LAKLLNFPVT NTLMGLGGYP
     GTDRQFLGML GMHGSYEANM AMHHADLILA VGARFDDRVT NATDKFCPTA RIIHIDIDPA
     SISKTIRADV PIVGPSKVVL EEMVSLVKES TKKPDAAAID SWWKQIDEWR GRHGGHYRTD
     DSELMKPQQV IEMLSKVTNG DAFVCSDVGQ HQMFAAQYYK FNKPNRWINS GGLGTMGFGF
     PAAMGVKMNF PDADVACVTG EGSIQMNIQE LSTCKQYDIP VKILCLNNQS LGMVRQWQDM
     NYESRHSQSY MKSLPDFVKL VEAYGHVGMK VDKYADLEGA MREAFALKDR LVFMDIAVDP
     YEHVYPMQVP RGSMRDMWLS KTERT
//
DBGET integrated database retrieval system