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Database: UniProt
Entry: A0A0K1PQX5_9DELT
LinkDB: A0A0K1PQX5_9DELT
Original site: A0A0K1PQX5_9DELT 
ID   A0A0K1PQX5_9DELT        Unreviewed;       584 AA.
AC   A0A0K1PQX5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   28-FEB-2018, entry version 10.
DE   SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:AKU95927.1};
GN   ORFNames=AKJ09_02591 {ECO:0000313|EMBL:AKU95927.1};
OS   Labilithrix luteola.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Labilitrichaceae; Labilithrix.
OX   NCBI_TaxID=1391654 {ECO:0000313|EMBL:AKU95927.1, ECO:0000313|Proteomes:UP000064967};
RN   [1] {ECO:0000313|EMBL:AKU95927.1, ECO:0000313|Proteomes:UP000064967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27648 {ECO:0000313|EMBL:AKU95927.1,
RC   ECO:0000313|Proteomes:UP000064967};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M.,
RA   Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J.,
RA   Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L.,
RA   Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J.,
RA   Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L.,
RA   Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z.,
RA   Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J.,
RA   Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W.,
RA   Hatfull G.F.;
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP012333; AKU95927.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKU95927; AKU95927; AKJ09_02591.
DR   KEGG; llu:AKJ09_02591; -.
DR   PATRIC; fig|1391654.3.peg.2629; -.
DR   KO; K01652; -.
DR   Proteomes; UP000064967; Chromosome.
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   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; 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   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000064967};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064967};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN       20    190       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      211    349       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      412    561       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   584 AA;  63018 MW;  FCDDD35139CDD572 CRC64;
     MTISQSPPPG SVRPAPAPRV IDVFLKYLKA EGVNVVFGIP GGLLYPFFAV IESDPDMQLV
     MTKHEQGAAF MADGYARAGR RLSCCAGTAG PGATNLLTGV ACAFADGVPM LVVTGQAASH
     ALGKGAAQET SREDMDIVAM FRPVTKYSAM VISPESMAQH LRRALRLALT GRPGPVHLNV
     PVDLWEKPLH EAWFDPKTYR PDTRTFDRVA VQRAASLLMN AKRPILFAGA GVGTAVAEEH
     LRALAELLPA RVATTPRGKG LFPEDHPLSL GVLGFAGHAA ARETILGPNV DLLMTIGTSL
     NETATLNWAP ALRKNRTFIQ LDIDADRIGR NYPVDLALVG DAQTILVELV YHLHRSMREG
     GTIASQWDTA APAKRVFSDG ELRDSDRVPL TPQRWRKDFE EAVPNDATVF SDIGGHMLSN
     IHYLTMKDRQ RFMINLGFGS MGHGTVAPIG AALAQPQHPT IAIIGDACFT MCGMDLVTAV
     EYEIPKLVWI VENNNMHGIT WHASRALASG ALSSVRYKRP LEVAAIARAM GLAAWIVDGP
     NQMQSTLRDA LKVRGPSLIE VRVDPAVPPP IGDRVKSIAG FVDK
//
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