(data stored in ACNUC7421 zone)

SWISSPROT: Q47SH6_THEFY

ID   Q47SH6_THEFY            Unreviewed;       553 AA.
AC   Q47SH6;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:AAZ54591.1};
GN   OrderedLocusNames=Tfu_0553 {ECO:0000313|EMBL:AAZ54591.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54591.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP000088; AAZ54591.1; -; Genomic_DNA.
DR   RefSeq; WP_011291000.1; NC_007333.1.
DR   STRING; 269800.Tfu_0553; -.
DR   EnsemblBacteria; AAZ54591; AAZ54591; Tfu_0553.
DR   KEGG; tfu:Tfu_0553; -.
DR   eggNOG; ENOG4105CFN; Bacteria.
DR   eggNOG; COG0028; LUCA.
DR   HOGENOM; HOG000010642; -.
DR   KO; K01652; -.
DR   OMA; PGPYGCL; -.
DR   OrthoDB; 391134at2; -.
DR   BioCyc; TFUS269800:G1G4Q-564-MONOMER; -.
DR   Proteomes; UP000000434; 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;
DR   PRODOM; Q47SH6.
DR   SWISS-2DPAGE; Q47SH6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN       14    180       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      199    330       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      391    538       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   553 AA;  58142 MW;  EDC5CAEFB904B37E CRC64;
     MGSPSFSGKL TGHGGNHAVE VARHHGVDTL FTLSGGHIFP IYDGAVKADP PMRLLDVRHE
     QTAVFAAEAV GKLTRRAGWA ALTAGPGVTN GVSGIATAHF NGSPLVVVGG RAPDNRWGQG
     LLQELDQSPL FTTITKRAWT VHDTAQIGPA LDEAFTLANT AHRGPVFLDI PMDRLYDQAE
     ITVTGQAAAE DRSPDPDAVA AVARLLSEAE RPVLVYGSDV WLDHAEQAAL EAAEELGVPV
     VTNGQGRGVL PAGHPLLATR ARGLALGRAD LVIVVGTPLD FRLNHGLFGG RDGAPLARTV
     HITDSPAQLA THLTLAGAVS GDLSAILRAL AEQAKPKREV AQWRTEVAEA AAATAAKDRE
     VLDSDASPIH PARIYGELNR ILDDDAVVIG DGGDFVSYAG KYIQPRRPGN WLDPGPFGCL
     GTGMGYAIAA RLVRPSSQVV ALFGDGALGF SLADVDTLVR HNLPVVMVCG NNGIWGLEKA
     PMQLVYGYDV LADLAPQTRY DQVVTALGGG GELVTDPAEI GPALRRAFDS GVPYLVNIVT
     DPENVYPRKT MGV
//

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