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Database: UniProt
Entry: A0A166WAX7_9HOMO
LinkDB: A0A166WAX7_9HOMO
Original site: A0A166WAX7_9HOMO 
ID   A0A166WAX7_9HOMO        Unreviewed;       596 AA.
AC   A0A166WAX7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   30-AUG-2017, entry version 7.
DE   SubName: Full=Pyruvate decarboxylase {ECO:0000313|EMBL:KZP33569.1};
GN   ORFNames=FIBSPDRAFT_720711 {ECO:0000313|EMBL:KZP33569.1};
OS   Fibularhizoctonia sp. CBS 109695.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Atheliales; Atheliaceae;
OC   Fibularhizoctonia.
OX   NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP33569.1, ECO:0000313|Proteomes:UP000076532};
RN   [1] {ECO:0000313|EMBL:KZP33569.1, ECO:0000313|Proteomes:UP000076532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP33569.1,
RC   ECO:0000313|Proteomes:UP000076532};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; KV417482; KZP33569.1; -; Genomic_DNA.
DR   EnsemblFungi; KZP33569; KZP33569; FIBSPDRAFT_720711.
DR   Proteomes; UP000076532; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   Gene3D; 3.40.50.1220; -; 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; IPR012110; TPP_enzyme.
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   PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000076532};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Pyruvate {ECO:0000313|EMBL:KZP33569.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN       29    203       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      247    351       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      438    573       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
FT   METAL       475    475       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR036565-2}.
FT   METAL       502    502       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR036565-2}.
FT   METAL       504    504       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR036565-2}.
SQ   SEQUENCE   596 AA;  65515 MW;  EFF81CB27A0DEB4C CRC64;
     MSDITSLQAE VKRLQSELNT LDVGGEKITV SEYLLKRLEQ LGVKHMFGVP GDFNLAFLDY
     VEDSPAINWV GNCNELNAAY AADGYARVNE HSIGVITTTF GVGELSAING IAGAFSEMVP
     ILHIAGVPST DQQLHKTLLH HTLGDGRFDA YRKASDQFTI AQADITSAAT AGAQIDYLLT
     ELITHVRPVY LTLPTNMVAV KISSASLSIP LTPTVVPNDP ETEKFVLEEI AKLAKVAEES
     DDGKDGVVIL VDACAIRHGV RDEVKELAEK TGFPVYAAPM GKTAIDEDWE RYGGIYLGSL
     TAPAIKERIE NARLIISVGS LKSDFNTGNF TYRIPTRNTV ELHSGHTTVQ YASFPGIGMK
     ELLPKLSEVL ATHRASALKI SVPHYRAVVP QDNEKSIMQD WFWPRMAQWF KPKDVIVSET
     GTSNFGLLDV PLPAQSIFVS QILWGSIGWA TGSALGAAIA AQDRGLGRTM LFIGDGSVQL
     SAQEIATMVK LGLKPILFIL NNEGYTIERC IHGKRRKYND IQNWNWPELL KFFGDDAKGE
     KSRSYTVRTK EELEALLADA TFVSADKIQL VEVIMDKYDA PRALRYVCFE YNAGLR
//
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