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Database: UniProt
Entry: G1X552_ARTOA
LinkDB: G1X552_ARTOA
Original site: G1X552_ARTOA 
ID   G1X552_ARTOA            Unreviewed;       563 AA.
AC   G1X552;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   28-FEB-2018, entry version 27.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX51807.1};
GN   ORFNames=AOL_s00043g826 {ECO:0000313|EMBL:EGX51807.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Arthrobotrys.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX51807.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX51807.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L.,
RA   Luo Y., Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L.,
RA   Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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:EGX51807.1}.
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DR   EMBL; ADOT01000061; EGX51807.1; -; Genomic_DNA.
DR   RefSeq; XP_011119614.1; XM_011121312.1.
DR   EnsemblFungi; EGX51807; EGX51807; AOL_s00043g826.
DR   GeneID; 22890581; -.
DR   InParanoid; G1X552; -.
DR   OrthoDB; EOG092C29BL; -.
DR   Proteomes; UP000008784; 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   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; 2.
DR   SUPFAM; SSF52467; SSF52467; 2.
DR   SUPFAM; SSF52518; SSF52518; 2.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008784};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN        9    155       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      191    340       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      421    531       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
FT   METAL       467    467       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR036565-2}.
FT   METAL       494    494       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR036565-2}.
FT   METAL       496    496       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR036565-2}.
SQ   SEQUENCE   563 AA;  61873 MW;  BEE1D63DC71A9DE3 CRC64;
     MADETEIVNY LFKRLYQLGI RSVHGVPGDF NLVALDYLDP AGLNWVGNCS ELNAGYAADG
     YARINGISAL ITTFGVGELS AVPAIAGSYS ERVSIVHIVG VPSTKTEKHG LPIHHTFADG
     DYSAFKNISK TISQACITLD DAKIAGKEID RVLRALPVDM VLSKTPAQGL DNPIDLTVPR
     NDLDTETEAV EAIKKALYGS SNAIILVGVG AMQYRVLKEV QEFIDLSQLP VFLTPMVRAP
     KKPQEQSINT DLRVNSALYG QEKLMLHVET SVHSQFRGVY NGDASGPEIQ QAIQSADLVV
     FIGPLNTDFN SGGFTSYTKT KNTIEFQSNF TKVGYATYLD VGMKLVLPRI LDSIDVRKIQ
     HPQTNITKVE KPIDVEAKIT EPSDQEVTQQ WFWGHIGDWL QEGDVVVAET GTSSFGIMDT
     RFPKGVTAIT QILWGSIGFS VGACQGATLA IAESERPTRR VILFVGDGSF QLTGNEISTM
     IRHGLKPIIV VLNNDGYTTE RKIHGPEMSY NDIQPWKYRK FLKAFGARKG EYKNYVVRTQ
     SECYGLFNKG NEFSKANVIQ ATS
//
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