(data stored in ACNUC16935 zone)

SWISSPROT: C8VMP9_EMENI

ID   C8VMP9_EMENI            Unreviewed;       605 AA.
AC   C8VMP9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-JUL-2017, entry version 42.
DE   SubName: Full=2-hydroxyphytanoyl-CoA lyase, putative (AFU_orthologue AFUA_8G05230) {ECO:0000313|EMBL:CBF85026.1};
GN   ORFNames=ANIA_10214 {ECO:0000313|EMBL:CBF85026.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF85026.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; BN001307; CBF85026.1; -; Genomic_DNA.
DR   ProteinModelPortal; C8VMP9; -.
DR   STRING; 162425.CADANIAP00008143; -.
DR   EnsemblFungi; CADANIAT00008143; CADANIAP00008143; CADANIAG00008143.
DR   HOGENOM; HOG000053808; -.
DR   InParanoid; C8VMP9; -.
DR   OMA; PYLPMSM; -.
DR   OrthoDB; EOG092C1NSE; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005777; C:peroxisome; IEA:EnsemblFungi.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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; 3.
PE   3: Inferred from homology;
DR   PRODOM; C8VMP9.
DR   SWISS-2DPAGE; C8VMP9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000560};
KW   Lyase {ECO:0000313|EMBL:CBF85026.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN        5    170       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      198    325       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      400    580       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   605 AA;  64769 MW;  793B91951520DE83 CRC64;
     MAIRTGAQII ARSLRDLGVT VIFGIVGIPV VEIAEEAINL GIRFVAFRNE QACSYAASVY
     GYMTGQPGVC LVVGGPGVLH ALAGIGNSSA NNFPLLVLAG SAETSAVTKG AFQELDAISL
     LTPHTKFAAR ASSLDFIPDA IKNAYRTCWY GRPGPTFIDL PADIIQGKLT SQFELPKPEN
     LLVSAPPKAS GDPALILKAT QLLKAASAPL IIVGKGAAYA RAELGIRKLV DQTQVPFLPT
     PMGKGVVPDS HPLNASSARS AALKHADVVL VLGARLNWIL HFGEPPKWSP KVKIIQVDIC
     AEEIGRNAGT SELGILGDIS LVVDQFRASL SSWKYSSSAK FPLLLAESAK KNEDKAQKAA
     LRQTPAGKPL TYQRAYHIIK TALNALTPVE DGNIVYVSEG ANTMDISRSI FPLYHPRQRL
     DAGTYATMGV GMGYIVAAHE AFNANPGAST SRPKKIVAFE GDSAFGFSAM EIETLARYRI
     PALIFVINNS GIYHGDSISK EDWKTLQNQT VANDTKTSES DSGTNAKTKG LRSTSLLYET
     RYEMLATMCG GKGYFVKSEE ELERATKEGF VSDTVTIVNV IVEPGIGKEI GFAWQNQGKE
     SKPKL
//

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