(data stored in SCRATCH zone)

SWISSPROT: C8VM21_EMENI

ID   C8VM21_EMENI            Unreviewed;       399 AA.
AC   C8VM21;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   30-AUG-2017, entry version 51.
DE   SubName: Full=Acetyl-CoA acetyltransferase, putative (AFU_orthologue AFUA_8G04000) {ECO:0000313|EMBL:CBF84799.1};
GN   ORFNames=ANIA_01409 {ECO:0000313|EMBL:CBF84799.1};
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:CBF84799.1, 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 thiolase family.
CC       {ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; BN001307; CBF84799.1; -; Genomic_DNA.
DR   STRING; 162425.CADANIAP00008019; -.
DR   EnsemblFungi; CADANIAT00008019; CADANIAP00008019; CADANIAG00008019.
DR   InParanoid; C8VM21; -.
DR   OMA; LMAGQGQ; -.
DR   OrthoDB; EOG092C2K2G; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005622; C:intracellular; IDA:AspGD.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8VM21.
DR   SWISS-2DPAGE; C8VM21.
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Transferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:CBF84799.1}.
FT   DOMAIN        7    267       Thiolase_N. {ECO:0000259|Pfam:PF00108}.
FT   DOMAIN      275    396       Thiolase_C. {ECO:0000259|Pfam:PF02803}.
FT   ACT_SITE     92     92       Acyl-thioester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR000429-1}.
FT   ACT_SITE    354    354       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000429-1}.
FT   ACT_SITE    384    384       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000429-1}.
SQ   SEQUENCE   399 AA;  41073 MW;  7D7B881C8BBA0F67 CRC64;
     MASLPPVYIV SYARTPVGSF LGSLSSQTAP QLGSHAIKAA LERADGIKPS DVQEVFFGNV
     LSANVGQNPA RQCALGAGLE TSTVCTTVNK VCASGLKAVI LGAQTIMTGN ADVVVAGGTE
     SMSNTPHYLP NLRTGAKYGN QTMVDGIVKD GLTDVGKQEL MGLQAEECAQ DHGFNRQQQD
     DYAIRSYEKA QAAQAAGLFN DEIAPIDLPG FRGKPGVTVT QDDEPKNLNP DKLRAMKPAF
     IPGTGTVTAP NSSPLNDGAA AVVLVSEAKL KELNLKPVAK ILGWGEAAQQ PSKFTTAPAL
     AIPRALKHAG VSQDAVDAFE INEAFSVVAL ANLKLLGLSE DKVNIHGGAV AIGHPLGASG
     ARILTTLLGV LKARKGKVGC AGICNGGGGA SALVVEYIA
//

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