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Entry: A1CCJ7_ASPCL
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ID   A1CCJ7_ASPCL            Unreviewed;       509 AA.
AC   A1CCJ7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   14-MAY-2014, entry version 40.
DE   SubName: Full=Aromatic-L-amino-acid decarboxylase;
GN   ORFNames=ACLA_062170;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC
OS   3887 / NRRL 1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
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DR   EMBL; DS027050; EAW12254.1; -; Genomic_DNA.
DR   RefSeq; XP_001273680.1; XM_001273679.1.
DR   ProteinModelPortal; A1CCJ7; -.
DR   STRING; 5057.CADACLAP00005893; -.
DR   EnsemblFungi; CADACLAT00006030; CADACLAP00005893; CADACLAG00006030.
DR   GeneID; 4705966; -.
DR   KEGG; act:ACLA_062170; -.
DR   HOGENOM; HOG000121941; -.
DR   KO; K01593; -.
DR   OMA; TARLEDN; -.
DR   OrthoDB; EOG75B8FF; -.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010977; Aromatic_deC.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Lyase; Pyridoxal phosphate.
SQ   SEQUENCE   509 AA;  57220 MW;  9F59F7F7F583B742 CRC64;
     MDREQFRAAA HAAIDEIVDY FDGLPSQRVL PTIEPGYLRP LIPESPPDEP EQWSQIQADI
     ETKIKPGLTH WQSPNFMAFF PAGVTYPSIL GEMYSAAFTA PAFNWLCSPA CTELETIVMD
     WMAQALGLPQ CFYSNSENKG GGVIQVSASD AVATVMIAAR ERRVREQVLA EGLTDGSAEY
     EDRVMELRPR LVALGSNQAH SSTAKGALLA GTRYRSVTAR LEDNMEMTGP RLREVLEQCD
     KDGLTPYYIT LGMGTTNTCA LDRFAEIKAV LKEKPHWQRI WVHIDAAYAG AALVADEWQY
     IAKDFAEGVD SFNVNMHKWL LVNFDASCLY IRNRFDLTDA LDITPAYLRN PYSETGKVID
     YRNWSISLGR RFRALKIWFV MRSYGLNGMK SFIRKTIALG DIFADLIRSR PDLFEIITRP
     AFCLTVFRIK GPKLVGSSVP QVDEESNSLT KEVYELINSR GEIFITSSVV AGVYAIRVVS
     ANPAAEEKYL RRAFEILVQT TDEVLQRQQ
//
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