ID   A0A100I6M2_ASPNG        Unreviewed;       987 AA.
AC   A0A100I6M2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:GAQ35682.1};
GN   ORFNames=ABL_01270 {ECO:0000313|EMBL:GAQ35682.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ35682.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAQ35682.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BCMY01000002; GAQ35682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100I6M2; -.
DR   VEuPathDB; FungiDB:An03g01690; -.
DR   VEuPathDB; FungiDB:An03g01710; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1166551; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1186414; -.
DR   VEuPathDB; FungiDB:ATCC64974_83650; -.
DR   VEuPathDB; FungiDB:ATCC64974_83670; -.
DR   VEuPathDB; FungiDB:M747DRAFT_281589; -.
DR   VEuPathDB; FungiDB:M747DRAFT_59805; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR008854; TPMT.
DR   PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   Pfam; PF05724; TPMT; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
DR   PROSITE; PS51585; SAM_MT_TPMT; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   MOD_RES         779
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   987 AA;  108563 MW;  975C4B68CFDEA68C CRC64;
     MAHTPNPPVQ GRLISHFAER SAEDQGSGWS ALWDSNESDL WDRGSPSIAL VDVVEQQTDV
     FSPFTPDKQR KRALVPGCGR GYDPVMLALH GFDVYGLDIS ATGVSEARKY AASEMQSPQG
     YNFASETATT ADIGNVKFVA GDFFSSEWES EALRDGEKFD LVYDYTFLCA LHPSLRQKWA
     ERMSHLLHPG GLLVCLEFPM YKDPSLPGPP WGLKGVHWDL LARGGDGICN IAEEEEDDTE
     AAKLKGQFRR AQYFRPTRSY PSGKGTDLLS IYYSDNGTEP ALSFSVVPDE RFILTDYPAR
     SAAGKVAHRP TSTSNCVNEY ASLIIYPVNN STAGLDPAAL LEGDLTDSIC PTANSTFLRN
     QQNIPDPLNG PQLLGWEPVN SSITSGGKVL RFGADGKAVQ QVDRVEIDGT VPRHWEIRPV
     PISVTQSLLR TLARPDFIKP HHWPPGSGYV DSHLDTIHAS LFSSPPVKVT RESDHSSKFV
     NMHFNTPQDP SDEGWTEVML IARSLLNQLL TTDLPLPSDP ILPILDTSEL PSLQDKIMPD
     DHPRDPVSIL QQAMTLFDYH IHHTHPHSFA YIPACPIPIA RLGALLTSVC NVNVANWDAS
     SGPSEVEKAM IHWLGSQLGL PDSVRGCFVS GGSMANMTAI VAARDEKLQP LQRANATIYM
     SDQTHLSVMK ALHIAGFMDY QVHKIPTDDN CCMDVNLLRH AIKTDRLFGR VPFLLVANCG
     STNTGTIDPL HELADIARDE GLWLHVDGAY GASIALSDKH RHLVDGIGRA DSVSWDGHKW
     LFQTYGCGIV LTRHVNSLAR SFSFDAEYIT GPLEPQATTS FYKLGPELSR PARAMSLWLT
     LKVLGRRRVG EMIDQGFLLT RTADHSIRQC KNWIIPVPTV ASIVVFRYAP PGFSEEELDS
     LNSAISQRLV AENIASILTT QIRGRTTLRM CAMNPAVQPE TISEVISRVD KVAQAEASKV
     KKTYPKMSNG LCSPLISCCV VEASDHA
//