ID A0A1F7ZY65_9EURO Unreviewed; 1025 AA.
AC A0A1F7ZY65;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Pyridoxal-dependent decarboxylase domain protein {ECO:0000313|EMBL:OGM43988.1};
GN ORFNames=ABOM_008013 {ECO:0000313|EMBL:OGM43988.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM43988.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM43988.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(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 -!- 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:OGM43988.1}.
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DR EMBL; LYCR01000062; OGM43988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZY65; -.
DR STRING; 109264.A0A1F7ZY65; -.
DR OrthoDB; 1607139at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF4; TYROSINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179}.
FT MOD_RES 434
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 1025 AA; 115847 MW; D04BA5DF687A5D5D CRC64;
MGDAGPPKIS NHDLISSYFI GPKSENLKPF SDNIAIILDQ LKKTRDNYGG HDEIFISDTA
QKKLEPVYQK FKEAVQKTAT LLGEHSIPFW HPRYQGHMCT DMTMPGLLGY FMTMIYNPNN
VAVEASPFTT VVELKVGQQL CEMFGYNINE KATHLPLSWG HITCDGTVAN LESIWVARNL
KFYPLTLYQA MKEGPLGFIA NDFQVTTCVG EEKLFKDLGV WELLNLQPDV ILDMGDALYR
QFGVTSKFLE QALTPFTIQT TGKDVLEREF RITKPAKYFL AQTRHYSWPK GGAIAGIGSA
NMQGVELDME GRISLDALER ELNRCLEEHQ AVYAVVAVIG TTEEGGVDRL HEILAMRRRF
QDRGLSFLVH ADAAWGGYFA SMIPRHMMDP TKPIDEEDGN TAVDEVPQLA LRQDTLTDMI
ALKEADTITV DPHKAGYIPY PAGSLCYRDG RMRFLVTWTS PYLTQGSTEN IGVYGVEGSK
PGAAAMAAWM SNQTIGLSPS GYGRLLGEAA FTSARLSAWY AAMHVDQPGW KEERPYYIII
PFNPLPIEKE GNGSLSDKVN TRREEILDNV IKKTNEEISK DEKVMDWLRN IGSDLNINAF
AINWYDENGK LNTELEEANY LMRRVVNRLS ITTTQGKAEK PLLFLTSTQF EPAMYGQCAQ
NFMRRLGLTP CAQDLWVLRN VVMSPFPTTK DFIRKLMKEE LEKVIIEEVK HCRTRNSRDQ
KELEFLLRGT DEVFLDFQTS FHRATQRQQI ILAATLAEDT KKDYIALKQK FLTQDIVFKS
TASHNLKELI DKIKEGTKSE TATEVEGVIG ARNGEAFIGT PIQCTVKMIR VVKSRPLNSA
NRDDHYPRHF MPFYLYGSED QYHISHMLLQ APNVNLSASD VQLDQELLKK VRPRLRNHNA
LILTLTGYRE ETMHPFPKKN NDDVLLSKDF FFRQDKVFNV KVYEDPKADD AQGPGLIDTL
GTPIARGTMK LGSDVHIDVE TLNRDPLETN EEGVRWDTKL DEIKDAFEEG RKLASGMAPQ
AAVVS
//
