ID A0A395H9U4_9EURO Unreviewed; 454 AA.
AC A0A395H9U4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:RAL04450.1};
GN ORFNames=BO80DRAFT_452539 {ECO:0000313|EMBL:RAL04450.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL04450.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAL04450.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL04450.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; KZ824424; RAL04450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395H9U4; -.
DR STRING; 1448316.A0A395H9U4; -.
DR VEuPathDB; FungiDB:BO80DRAFT_452539; -.
DR OrthoDB; 125961at2759; -.
DR Proteomes; UP000249402; 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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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 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 PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402}.
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 454 AA; 50847 MW; FB91459C2FDB2A8A CRC64;
MEKIVWDVFR ELPGIVEEHK LFCEQGDLIK RPTRKQVADL SESSPPEKGR SLENVVRDTE
EILSFRFSTG NPRFFSFLGD ALTTAFNNYA GSFESGAGIS AIEDSIIRWV AERFGMPLSA
GGQFVSGASI ACLTALTVAR DQLVEEDMRT KAVAYLSEET HFCVAKTLRV TGLLERQIRT
VPCNAKFQMD PDHLRSAIVQ DIKDGLKPYV VVATSKEYKM WIHVNAAYGG SVAFCESHRA
LLQGMGRADS IAWDPHKWLF QTLGCSVVMS RERSHPTKSF AVGAHFLRDL EEDETKNPFN
YGIELFRPAR HMRLWFSLQV LGTDTVDRMI SRGFELAGLA ESELRELADW EIVSPNTLAV
LDFRFNPKGM IADDVDRING LVSKELAAQN IGVVFTTCIH GAVCLRICTI NPQTTDNDIR
DVIKALDQNA RLISKRFPKT ETGFEDRLVS LDAQ
//
