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Database: UniProt
Entry: A0A0G2HPV6_9PEZI
LinkDB: A0A0G2HPV6_9PEZI
Original site: A0A0G2HPV6_9PEZI 
ID   A0A0G2HPV6_9PEZI        Unreviewed;       965 AA.
AC   A0A0G2HPV6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Putative pyridoxal-dependent decarboxylase domain protein {ECO:0000313|EMBL:KKY30245.1};
GN   ORFNames=UCDDA912_g09818 {ECO:0000313|EMBL:KKY30245.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY30245.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY30245.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY30245.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY30245.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY30245.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KKY30245.1}.
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DR   EMBL; LCUC01000512; KKY30245.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2HPV6; -.
DR   STRING; 1214573.A0A0G2HPV6; -.
DR   OrthoDB; 1607139at2759; -.
DR   Proteomes; UP000034680; 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   Reference proteome {ECO:0000313|Proteomes:UP000034680}.
SQ   SEQUENCE   965 AA;  105932 MW;  18D429E2C7F0AE16 CRC64;
     MTTFNLGGAT LQSGINVPGF GKASGSSGLN IPKLGSISSN VGVDLSKGVN GLTGDIKLTK
     DKGNVFRSGA TGSAAVNDVS HQAVCSYFIG PQAENMKYFR KNMDEILNQL EQSRVNYFPE
     DGAFITEQIQ NSAEFQDRTT AVAKAIQKTG ELLGKHSIPF WSPRYQAHMS NLESMWAARN
     LKFYPLSLRM AFDGPLANVG KTFTVVNAQN KEDLMLKMPT WDLLNLKVET ILDLPDRLNR
     DYGISSKYLE NVLDNYGIQS IGKDEIEKHF GIEKPAQYML SSTRHYSWPK GAAIAGIGSQ
     NVVSIAVDHG ARLDLSKLEE QLGLSLKEKQ PVYAVVAIIG STEEGAVDRL GEILNMRRRF
     QARGLSFVVH ADAAWGGYFA SMLPKDYTPG SKFSGPLPAG LGPAEGFVPD SGLRPDTQED
     LWWLRFADSI TVDPHKAGYI PYPAGGLCYR DGRMRCIGLN PDGYGALLGE VTFTCSRLSA
     QWAAMSDDSM PFTVVPFNML PSELEDGATK ESIEAERQWI RDNILSASNL EIVSNTSTSP
     GGDDALTLLR KLGSDLNINA FACNFKYSNG DLNTDVLEAN YFMQRIVESL SVDSPGDDPT
     KIPLYLTSTE FSTDLYGECA AKFKERLGLK DGNQDLFVLR NVVMSPFPTE KDFIAELAGI
     FKKVALEAVS VSRGRNEETK GIHSFLIQGE NPVYLLHKPS FHVANHRRQT VLEVELPKAA
     QEWYSTLRSQ YPGEIFTFKT VKDVDLTEAI KNGGDLTGFI TSGSSHGAPM LPNFTLNITK
     PIIDRHLNGL YLASSYPTGR MPFYLYGSST EHHIDHALLT SPNIQLSAGD IKLGLSDSSG
     LPSDGSRPLV LMLDNVREEQ MQPFPSKNSV LASLPDFFFQ PGKEFEVSIW EDPTPSENDA
     ESILSAWEAL GRDGNENGLV GRGTIVLGES VFVDAESLNF DPYKKVDDVG AWTEEFAKIG
     RELQK
//
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