ID A0A074X6B1_AURPU Unreviewed; 487 AA.
AC A0A074X6B1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:KEQ80943.1};
GN ORFNames=M438DRAFT_280347 {ECO:0000313|EMBL:KEQ80943.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ80943.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ80943.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ80943.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584994; KEQ80943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074X6B1; -.
DR STRING; 1043002.A0A074X6B1; -.
DR HOGENOM; CLU_011856_6_2_1; -.
DR OrthoDB; 51460at2759; -.
DR Proteomes; UP000030706; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:SF165; DECARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04980)-RELATED; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
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:UP000030706};
KW Transferase {ECO:0000313|EMBL:KEQ80943.1}.
FT MOD_RES 305
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 487 AA; 51971 MW; A60AD5F9A0A572BB CRC64;
MEAADSTPPS DLPVLPSISQ LDLARSSLRR ELVPALGFAG TQQHLTHVIA PALNGNSQSS
RYYGFVTGGA TPAAVFADKM VTDYDQNVQV HLPNETVATD VEAAALDLVC QLVELDPKEW
THRTFTTGAT SSNINGLACG REYVISTAAA RNNTKADVSS LGLMAAMRVA GIDDIQILTS
APHSSLRKAA SVLGLGHDSV KDVSDPTAPH RLDLEALENA LQSPRAASII AISCSEVNSG
LFATTGKDMV QLRRLADEYG AWLHVDAAFG LLARILPSDE PAYAQLKEGV ESLQLADSIA
ADAHKLFNVP YDCGILLSRH LDVGTAVFQN PGAPYLNAAA GSVPSPLNIG IENSRRFRAL
PVYANLVAYG RSGFVNMLEN QIALARGIAS YIQSSSVFKL LPEVESGSMD PLSRVFIIVL
FKAINSELND TLVKKINATR KIYVSGTKHA GQPACRFAIS NWQTSVEKDL AVIIDVLETV
SSGHNKQ
//
