ID L5KQB4_PTEAL Unreviewed; 467 AA.
AC L5KQB4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Pyridoxal-dependent decarboxylase domain-containing protein 1 {ECO:0000313|EMBL:ELK13547.1};
GN ORFNames=PAL_GLEAN10009731 {ECO:0000313|EMBL:ELK13547.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13547.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; KB030624; ELK13547.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KQB4; -.
DR STRING; 9402.L5KQB4; -.
DR eggNOG; KOG0630; Eukaryota.
DR InParanoid; L5KQB4; -.
DR Proteomes; UP000010552; 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:SF1; PYRIDOXAL-DEPENDENT DECARBOXYLASE DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552}.
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 51304 MW; C4414B97425BA801 CRC64;
MGKNLKEAMK MLEDSQRRTE EENGKKLMSG DIPGPLQGSG QDMVSILQLV QNLMHGDEDE
EPQSARIQNI GEQGHIALLG HSLGAYISTL DKEKLRKLTT RILSDTTLWL CRIFRYENGC
AYFHEEEREG LAKICRLAIH SRYEDFVVDG FNVLYNKKPV VYLSAAARPG LGQYLCNQLG
LPFPCLSRVP CNTMFGSQHQ MDVALLEKLI KDDIERGKLP LLLVANAGTA AVGHTDKIGR
LRELCEQYGM WLHVEGVNLA TLALGYVSSS VLAATKCDSM TLTPGPWLGL PAVPAVTLYK
HDDPALTLVA GLTSNKPADK LRALPLWLSL QYLGLDGIVE RIKHACQLVE DELSSPVVVF
RFFQELPGSE PVLKAVPAPN TAPSVVGRER RSCDALNRWV RGQSCASSAP WVVAMAPGHV
RETRPDEGAL CEDAGLRSAV LFLIASPPHK PCDFWEALSM LSPPGFT
//
