ID A0A137P817_CONC2 Unreviewed; 530 AA.
AC A0A137P817;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:KXN71132.1};
GN ORFNames=CONCODRAFT_17131 {ECO:0000313|EMBL:KXN71132.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN71132.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN71132.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN71132.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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|RuleBase:RU000382}.
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DR EMBL; KQ964483; KXN71132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137P817; -.
DR STRING; 796925.A0A137P817; -.
DR EnsemblFungi; KXN71132; KXN71132; CONCODRAFT_17131.
DR OMA; AGMVIFK; -.
DR OrthoDB; 888358at2759; -.
DR Proteomes; UP000070444; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.170; -; 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 PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-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|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000070444};
KW Transferase {ECO:0000313|EMBL:KXN71132.1}.
FT MOD_RES 322
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 530 AA; 59103 MW; C526663AE360115D CRC64;
MVTEPELLKS IINNNSNNEF QTGEFSGEAE EFDQLLTLIK SKLKNYINEG TNNSEACPAI
TPIDKRELSK VLNLNLTKKG EGHEGVDKLV DNVLKYSVNG WTPNYCDKLC SSTTPIGVMS
ELILGALNAT AHVYHVSPCL IQMELAAGRE LTNLLGYSGP SRGGLTFPGG SQSNFMAISL
ARNLKFPSIK INGFDGEKLA IFTPQQGHYS IDKAAISLGV GLKRVYKVPC NIDGSMIPEQ
LELMIQQSIR NGEQPFFVNS SAGSTVLGAF DDFGKISQIC KKYDLWYHID GSWGGSIIFS
KTHRHLLNNA ELSDSFTVNP HKLLGVPVQC SYLLLQDRFL LNQAHTLNAD YLFHNNDTAT
NSTTSPDSLD PDSWLYSNMD LADGTVGCGR RPDGFKMFLT WKYVGTEGFT KRVDHALSCA
QFFQHKIQQH PNFKLLVPAT SLNVCFYYLP SCRDQGLFDE TVLTTNSEIP QIPEHYSYIT
KDIIEMMKEE GKIMIDYSHS KMVFNHPKTS EASISNLINE INRFGHELME
//
