ID   F8MF82_NEUT8            Unreviewed;       532 AA.
AC   F8MF82;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=PLP-dependent transferase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=NEUTE1DRAFT_57882 {ECO:0000313|EMBL:EGO60936.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO60936.1};
RN   [1] {ECO:0000313|EMBL:EGO60936.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO60936.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
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; GL891302; EGO60936.1; -; Genomic_DNA.
DR   RefSeq; XP_009847323.1; XM_009849021.1.
DR   AlphaFoldDB; F8MF82; -.
DR   GeneID; 20828636; -.
DR   KEGG; nte:NEUTE1DRAFT57882; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_57882; -.
DR   HOGENOM; CLU_011856_6_2_1; -.
DR   OrthoDB; 51460at2759; -.
DR   Proteomes; UP000008065; 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; 3.90.1150.10; 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   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.
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}.
FT   MOD_RES         377
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         532
FT                   /evidence="ECO:0000313|EMBL:EGO60936.1"
SQ   SEQUENCE   532 AA;  58093 MW;  682C0D84D5116DD6 CRC64;
     MASTPLPDHI QPTFVDEILK PIESRISELL DEFCPVNQGT ERLNDVKKLV VSYTVLQILT
     QTFDPNLYVT PRPEDLAHAE AWVENYCRDS SIYSGGEPPQ NPGFAGDGKE FYSTLTHILA
     DIVPALNSQA LSSRYYGFVT GGVHPVAQAA DNVVTALDQN VQVHMPSTHS ISTVVEHHAL
     SMLRSLLDLD GFHGKTFTTG ATASNIMGLA CGREAVISAR LPDYAKNTGG VGELGLLAAC
     MAAGVKEVQV LTSKGHSSLY KAASVVGLGR AAVRDLGLAD APWLLDLKAV ERELKREDVA
     NIIVVSAGEV NTGHFGTTGE TMKELRQLAD RYKAWIHVDG AFGIFARALP KTERFAKLFE
     RTAGLELADS IAADGHKLLN VPYDNGIFFC SSPEVMSHVF QNPNAAYLAP VALTSRSGTT
     TDIQSPLHVG LENSRRFRAL PVYALLVHLG RDNMGEMLAR MVDLARRIAA FIRDSDKYDL
     LPDETADIEC THIIVLFKAK NPDLNEALVG KINETRRMYE VGGLMLKKIW RL
//