ID   A0A1Y2B2H7_9FUNG        Unreviewed;       524 AA.
AC   A0A1Y2B2H7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:ORY28697.1};
GN   ORFNames=LY90DRAFT_460911 {ECO:0000313|EMBL:ORY28697.1};
OS   Neocallimastix californiae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY28697.1, ECO:0000313|Proteomes:UP000193920};
RN   [1] {ECO:0000313|EMBL:ORY28697.1, ECO:0000313|Proteomes:UP000193920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:ORY28697.1,
RC   ECO:0000313|Proteomes:UP000193920};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:ORY28697.1}.
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DR   EMBL; MCOG01000184; ORY28697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2B2H7; -.
DR   STRING; 1754190.A0A1Y2B2H7; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000193920; 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; 3.90.1150.10; 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; 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:UP000193920};
KW   Transferase {ECO:0000313|EMBL:ORY28697.1}.
FT   MOD_RES         284
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   524 AA;  59716 MW;  BB9A4D926A6AAF1C CRC64;
     MLKFGNSTIP KGISYDKKDI INYFFKIKTN VVENATRVSS PYMMGHMTSA LPFFHKHISK
     LISSLNQNVV KVETSSTMTF LERETLSKLH RAFYNMEDNY YKELLTKNDG CFGCITSGGT
     IANLTALWIS RNNAFPKTDN FNGIEKEGII SALKYYNYND IAIIGSELMH YSFKKAADIL
     GIGLNKIYTI PVDSEYKIRI DLLTEKLQEL KQKRIKVITI VGIASTTEVG SIDDLEKLAD
     LAEEYGAMFH VDGAWGGSFI LSDKYRHLLK GIQRADTITI DGHKLLYTPI GCGVVLFKSP
     FLPTTTIRKV ANYIIKTDSM DHGKTTLEGS RPANALYIHA SLNILGQHGL RYLLETSIEN
     TKYMYNLINL YPQFEIISKP ITNIFTYRYI PTWLQNKNIQ IKNKNNDINS SFYTTNNNNN
     NNNSNNNNNN KIYLEKYNNS DNAYERINDV TFNNEESEII DDERLRKGFV SKTIIKTTKY
     PNCTNGVAVL RVVIANPLIT KESIKTVIEE QIEFGLKLEK EYCN
//