ID A0A1Y1XDI3_9FUNG Unreviewed; 594 AA.
AC A0A1Y1XDI3;
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:ORX83820.1};
GN ORFNames=BCR32DRAFT_266694 {ECO:0000313|EMBL:ORX83820.1};
OS Anaeromyces robustus.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Anaeromyces.
OX NCBI_TaxID=1754192 {ECO:0000313|EMBL:ORX83820.1, ECO:0000313|Proteomes:UP000193944};
RN [1] {ECO:0000313|EMBL:ORX83820.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX83820.1,
RC ECO:0000313|Proteomes:UP000193944};
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.
RN [2] {ECO:0000313|EMBL:ORX83820.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX83820.1,
RC ECO:0000313|Proteomes:UP000193944};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
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:ORX83820.1}.
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DR EMBL; MCFG01000064; ORX83820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1XDI3; -.
DR STRING; 1754192.A0A1Y1XDI3; -.
DR OrthoDB; 888358at2759; -.
DR Proteomes; UP000193944; 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:UP000193944};
KW Transferase {ECO:0000313|EMBL:ORX83820.1}.
FT MOD_RES 330
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 594 AA; 67023 MW; 7CE5ADD1584FEEFE CRC64;
MIVLKFFKDC EIQEENVQQY IDNIIKEFYK PSPSIYAANT DTDEELKSKF GDSSIPQGII
CDKNNINKYF TEIKETVIDK ATRVSSPNMV GHMTSALPFF HRPLSKLITS LNQNVVKVET
SSTMTFLERE TLSKLHRAFY NESDEFYEKY LSTTDGSFGC VTSGGTIANL TAMWVARNNA
FPKTNDFEGI EKEGVISALK YYGYNDMAIV GSELMHYSFK KAADILGMGL KNIYTIPVDS
EYRIRIDLLI KKLEELRNKK IKVIAIVGIA CTTEVGSIDN LEILSDLAKK YGALFHVDGA
WGGSFIMSDK YQHLLKGIEK ADTITIDGHK LLYTPMGCGI VLFKSPLLPT TTIRKVASYV
IRADSMDHGK TTLEGSRPAN VLYLHASLNL LGHDGLSSIL DIAVENTKYM ADLVKTYPQF
EIISYPVTNI FLYRYIPSWL RKKPINEHIE QMVEIKSNAT ARTFVANSED NNEGTNDLST
LCSDTIQDLS DISDKEECSI SYDESLYNEE ENKIIDYFTT ELQAKQKREG KGFVSKTTVK
TTKYPNYRNG VAVFRVVIAN PLVTSENIKG VIEEQIKLGE IIEEDYKINH KTLL
//
