ID A0A2T3BA87_AMORE Unreviewed; 413 AA.
AC A0A2T3BA87;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Cystathionine gamma-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=M430DRAFT_95877 {ECO:0000313|EMBL:PSS25190.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS25190.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS25190.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS25190.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(2018).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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DR EMBL; KZ679007; PSS25190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3BA87; -.
DR STRING; 857342.A0A2T3BA87; -.
DR InParanoid; A0A2T3BA87; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000241818; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF15; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000241818}.
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 413 AA; 44149 MW; 1D9CF96F7B91DE8C CRC64;
MTFTDHPIET PPRAPSPVQR FGTLAVHAGS PHDPVTGAVI EPISLSTTFA QNGVGKPVGA
YEYSRSSNPN RTNFEAAVAA LEHAKYALAF ASGSATTAVV LQSLAAGSHI ISVSDVYGGT
HRYFTQVAKA HGVRVTFTPE IEVDIREHIT PETKLVWIES PSNPTLRLVD IRAVASQAHE
YGIMVVVDNT FLSPYVQNPL DHGADIVVHS VTKYINGHSD VVMGVAAFNS DAMKERLGFL
QNAIGAIPSA FDSWLAHRGL KTLHLRAREA TINATLIAHT LEASPHVIAV NYPGLDSHPH
RAIAKKQHRD GMGGGMLSFR IKGGSAAAER FCQATNIFTL AESLGGVESL VEVPGSMTHA
GIPKEQREAV GVFDDLVRIS CGVEDAEDLK ADVLQALEKA VVWPKISNIS NGL
//
