ID A0A1E5RF12_9ASCO Unreviewed; 392 AA.
AC A0A1E5RF12;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:OEJ85456.1};
GN ORFNames=AWRI3579_g2255 {ECO:0000313|EMBL:OEJ85456.1};
OS Hanseniaspora osmophila.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=56408 {ECO:0000313|EMBL:OEJ85456.1, ECO:0000313|Proteomes:UP000095728};
RN [1] {ECO:0000313|Proteomes:UP000095728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3579 {ECO:0000313|Proteomes:UP000095728};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
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}.
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:OEJ85456.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LPNM01000007; OEJ85456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5RF12; -.
DR STRING; 56408.A0A1E5RF12; -.
DR InParanoid; A0A1E5RF12; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000095728; 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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:OEJ85456.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000095728}.
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 392 AA; 42064 MW; 39B0755C32FEC9D2 CRC64;
MAINNNDQFA TLAVHAGSHV DSHGSVIEPI SLSTTFAQSA PAKPLGEYEY SRSSNPNRKN
FEDAIAALEK GKYGLAFASG SATTAIILQS LPQGSHAISI GDVYGGTHRY FTKVANTHGV
ETDFTNNLLE DLPKLVKPQT KLVWIETPTN PTLQVTDIKL VSETIKSINK DILLVVDNTF
LSPYLSNPLT LGADIVVHSA TKYINGHSDV VMGVLALNDK VLFEKLQFLQ NAVGAIPSPF
DSWLAHRGLK TLHLRVKQAS ESALKIATFL ENTTDKVIAV NYPGLKSHPQ NAVVQKQHRN
GLGGGMISFR IKGGAEAAAK FSSSTRLFTL AESLGGIESL LEVPAVMTHG GIPKESREAS
GVYDDLVRLS VGIEDVEDLL EDIKQALNAA SA
//
