ID A0A0C5GEU3_9ACTN Unreviewed; 402 AA.
AC A0A0C5GEU3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:AJP02876.1};
DE EC=4.4.1.1 {ECO:0000313|EMBL:AJP02876.1};
GN ORFNames=TU94_16700 {ECO:0000313|EMBL:AJP02876.1};
OS Streptomyces cyaneogriseus subsp. noncyanogenus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP02876.1, ECO:0000313|Proteomes:UP000032234};
RN [1] {ECO:0000313|EMBL:AJP02876.1, ECO:0000313|Proteomes:UP000032234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP02876.1,
RC ECO:0000313|Proteomes:UP000032234};
RA Wang H., Li C., Xiang W., Wang X.;
RT "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp.
RT Noncyanogenus NMWT1, the producer of nematocidal antibiotics nemadectin.";
RL Submitted (FEB-2015) 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|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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DR EMBL; CP010849; AJP02876.1; -; Genomic_DNA.
DR RefSeq; WP_044382780.1; NZ_CP010849.1.
DR AlphaFoldDB; A0A0C5GEU3; -.
DR STRING; 477245.TU94_16700; -.
DR KEGG; scw:TU94_16700; -.
DR PATRIC; fig|477245.3.peg.3539; -.
DR HOGENOM; CLU_018986_2_2_11; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000032234; Chromosome.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 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:AJP02876.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000032234}.
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 226
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 402 AA; 42702 MW; 2955FAD0D314D726 CRC64;
MNDSATDTGG GTRQQGQHSG AADGGNAAGR TGDGTRAVRA GLPEPVKHEP TLPGPVFAAH
FHLPGDPTGP YTYGRDENPT WTLLERAIGE LEAPGRDDVE TLVFASGMAA ISSVLFSQLR
AGDAVVLPSD GYQVLPLVRA QLEAYGVEVR TAPTGGDAQL DVLDGAKLLW IETPSNPGLD
VCDVRRLAEA AHTRGALVAV DNTLASPLGQ RPLELGADFS VASGTKQLTG HGDILLGYVT
GHDAEAMTAV RRWRKIVGAI PGPMEAWLAH RSIATLELRV ERQNATALKV AEALRERPEV
SGLRYPGLPD DPSHKIASQQ MRRYGCVVSF TLPTRARADR FLDALRLVDD ATSFGGVRST
AERRGRWGGD SVPEGFIRLS VGAEDSEDLL ADLLRALDES AD
//
