ID I2N200_STRT9 Unreviewed; 378 AA.
AC I2N200;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:QKM68771.1};
GN ORFNames=STSU_017890 {ECO:0000313|EMBL:QKM68771.1};
OS Streptomyces tsukubensis (strain DSM 42081 / NBRC 108919 / NRRL 18488 /
OS 9993).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1114943 {ECO:0000313|EMBL:QKM68771.1, ECO:0000313|Proteomes:UP000005940};
RN [1] {ECO:0000313|EMBL:QKM68771.1, ECO:0000313|Proteomes:UP000005940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 42081 / NBRC 108919 / NRRL 18488 / 9993
RC {ECO:0000313|Proteomes:UP000005940};
RX PubMed=22740677; DOI=10.1128/JB.00692-12;
RA Barreiro C., Prieto C., Sola-Landa A., Solera E., Martinez-Castro M.,
RA Perez-Redondo R., Garcia-Estrada C., Aparicio J.F.,
RA Fernandez-Martinez L.T., Santos-Aberturas J., Salehi-Najafabadi Z.,
RA Rodriguez-Garcia A., Tauch A., Martin J.F.;
RT "Draft genome of Streptomyces tsukubaensis NRRL 18488, the producer of the
RT clinically important immunosuppressant tacrolimus (FK506).";
RL J. Bacteriol. 194:3756-3757(2012).
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; CP029159; QKM68771.1; -; Genomic_DNA.
DR RefSeq; WP_006348087.1; NZ_CP029159.1.
DR AlphaFoldDB; I2N200; -.
DR Proteomes; UP000005940; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:QKM68771.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 199
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 378 AA; 40124 MW; F11CB191C18BA7FF CRC64;
MDTGIGDGTR AVRAGLPEPV KHEPTLPGPA FAAHFHLPGE PTGPYTYGRD TNPSWTLLER
AIGELEAPGE PVETTVFASG MAAVSAVLFS TLRAGDAVVL PSDGYQALPL VRDQLEAYGI
EVRTAPTAGD AQLSVLEGAR LLWVESPSNP GLDVCDIRRM VRVAHAQGAL VAVDNTLATP
LAQRPLALGA DFSVASDTKG MTGHGDLLLG HVTCRDTALA ADVRRWRKVV GAIPGPMETW
LAHRSLATLH LRIDRQCINA LALARALGER AEVTGLRYPG LPTDPSYTLA GRQMRRYGGV
LSFVLPDRDH AERFLDALRL VDDATSFGGV RSSAERRGRW GGDAVPEGFI RLSAGAEDTD
DLVADVLRAL DEAAGPIG
//
