ID D7B322_NOCDD Unreviewed; 380 AA.
AC D7B322;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=L-cysteine desulfhydrase Cds1 {ECO:0000256|HAMAP-Rule:MF_00868};
DE EC=4.4.1.1 {ECO:0000256|HAMAP-Rule:MF_00868};
GN Name=cds1 {ECO:0000256|HAMAP-Rule:MF_00868};
GN OrderedLocusNames=Ndas_3306 {ECO:0000313|EMBL:ADH68712.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH68712.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH68712.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
CC -!- FUNCTION: A cysteine desulfhydrase that generates hydrogen sulfide,
CC H(2)S. The H(2)S produced by this enzyme modulates the balance between
CC respiration and glycolysis, and contributes to redox homeostasis.
CC Probably eliminates toxic levels of Cys (which can induce oxidative
CC stress). {ECO:0000256|HAMAP-Rule:MF_00868}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:24931, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:35235; EC=4.4.1.1; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00868};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00868};
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. Cds1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00868}.
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DR EMBL; CP002040; ADH68712.1; -; Genomic_DNA.
DR RefSeq; WP_013154319.1; NC_014210.1.
DR AlphaFoldDB; D7B322; -.
DR STRING; 446468.Ndas_3306; -.
DR KEGG; nda:Ndas_3306; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_046285_0_0_11; -.
DR OrthoDB; 7624112at2; -.
DR Proteomes; UP000002219; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019450; P:L-cysteine catabolic process to pyruvate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00868; Cds1; 1.
DR InterPro; IPR047586; Cds1.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF211; PALP DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00868};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00868};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00868}; Reference proteome {ECO:0000313|Proteomes:UP000002219}.
FT DOMAIN 51..336
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 74
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00868"
SQ SEQUENCE 380 AA; 41891 MW; F9203A6D7024413E CRC64;
MASSPTGPRP GDDTPWVDRC DDSARSWADE AVRRVVADAN RSADTHLHVF PLPPEWGIDL
YLKDESVHPT GSLKHRLARS LFLYGLANGW IREGTTIVEA SSGSTAVSEA YFAQLVGLDF
ITVIPRRTSP EKIALIERYG GRCHFVDAPP AMYAEAERLA AETGGHYMDQ FTYAERATDW
RGNNNIAESI FEQLAMERHP CPEWIVVGAG TGGTSATIGR YLRYRRLGTR LAVVDPENSA
FFPGWVTGAS DYATGMPSRI EGIGRPRMEP SFVPSVIDLM MPVPDAASIA AMRHLHDRTG
LSAGGSTGTN LWGVWHLVAR MLREGRRGSV VTLICDGGER YQHSYYNDAW VAERGLDPAP
YRATIDRFLA EGVWEPPQTP
//
