ID A0A1H9B5I2_9PSEU Unreviewed; 347 AA.
AC A0A1H9B5I2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ORFNames=SAMN05216188_101655 {ECO:0000313|EMBL:SEP84194.1};
OS Lentzea xinjiangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=402600 {ECO:0000313|EMBL:SEP84194.1, ECO:0000313|Proteomes:UP000199352};
RN [1] {ECO:0000313|Proteomes:UP000199352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3525 {ECO:0000313|Proteomes:UP000199352};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOFR01000001; SEP84194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9B5I2; -.
DR STRING; 402600.SAMN05216188_101655; -.
DR Proteomes; UP000199352; Unassembled WGS sequence.
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:0044249; P:cellular biosynthetic process; IEA:UniProt.
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:SF135; 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}.
FT DOMAIN 20..309
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 47
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00868"
SQ SEQUENCE 347 AA; 38225 MW; 8377780E29B986D5 CRC64;
MCEAVGIIEA DANRSADTHL LRYPLPLDWG IDLYLKDEST HPTGSLKHRL ARSLFLYAIC
NGWITGGTPV IEASSGSTAV SEAYFARLLG LPFIAVMPRS TSAEKVALIE RQGGRCHFVD
EPSAIYDESR RLATELGGHF MDQFTHAERA TDWRGNNNIA ESIFDQMKLE PSPEPDWIVV
GAGTGGTSAT IGRYIHYQKL STRLAVVDPE HSVFFEAWRD GNPDLVATRG SGIEGIGRPR
VEPSFIGQVI DRMIKVPDAA SIATIRFVED LLGRRVGGST GTNLWGAFQV VAEMRQSRSR
GSVVTLLCDG GERYANTYYD DSWVAAQGMD LDPCLDRLNN FHRTGNW
//