ID A0A022M8D4_9ACTN Unreviewed; 374 AA.
AC A0A022M8D4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=CF54_35035 {ECO:0000313|EMBL:EYT78812.1};
OS Streptomyces sp. Tu 6176.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1470557 {ECO:0000313|EMBL:EYT78812.1, ECO:0000313|Proteomes:UP000020060};
RN [1] {ECO:0000313|EMBL:EYT78812.1, ECO:0000313|Proteomes:UP000020060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu 6176 {ECO:0000313|EMBL:EYT78812.1,
RC ECO:0000313|Proteomes:UP000020060};
RA Olano C., Cano-Prieto C., Mendez C., Salas J.A.;
RT "Draft genome sequence of Streptomyces sp. Tu 6176, producer of the
RT cytotoxic benzoxazol nataxazol.";
RL Submitted (MAR-2014) 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}.
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:EYT78812.1}.
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; JFJQ01001099; EYT78812.1; -; Genomic_DNA.
DR RefSeq; WP_037896070.1; NZ_KK106994.1.
DR AlphaFoldDB; A0A022M8D4; -.
DR HOGENOM; CLU_046285_0_0_11; -.
DR OrthoDB; 7624112at2; -.
DR Proteomes; UP000020060; 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 43..334
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00868"
SQ SEQUENCE 374 AA; 41755 MW; B71E891BB42852AA CRC64;
MSTTEQRRTG ETQDVDRSDP GYRDWLKEAV RKVQADANRS ADTHLLRFPL PEEWGVDLYL
KDESTHPTGS LKHRLARSLF LYGLCNGWIR PDRPVIEASS GSTAVSEAYF AKLIGVPFIA
VMPRTTSAEK CRLIEFHGGR CHFVDDPRTM YEASARLAVD TGGHYMDQFT YAERATDWRG
NNNIAESIFR QLELERFPEP AWIVATAGTG GTSATLARYV HYMQYDTRIC VADPDNSCFF
EGWTTGDADV VCERGSRIEG IGRPRMEPSF VPGAIDRMMK VPDAAAVASV RALERVIGRK
AGGSTGTGLW SALKIVAEMR EQGRRGSVVT LLCDPGDRYL DKYYSDTWLA EQGLDHTPYT
ATLDTFLTTG AWPR
//