ID A0A068QZM4_9GAMM Unreviewed; 350 AA.
AC A0A068QZM4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=XPG1_0471 {ECO:0000313|EMBL:CDG20126.1};
OS Xenorhabdus poinarii G6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1354304 {ECO:0000313|EMBL:CDG20126.1, ECO:0000313|Proteomes:UP000032735};
RN [1] {ECO:0000313|EMBL:CDG20126.1, ECO:0000313|Proteomes:UP000032735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G6 {ECO:0000313|EMBL:CDG20126.1,
RC ECO:0000313|Proteomes:UP000032735};
RA Genoscope - CEA;
RL Submitted (JUL-2013) 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 may modulate central
CC metabolism. {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 -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC Evidence={ECO:0000256|ARBA:ARBA00000298};
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; FO704551; CDG20126.1; -; Genomic_DNA.
DR RefSeq; WP_045957617.1; NZ_FO704551.1.
DR AlphaFoldDB; A0A068QZM4; -.
DR STRING; 1354304.XPG1_0471; -.
DR KEGG; xpo:XPG1_0471; -.
DR HOGENOM; CLU_046285_0_0_6; -.
DR OrthoDB; 7624112at2; -.
DR Proteomes; UP000032735; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:RHEA.
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}; Transferase {ECO:0000313|EMBL:CDG20126.1}.
FT DOMAIN 22..314
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 52
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00868"
SQ SEQUENCE 350 AA; 39435 MW; 7E6DD94F1F7E8F45 CRC64;
MSSLWAKNAI KSIQADYQRS ADTHLIRLNL PMFPGIHLYL KDESTHPTGS LKHRLARSLF
LYALTNGWIK EGTPIIEASS GSTAVSEAYF ARLLGLPFIA VMPSCTAKRK IQEIEFYGGK
CHFVEHSALI YQESERLAKE LNGHYMDQFT YAERATDWRG NNNIAESIFR QMQLEPFPEP
TYIVMSAGTG GTSATLGRYI RYQGYNTKLI VVDPENSVFY DCYHQNRRDL CGGTGSKIEG
IGRPRAEPSF IPTVIDDLIQ VPDLATIATI YWLEKFIGRK TGASTGTNVW GALQLAKQMH
DNKQQGAIVT LLCDSGERYL DTYYNPEWVM NNIGDVTQYL TQLPKLNGYE
//
