ID F4GBI6_ALIDK Unreviewed; 382 AA.
AC F4GBI6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=Alide2_3503 {ECO:0000313|EMBL:AEB85831.1};
OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Alicycliphilus.
OX NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB85831.1, ECO:0000313|Proteomes:UP000007938};
RN [1] {ECO:0000313|EMBL:AEB85831.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RX PubMed=21742888; DOI=10.1128/JB.00365-11;
RA Oosterkamp M.J., Veuskens T., Plugge C.M., Langenhoff A.A., Gerritse J.,
RA van Berkel W.J., Pieper D.H., Junca H., Goodwin L.A., Daligault H.E.,
RA Bruce D.C., Detter J.C., Tapia R., Han C.S., Land M.L., Hauser L.J.,
RA Smidt H., Stams A.J.;
RT "Genome Sequences of Alicycliphilus denitrificans Strains BC and K601T.";
RL J. Bacteriol. 193:5028-5029(2011).
RN [2] {ECO:0000313|EMBL:AEB85831.1, ECO:0000313|Proteomes:UP000007938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14773 / CIP 107495 / K601
RC {ECO:0000313|Proteomes:UP000007938};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M.,
RA Pieper D., van Berkel W., Langenhoff A., Smidt H., Stams A., Woyke T.;
RT "Complete sequence of chromosome of Alicycliphilus denitrificans K601.";
RL Submitted (APR-2011) 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 -!- 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; CP002657; AEB85831.1; -; Genomic_DNA.
DR RefSeq; WP_013722757.1; NC_015422.1.
DR AlphaFoldDB; F4GBI6; -.
DR STRING; 596154.Alide2_3503; -.
DR KEGG; adk:Alide2_3503; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_046285_0_0_4; -.
DR OrthoDB; 7624112at2; -.
DR Proteomes; UP000007938; Chromosome.
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:UP000007938}.
FT DOMAIN 29..320
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 58
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00868"
SQ SEQUENCE 382 AA; 42062 MW; F2907BB65CE7AF6D CRC64;
MPSIQVTSRS WVLEAVRRIE RDFQRSSDTH LLQLDLPAMP QVRLYLKDES THPTGSLKHR
LARSLFLYGL CNGWIREGTT IVEASSGSTA VSEAYFARLL GLPFVAVMPR GTSAAKIAQI
EFYGGRCHFV GSSAQLYAEA ERLARECNGH YMDQFTYAER ATDWRGNNNI AESIFQQMRG
EPHPTPAWIV VGAGTGGTSA TIGRYIRYQG CATQLCVVDP EHSVFHSYFH HRDASITSAR
GSDVEGIGRP RVEPSFVPDV IDRMERVPNA ASYAAMRVLQ RLVGRRYGGS TGTDFYVAMQ
LACEMAQRNQ AGSIVALACD SGDRYMDSYY DDAWLASNHY DIAPYVVQLE EAWLRGVWRD
GGGSRPAAQP SASEAAALAA AG
//
