ID E8RP30_ASTEC Unreviewed; 354 AA.
AC E8RP30;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-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=Astex_1327 {ECO:0000313|EMBL:ADU13000.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU13000.1, ECO:0000313|Proteomes:UP000001492};
RN [1] {ECO:0000313|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC CB 48 {ECO:0000313|Proteomes:UP000001492};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) 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}.
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; CP002395; ADU13000.1; -; Genomic_DNA.
DR AlphaFoldDB; E8RP30; -.
DR STRING; 573065.Astex_1327; -.
DR KEGG; aex:Astex_1327; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_046285_0_0_5; -.
DR Proteomes; UP000001492; 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:UP000001492}.
FT DOMAIN 36..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 354 AA; 39266 MW; 317CC4FEA79934E5 CRC64;
MSSMTQLPRE WLIEAVRRIE ADFNRSSDTH LIHHEVAAFP GVHLYFKDES SHPTGSLKHR
LARSLILYAL CNEWVGPQTT LIESSSGSTA VSEAYFARLL GLRFIAVVPK SVAQAKIDAI
RFQGGEVHGV DDPNAVYAEA QRLADETGGH YLDQFTYAER ATDWRGNNNI AESLFSQMTA
EPYPVPTWLV TGAGTGGTSA TLGRYIRYRR LPTRLCVADP EGSVFHRHYH DRSVQLIDRC
GSCIEGIGRP RVEPSFIPSL IDHMEVVTDA QSIAAVRLLS ERLGRRVGGS TGTNLWACVR
LMQEMAQKGE TGSIVTILCD GGERYADTYY NDGWLSARAI DWRSPYADLK SLMG
//
