ID   CYDE_METM6              Reviewed;         396 AA.
AC   A9A9J5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=L-cysteine desulfidase {ECO:0000250|UniProtKB:Q58431};
DE            EC=4.4.1.28 {ECO:0000250|UniProtKB:Q58431};
DE   AltName: Full=L-cysteine desulfhydrase;
GN   OrderedLocusNames=MmarC6_1205;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cleavage of L-cysteine to form 2-aminoprop-2-
CC       enoate and sulfide. The former then spontaneously hydrolyzes to
CC       pyruvate and NH(3). May be responsible for the production of sulfide
CC       required for the biosynthesis of iron-sulfur centers in this archaea.
CC       {ECO:0000250|UniProtKB:Q58431}.
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=4.4.1.28;
CC         Evidence={ECO:0000250|UniProtKB:Q58431};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q58431};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:Q58431};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q58431}.
CC   -!- SIMILARITY: Belongs to the L-cysteine desulfidase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000867; ABX02018.1; -; Genomic_DNA.
DR   RefSeq; WP_012193958.1; NC_009975.1.
DR   AlphaFoldDB; A9A9J5; -.
DR   STRING; 444158.MmarC6_1205; -.
DR   EnsemblBacteria; ABX02018; ABX02018; MmarC6_1205.
DR   GeneID; 5738054; -.
DR   KEGG; mmx:MmarC6_1205; -.
DR   eggNOG; arCOG05065; Archaea.
DR   HOGENOM; CLU_051840_0_0_2; -.
DR   OMA; GAMIPVM; -.
DR   OrthoDB; 27747at2157; -.
DR   PhylomeDB; A9A9J5; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR005130; Ser_deHydtase-like_asu.
DR   InterPro; IPR021144; UPF0597.
DR   PANTHER; PTHR30501; PTHR30501; 1.
DR   Pfam; PF03313; SDH_alpha; 1.
DR   PIRSF; PIRSF006054; UCP006054; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding.
FT   CHAIN           1..396
FT                   /note="L-cysteine desulfidase"
FT                   /id="PRO_1000188461"
FT   ACT_SITE        23
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q58431"
FT   BINDING         288
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q58431"
FT   BINDING         330
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q58431"
FT   BINDING         337
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q58431"
SQ   SEQUENCE   396 AA;  43171 MW;  2801CB14844B2989 CRC64;
     MDDSKHILIT KILKNEVTEA LGCTEVGLIG YAVSLCNISD PFSIDKLELT LNNGSFKNAY
     AVGVPNTGKY GILPAVVGGL LGNSKNKLLI FNDITYSQEL EDFIKEKLEI KVIDGPLFCN
     IKIKDNSGNY FESLIKDNHL NVVIPKIEKE KIDVEITTSE KGEYKNLELI DFLDYLDEIP
     EKIGKLVEKT VQTNKNLIKG DFLNYGTDIL SIIVNKTTSA CNTRMTGENM PAMSVAKSGN
     MGIMATLPII SYDSSTENNS EKLIKSVLLS MLVTIYSTYN SSYLSSMCGC VSKGGMGAVI
     GLCYYKNGKN LKKLDSSART FTANLPGIIC DGGKVGCALK LASGCFAAYS SLFVDISYEN
     GIVGKDFKEC VENISKISKA MGDLDCDIVE IMSKKM