ID   CYDE_METM7              Reviewed;         397 AA.
AC   A6VH54;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=MmarC7_0713;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
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., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-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; CP000745; ABR65780.1; -; Genomic_DNA.
DR   RefSeq; WP_011977100.1; NC_009637.1.
DR   AlphaFoldDB; A6VH54; -.
DR   STRING; 426368.MmarC7_0713; -.
DR   EnsemblBacteria; ABR65780; ABR65780; MmarC7_0713.
DR   GeneID; 5329419; -.
DR   KEGG; mmz:MmarC7_0713; -.
DR   eggNOG; arCOG05065; Archaea.
DR   HOGENOM; CLU_051840_0_0_2; -.
DR   OMA; GAMIPVM; -.
DR   OrthoDB; 27747at2157; -.
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..397
FT                   /note="L-cysteine desulfidase"
FT                   /id="PRO_0000339871"
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   397 AA;  43732 MW;  13BFF4DC00E97744 CRC64;
     MDDSKRILIT KVLKNEVTEA LGCTEVGLIG YAISLCNISY PFSIEKIEVT LNNGSFKNAY
     AVGVPNTKKY GILPAVVGGL LGNSKNKLLI FNDIKYDQKL EDFIKKRLEV KVLDGPLYCG
     VKIKDTSGKF FESLIKDNHL NVVIPKIEKE KISLEITDFE KEEYKSLELT DFLNYLDEIP
     EEIINLVEKT IYTNKNLIKG DFLNYGNDIL SNMVNKTTSA CNTRMTGENM PAMSVAKSGN
     MGLMATLPII SYDNLTENNF EKLKKSLLLA MLVTIYSTYN SSYLSSMCGC VSKGGMGAVI
     GLCYYKNGKN LKKLNSAARA FTANLPGIIC DGGKVGCALK LASGCFAAYS SLYVEISHEN
     GIVGKNFKEC VQNISKISKA MGDLDCDIVK IMSKKEM