ID   CYDE_METM5              Reviewed;         397 AA.
AC   A4FW56;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, 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=MmarC5_0110;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-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; CP000609; ABO34427.1; -; Genomic_DNA.
DR   RefSeq; WP_011867887.1; NC_009135.1.
DR   AlphaFoldDB; A4FW56; -.
DR   STRING; 402880.MmarC5_0110; -.
DR   EnsemblBacteria; ABO34427; ABO34427; MmarC5_0110.
DR   GeneID; 4927595; -.
DR   KEGG; mmq:MmarC5_0110; -.
DR   eggNOG; arCOG05065; Archaea.
DR   HOGENOM; CLU_051840_0_0_2; -.
DR   OMA; GAMIPVM; -.
DR   OrthoDB; 27747at2157; -.
DR   Proteomes; UP000000253; Chromosome.
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_0000339870"
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;  43604 MW;  5F36FB917F0F3A55 CRC64;
     MDDSKRILIT KILKNEVTEA LGCTEVGLIG YAVSLCNISD PFSIEKIELT LNNGSFKNVY
     AVGVPNTGKY GLLPAVVGGF LGNSKNKLLI FNDITYSQEL EDFTKEKLEI KVINGPLYCS
     VKIKDNSGKI HESLIKDNHL NVVIPEIKKE KINMEINSSE KEKYKNLELL DFLNYLDEIP
     EEIIKLVEKT IYTNKNLIKG DFLNYGTDIL SNMVNKTTSA CNIRMTGENM TAMSVAKSGN
     MGIMATLPII SYDFSTENNS EKLIKSVLLS MLVTIYSTYN SSYLSSMCGC VSKGGMGAVI
     GLSHYKNGKN LKKFDSSART FTANLPGIIC DGGKVGCALK LASGCFAAYS SLFVDISYEN
     GIVGKNFKEC VENISKISKA MGDLDCDIVE IMSKKEM