ID   CYDE_METMP              Reviewed;         396 AA.
AC   Q6LX84;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=MMP1468;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF31024.1; -; Genomic_DNA.
DR   RefSeq; WP_011171412.1; NC_005791.1.
DR   AlphaFoldDB; Q6LX84; -.
DR   STRING; 267377.MMP1468; -.
DR   DNASU; 2761691; -.
DR   EnsemblBacteria; CAF31024; CAF31024; MMP1468.
DR   GeneID; 2761691; -.
DR   KEGG; mmp:MMP1468; -.
DR   PATRIC; fig|267377.15.peg.1504; -.
DR   eggNOG; arCOG05065; Archaea.
DR   HOGENOM; CLU_051840_0_0_2; -.
DR   OMA; GAMIPVM; -.
DR   OrthoDB; 27747at2157; -.
DR   BioCyc; MMAR267377:MMP_RS07550-MON; -.
DR   Proteomes; UP000000590; 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; Reference proteome.
FT   CHAIN           1..396
FT                   /note="L-cysteine desulfidase"
FT                   /id="PRO_0000339869"
FT   ACT_SITE        23
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q58431"
FT   BINDING         287
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q58431"
FT   BINDING         329
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q58431"
FT   BINDING         336
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q58431"
SQ   SEQUENCE   396 AA;  43545 MW;  02D6F7D5CB46AEC3 CRC64;
     MDDYKRILIT KILKNEVTEA LGCTEVGLIG YAVSLCNISD PFSIEKIELT LNNGSFKNAY
     AVGVPNTKKY GILPAVVGGL LGDHKNKLLV FNGIKYSQKL EDFIKERLKI RVINSPLYCG
     VKIKDNSGNT FESLIKDNHL NVVIPKINNK LISEINGSEK EEYKNLELLD FLEYIDEIPE
     EIIQLVEKTI YTNNNLIKGD FLNFGNDCLS NMVNKTTSAC NTRMIGENMP AMSVAKSGNM
     GIMATLPIIA YDYSNEQNQE KLIKSILLSV LVTIYATYKS SYLSSMCGCV SKGGMGAVIG
     LCYYKNGKNI KKLDSAARTF TANLPGIICD GGKVGCALKL ASGCFAAYSS LFVDISYENG
     IVGKNFKECV ENISEISKIM GDLDSDIVKI MSKKEI