CYDE_METJA
ID CYDE_METJA Reviewed; 388 AA.
AC Q58431;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=L-cysteine desulfidase {ECO:0000303|PubMed:15683250};
DE EC=4.4.1.28 {ECO:0000269|PubMed:15683250};
DE AltName: Full=L-cysteine desulfhydrase;
GN OrderedLocusNames=MJ1025;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, COFACTOR, MUTAGENESIS OF CYS-25; HIS-139; CYS-282;
RP CYS-322; ASP-323 AND CYS-329, AND REACTION MECHANISM.
RX PubMed=15683250; DOI=10.1021/bi0484769;
RA Tchong S.I., Xu H., White R.H.;
RT "L-cysteine desulfidase: an [4Fe-4S] enzyme isolated from
RT Methanocaldococcus jannaschii that catalyzes the breakdown of L-cysteine
RT into pyruvate, ammonia, and sulfide.";
RL Biochemistry 44:1659-1670(2005).
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 Is very specific for L-cysteine, with no activity being detected with
CC D-cysteine, L-homocysteine, 3-mercaptopropionate (cysteine without the
CC amino group), cysteamine (cysteine without the carboxylate), or
CC mercaptolactate (the hydroxyl analog of cysteine).
CC {ECO:0000269|PubMed:15683250}.
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:0000269|PubMed:15683250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:15683250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:15683250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.78 mM for L-cysteine (at 65 degrees Celsius)
CC {ECO:0000269|PubMed:15683250};
CC Note=kcat is 39.6 sec(-1) (at 65 degrees Celsius).
CC {ECO:0000269|PubMed:15683250};
CC pH dependence:
CC Optimum pH is 7.6. {ECO:0000269|PubMed:15683250};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:15683250}.
CC -!- SIMILARITY: Belongs to the L-cysteine desulfidase family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99029.1; -; Genomic_DNA.
DR PIR; H64427; H64427.
DR AlphaFoldDB; Q58431; -.
DR STRING; 243232.MJ_1025; -.
DR EnsemblBacteria; AAB99029; AAB99029; MJ_1025.
DR KEGG; mja:MJ_1025; -.
DR eggNOG; arCOG05065; Archaea.
DR HOGENOM; CLU_051840_0_0_2; -.
DR InParanoid; Q58431; -.
DR OMA; GAMIPVM; -.
DR PhylomeDB; Q58431; -.
DR BRENDA; 4.4.1.28; 3260.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019450; P:L-cysteine catabolic process to pyruvate; IBA:GO_Central.
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 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..388
FT /note="L-cysteine desulfidase"
FT /id="PRO_0000107148"
FT ACT_SITE 25
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:15683250"
FT BINDING 282
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:15683250"
FT BINDING 322
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:15683250"
FT BINDING 329
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:15683250"
FT MUTAGEN 25
FT /note="C->A: No activity."
FT /evidence="ECO:0000269|PubMed:15683250"
FT MUTAGEN 139
FT /note="H->N: Almost no effect."
FT /evidence="ECO:0000269|PubMed:15683250"
FT MUTAGEN 282
FT /note="C->A: Retains 5% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:15683250"
FT MUTAGEN 322
FT /note="C->A: No activity; when associated with Ala-329."
FT /evidence="ECO:0000269|PubMed:15683250"
FT MUTAGEN 322
FT /note="C->S: Retains 10% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:15683250"
FT MUTAGEN 323
FT /note="D->N: Retains 50% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:15683250"
FT MUTAGEN 329
FT /note="C->A: No activity; when associated with Ala-322."
FT /evidence="ECO:0000269|PubMed:15683250"
FT MUTAGEN 329
FT /note="C->S: Retains 10% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:15683250"
SQ SEQUENCE 388 AA; 42645 MW; 80CA180E1061315C CRC64;
MVSIMNKNEL ITEILKNEVV KALGCTEVGL IGYTVAKAKP EDLYSIKEIK LILDKGTFKN
AFSVGVPNTN KFGILPAVVG GLLGREENKL EVFKDIKYDE KLEEFIENKL KIEVIDSDVY
CKVIIKANKV YEAETKGSHS GKSLSDDLKN AYKSLTLKDF IDYIEDIPEE VIKIIKETIE
TNKNLSTPEV PEDFISLDLK DEILNHMLKK TVSAVYNRMI GINKPAMAIA GSGNMGLTAT
LPIIAYDEIK GHDEEKLTKS ITLSALTTIY SAYHSSYISA MCGCVNRGGI GAVSGLSYYI
FGFDRIEESI KSFTANLPGI VCDGGKIGCA LKIASGVFAI YLSLFSKVPY TNGIVGKDFK
ECIENIGKIG KAMKPVDDEI IEILKNKK
