ID   Q9ZHG9_SYNY4            Unreviewed;       393 AA.
AC   Q9ZHG9;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   SubName: Full=L-cysteine/cystine lyase C-DES {ECO:0000313|EMBL:AAD02935.1};
GN   Name=c-des {ECO:0000313|EMBL:AAD02935.1};
OS   Synechocystis sp. (strain PCC 6714) (Aphanocapsa sp. (strain PCC 6714)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1147 {ECO:0000313|EMBL:AAD02935.1};
RN   [1] {ECO:0000313|EMBL:AAD02935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PCC 6714 {ECO:0000313|EMBL:AAD02935.1};
RX   PubMed=9099686; DOI=10.1074/jbc.272.16.10442;
RA   Leibrecht I., Kessler D.;
RT   "A novel L-cysteine/cystine C-S-lyase directing [2Fe-2S] cluster formation
RT   of Synechocystis ferredoxin.";
RL   J. Biol. Chem. 272:10442-10447(1997).
RN   [2] {ECO:0000313|EMBL:AAD02935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PCC 6714 {ECO:0000313|EMBL:AAD02935.1};
RX   PubMed=9867829; DOI=10.1074/jbc.274.1.189;
RA   Lang T., Kessler D.;
RT   "Evidence for cysteine persulfide as reaction product of L-Cyst(e)ine C-S-
RT   lyase (C-DES) from Synechocystis. Analyses using cystine analogues and
RT   recombinant C-DES.";
RL   J. Biol. Chem. 274:189-195(1999).
RN   [3] {ECO:0007829|PDB:1ELQ, ECO:0007829|PDB:1ELU}
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 12-393, PYRIDOXAL PHOSPHATE AT
RP   LYS-223, AND ACTIVE SITE.
RX   PubMed=10760256; DOI=10.1073/pnas.97.8.3856;
RA   Clausen T., Kaiser J.T., Steegborn C., Huber R., Kessler D.;
RT   "Crystal structure of the cystine C-S lyase from Synechocystis:
RT   stabilization of cysteine persulfide for FeS cluster biosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:3856-3861(2000).
RN   [4] {ECO:0007829|PDB:1N2T, ECO:0007829|PDB:1N31}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 9-393 IN COMPLEX WITH PYRIDOXAL
RP   5'-PHOSPHATE.
RX   PubMed=12386155; DOI=10.1074/jbc.m209862200;
RA   Kaiser J.T., Bruno S., Clausen T., Huber R., Schiaretti F., Mozzarelli A.,
RA   Kessler D.;
RT   "Snapshots of the cystine lyase C-DES during catalysis. Studies in solution
RT   and in the crystalline state.";
RL   J. Biol. Chem. 278:357-365(2003).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU004075}.
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DR   EMBL; AF061964; AAD02935.1; -; Genomic_DNA.
DR   RefSeq; WP_028948110.1; NZ_CP007542.1.
DR   PDB; 1ELQ; X-ray; 1.80 A; A/B=12-393.
DR   PDB; 1ELU; X-ray; 1.55 A; A/B=12-393.
DR   PDB; 1N2T; X-ray; 2.00 A; A/B=9-393.
DR   PDB; 1N31; X-ray; 2.20 A; A/B=9-393.
DR   PDBsum; 1ELQ; -.
DR   PDBsum; 1ELU; -.
DR   PDBsum; 1N2T; -.
DR   PDBsum; 1N31; -.
DR   AlphaFoldDB; Q9ZHG9; -.
DR   SMR; Q9ZHG9; -.
DR   DrugBank; DB04467; N-(5'-phosphopyridoxyl)-L-alanine.
DR   DrugBank; DB02761; S-Mercaptocysteine.
DR   OrthoDB; 9804366at2; -.
DR   SABIO-RK; Q9ZHG9; -.
DR   EvolutionaryTrace; Q9ZHG9; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR43586:SF4; ISOPENICILLIN N EPIMERASE; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1ELQ, ECO:0007829|PDB:1ELU};
KW   Lyase {ECO:0000313|EMBL:AAD02935.1}.
FT   DOMAIN          32..361
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   ACT_SITE        114
FT                   /note="EMO_00062 proton shuttle (general acid/base)"
FT                   /evidence="ECO:0007829|PDB:1ELU"
FT   ACT_SITE        223
FT                   /note="EMO_00050 covalent catalysis,EMO_00062 proton
FT                   shuttle (general acid/base)"
FT                   /evidence="ECO:0007829|PDB:1ELU"
FT   BINDING         88
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:1ELQ, ECO:0007829|PDB:1N2T"
FT   BINDING         89
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:1ELQ, ECO:0007829|PDB:1N2T"
FT   BINDING         114
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:1ELQ, ECO:0007829|PDB:1N2T"
FT   BINDING         200
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:1ELQ, ECO:0007829|PDB:1N2T"
FT   BINDING         222
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:1N2T, ECO:0007829|PDB:1N31"
FT   BINDING         223
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="covalent"
FT                   /evidence="ECO:0007829|PDB:1ELQ"
FT   BINDING         251
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:1ELQ, ECO:0007829|PDB:1N2T"
FT   BINDING         276
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:1ELQ, ECO:0007829|PDB:1N2T"
FT   SITE            197
FT                   /note="EMO_00033 electrostatic stabiliser"
FT                   /evidence="ECO:0007829|PDB:1ELU"
FT   SITE            199
FT                   /note="EMO_00033 electrostatic stabiliser"
FT                   /evidence="ECO:0007829|PDB:1ELU"
FT   SITE            200
FT                   /note="EMO_00033 electrostatic stabiliser"
FT                   /evidence="ECO:0007829|PDB:1ELU"
FT   SITE            360
FT                   /note="EMO_00029 steric role"
FT                   /evidence="ECO:0007829|PDB:1ELU"
FT   MOD_RES         114
FT                   /note="Cysteine persulfide"
FT                   /evidence="ECO:0007829|PDB:1ELU"
FT   MOD_RES         360
FT                   /note="Cysteine persulfide"
FT                   /evidence="ECO:0007829|PDB:1ELU"
SQ   SEQUENCE   393 AA;  43154 MW;  4AC0ADA899A3264C CRC64;
     MADPVNLIPD RHQFPGLANK TYFNFGGQGI LPTVALEAIT AMYGYLQENG PFSIAANQHI
     QQLIAQLRQA LAETFNVDPN TITITDNVTT GCDIVLWGLD WHQGDEILLT DCEHPGIIAI
     VQAIAARFGI TYRFFPVAAT LNQGDAAAVL ANHLGPKTRL VILSHLLWNT GQVLPLAEIM
     AVCRRHQGNY PVRVLVDGAQ SAGSLPLDFS RLEVDYYAFT GHKWFAGPAG VGGLYIHGDC
     LGEINPTYVG WRSITYGAKG EPTGWAEGGK RFEVATSAYP QYAGLLAALQ LHQRQGTAEE
     RYQAICQRSE FLWRGLNQLP HVHCLATSAP QAGLVSFTVD SPLGHRAIVQ KLEEQRIYLR
     TIADPDCIRA CCHYITDEEE INHLLARLAD FGP
//