ID   CYSK_SYNY3              Reviewed;         312 AA.
AC   P73410;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Cysteine synthase;
DE            Short=CSase;
DE            EC=2.5.1.47;
DE   AltName: Full=O-acetylserine (thiol)-lyase;
DE            Short=OAS-TL;
DE   AltName: Full=O-acetylserine sulfhydrylase;
GN   Name=cysK; OrderedLocusNames=slr1842;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC         Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA17450.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000022; BAA17450.1; ALT_INIT; Genomic_DNA.
DR   PIR; S77347; S77347.
DR   AlphaFoldDB; P73410; -.
DR   SMR; P73410; -.
DR   IntAct; P73410; 7.
DR   STRING; 1148.1652529; -.
DR   PaxDb; P73410; -.
DR   EnsemblBacteria; BAA17450; BAA17450; BAA17450.
DR   KEGG; syn:slr1842; -.
DR   eggNOG; COG0031; Bacteria.
DR   InParanoid; P73410; -.
DR   OMA; FWDSGER; -.
DR   PhylomeDB; P73410; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
DR   GO; GO:0080146; F:L-cysteine desulfhydrase activity; IBA:GO_Central.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR005856; Cys_synth.
DR   InterPro; IPR005859; CysK.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01139; cysK; 1.
DR   TIGRFAMs; TIGR01136; cysKM; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..312
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000167104"
FT   BINDING         77
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         181..185
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         46
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  33173 MW;  54D4DF4F5613EFC8 CRC64;
     MKIASNITEL IGRTPLVRLN RIPLLEGCGA KIVVKLEGMN PAASVKDRIG INMINRAEQE
     GLIEPGKTLL IEPTSGNTGI ALAMVAAAKG YQLILTMPET MSQERRAMLK AYGAKLELTP
     GSEGMGGCIR RAQELAESLP NAYMLQQFDN PANPQIHQQT TALEIWQDTD GAIDFLVAGV
     GTGGTITGVA SVLKEKKPSF QAIAVEPQNS PVLSGGKPGP HKIQGIGAGF IPEVLDVNLI
     DEVIAVTDEE AIAYGRRLAR EEGILSGIST GAALAAAIKV AKRPANKDKL IVMIQPSFGE
     RYLSTPLFQD LE