CYSK_SYNE7
ID CYSK_SYNE7 Reviewed; 329 AA.
AC Q59966; Q7BA84;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cysteine synthase;
DE Short=CSase;
DE EC=2.5.1.47 {ECO:0000250|UniProtKB:P9WP55};
DE AltName: Full=O-acetylserine (thiol)-lyase {ECO:0000303|PubMed:7603442};
DE Short=OAS-TL;
DE AltName: Full=O-acetylserine sulfhydrylase;
GN Name=srpG; OrderedLocusNames=Synpcc7942_B2664; ORFNames=pANL40;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OG Plasmid pANL.
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION BY SULFUR
RP STARVATION, AND PATHWAY.
RC STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RX PubMed=7603442; DOI=10.1007/bf00290354;
RA Nicholson M.L., Gaasenbeek M., Laudenbach D.E.;
RT "Two enzymes together capable of cysteine biosynthesis are encoded on a
RT cyanobacterial plasmid.";
RL Mol. Gen. Genet. 247:623-632(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RA Holtman C.K., Chen Y., Sandoval P., Socias T., Mohler B.J., Youderian P.,
RA Golden S.S.;
RT "pANL, the large plasmid of Synechococcus elongatus PCC 7942.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805; PLASMID=pANL;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of plasmid 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of O-acetylserine (OAS) to cysteine
CC through the elimination of acetate and addition of hydrogen sulfide.
CC {ECO:0000250|UniProtKB:P9WP55, ECO:0000305|PubMed:7603442}.
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 Evidence={ECO:0000250|UniProtKB:P9WP55};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P9WP55};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2. {ECO:0000269|PubMed:7603442}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WP55}.
CC -!- INDUCTION: Transcriptionally induced in the absence of sulfur, requires
CC CysR for transcription. Part of the srpG-srpH-srpI operon.
CC {ECO:0000269|PubMed:7603442}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; U23436; AAA86725.1; -; Genomic_DNA.
DR EMBL; AF441790; AAM81167.1; -; Genomic_DNA.
DR EMBL; CP000101; ABB58693.1; -; Genomic_DNA.
DR RefSeq; NP_665779.1; NC_004073.2.
DR RefSeq; WP_011055156.1; NC_007595.1.
DR AlphaFoldDB; Q59966; -.
DR SMR; Q59966; -.
DR STRING; 1140.Synpcc7942_B2664; -.
DR PRIDE; Q59966; -.
DR EnsemblBacteria; ABB58693; ABB58693; Synpcc7942_B2664.
DR KEGG; syf:Synpcc7942_B2664; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_1_0_3; -.
DR OMA; RTPVFKF; -.
DR OrthoDB; 1033353at2; -.
DR BioCyc; SYNEL:SYNPCC7942_B2664-MON; -.
DR UniPathway; UPA00136; UER00200.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Plasmid;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..329
FT /note="Cysteine synthase"
FT /id="PRO_0000167115"
FT BINDING 78
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
FT BINDING 183..187
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
FT BINDING 278
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
FT MOD_RES 48
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
SQ SEQUENCE 329 AA; 34601 MW; 3800262555CD7745 CRC64;
MSTSGTFFAD NSQTIGKTPL VRLNRIVKGA PATVLAKIEG RNPAYSVKCR IGAAMIWDAE
QRGLLGPGKE LIEPTSGNTG IALAFVAAAR GIPLTLTMPE TMSLERRKLL AAYGAKLVLT
EGVKGMTGAV RRAEDIAASD PDRYVLLQQF RNPANPAIHE QTTGPEIWED TGGAIDILVS
GVGTGGTITG VSRYIKQTQG KPILSVAVEP EASPVISQQR SGLPLKPGPH KIQGIGAGFI
PENLDLSLVD QVERVSNEEA IAYARRLAQE EGLISGISCG AAVAAAVRLA QQSEHAGKTI
VVVLPDSGER YLSTALFDGI FNEQGLAVV
