ID   CYSM_PSESY              Reviewed;         169 AA.
AC   P48028;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Cysteine synthase B;
DE            Short=CSase B;
DE            EC=2.5.1.47;
DE   AltName: Full=O-acetylserine (thiol)-lyase B;
DE            Short=OAS-TL B;
DE   AltName: Full=O-acetylserine sulfhydrylase B;
DE   Flags: Fragment;
GN   Name=cysM;
OS   Pseudomonas syringae pv. syringae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1314807; DOI=10.1128/jb.174.9.3011-3020.1992;
RA   Hrabak E.M., Willis D.K.;
RT   "The lemA gene required for pathogenicity of Pseudomonas syringae pv.
RT   syringae on bean is a member of a family of two-component regulators.";
RL   J. Bacteriol. 174:3011-3020(1992).
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}.
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DR   EMBL; M80477; AAA25876.1; -; Genomic_DNA.
DR   PIR; A41863; A41863.
DR   AlphaFoldDB; P48028; -.
DR   SMR; P48028; -.
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; IPR005858; CysM.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   PANTHER; PTHR10314:SF100; PTHR10314:SF100; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..>169
FT                   /note="Cysteine synthase B"
FT                   /id="PRO_0000167114"
FT   REGION          146..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         75
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         45
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         169
SQ   SEQUENCE   169 AA;  18023 MW;  E12781E90CA77F87 CRC64;
     MTLQYQTIAD CVGNTPLVRL QRMAGNTSNT LLLKLEGNNP AGSVKDRPAL SMITRAELRG
     QIHPGDTLIE ATSGNTGIAL AMAAAIKGYR MILIMPDNSS AERKAAMTAY GAELISVSKD
     DGMEGARDLA ERMQAEGRGK VLDQFANGDN PEAHYTSTGP EIWRQTGGT