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CYSM_PSEAE
ID   CYSM_PSEAE              Reviewed;         299 AA.
AC   Q9I526;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
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;
GN   Name=cysM; OrderedLocusNames=PA0932;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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         Evidence={ECO:0000250};
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; AE004091; AAG04321.1; -; Genomic_DNA.
DR   PIR; A83530; A83530.
DR   RefSeq; NP_249623.1; NC_002516.2.
DR   RefSeq; WP_003102419.1; NZ_QZGE01000007.1.
DR   AlphaFoldDB; Q9I526; -.
DR   SMR; Q9I526; -.
DR   STRING; 287.DR97_1007; -.
DR   PaxDb; Q9I526; -.
DR   PRIDE; Q9I526; -.
DR   EnsemblBacteria; AAG04321; AAG04321; PA0932.
DR   GeneID; 881832; -.
DR   KEGG; pae:PA0932; -.
DR   PATRIC; fig|208964.12.peg.967; -.
DR   PseudoCAP; PA0932; -.
DR   HOGENOM; CLU_021018_1_0_6; -.
DR   InParanoid; Q9I526; -.
DR   OMA; GIRRWPE; -.
DR   PhylomeDB; Q9I526; -.
DR   BioCyc; PAER208964:G1FZ6-952-MON; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000002438; 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; 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   TIGRFAMs; TIGR01136; cysKM; 1.
DR   TIGRFAMs; TIGR01138; cysM; 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..299
FT                   /note="Cysteine synthase B"
FT                   /id="PRO_0000287759"
FT   BINDING         75
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         178..182
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
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"
SQ   SEQUENCE   299 AA;  32448 MW;  9B78F6986CD14CC8 CRC64;
     MTVQYPTIAD CVGNTPLVRL QRLPGETSNT LLVKLEGNNP AGSVKDRPAL SMITRAELRG
     DIRPGDTLIE ATSGNTGIAL AMAAAIKGYK MILIMPDNST AERKAAMTAY GAELILVSKE
     EGMEGARDLA DKLQREGRGK VLDQFANGDN PEAHYHSTGP EIWQQTGGSI THFVSSMGTT
     GTIMGVSRYL KEQNPAVQIV GLQPMEGSAI PGIRRWPQEY LPKIYDASRV DRVVDMHQDE
     AEDIMRRLAR EEGIFCGVSS GGAVAAMLRL SRELENAVLV AIICDRGDRY LSSGVYDPR
 
 
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