ID   Y4XP_SINFN              Reviewed;         336 AA.
AC   P55708;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Putative cysteine synthase;
DE            EC=2.5.1.47;
DE   AltName: Full=O-acetylserine (Thiol)-lyase;
DE   AltName: Full=O-acetylserine sulfhydrylase;
DE            Short=CSase;
GN   OrderedLocusNames=NGR_a00730; ORFNames=y4xP;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: As it is highly similar to bacterial and plant cysteine
CC       synthases, it is possible that it catalyzes a related reaction.
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   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; U00090; AAB91939.1; -; Genomic_DNA.
DR   RefSeq; NP_444152.1; NC_000914.2.
DR   RefSeq; WP_010875114.1; NC_000914.2.
DR   AlphaFoldDB; P55708; -.
DR   SMR; P55708; -.
DR   STRING; 394.NGR_a00730; -.
DR   EnsemblBacteria; AAB91939; AAB91939; NGR_a00730.
DR   KEGG; rhi:NGR_a00730; -.
DR   PATRIC; fig|394.7.peg.65; -.
DR   eggNOG; COG0031; Bacteria.
DR   HOGENOM; CLU_021018_1_0_5; -.
DR   OMA; GSWCPDQ; -.
DR   OrthoDB; 1033353at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
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; 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   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Plasmid;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..336
FT                   /note="Putative cysteine synthase"
FT                   /id="PRO_0000167136"
FT   BINDING         71
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         179..183
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         41
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   336 AA;  35415 MW;  9D31197DE4163A66 CRC64;
     MLHTTVTQLI GQTPVMSIDV PGRNATLVLK IEKNNPGGSM KDRMARSMVI AALQDGRLPP
     GGTIVESSSG NTGTGLALAA LEFGLRFIAV VDHHAAPDKI RMMRALGAEI RYVEGDFRED
     EVAVVERQRL AAQLGAQLPG ALFMNQSDNP ANPEGYTGLV DELVAQLPDG IDAFVGCVGT
     GGSMTGISQR LKRNNPAVRT IAVEPAGSIV FGKPGHPYYQ SGTGTPAGDE VGKVLDYGCI
     DEGVQVTDTQ AFETARYIAR RKGLLVGGST GGAIYKALEF IGAGKLTGTV VTTVADGGEK
     YLGTIFDEEW MAKRRLLDPA IAAQLDGWLF GKARAA