CYSM_SALTY
ID CYSM_SALTY Reviewed; 303 AA.
AC P29848;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 146.
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=STM2440;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Sivaprasad A.V., Kuczek E.S., Bawden C.S., Rogers G.E.;
RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Two cysteine synthase enzymes are found. Both catalyze the
CC same reaction. Cysteine synthase B can also use thiosulfate in place of
CC sulfide to give cysteine thiosulfonate as a product.
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; X59595; CAA42164.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21334.1; -; Genomic_DNA.
DR PIR; S29567; S29567.
DR RefSeq; NP_461375.1; NC_003197.2.
DR RefSeq; WP_001093886.1; NC_003197.2.
DR PDB; 2JC3; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-303.
DR PDBsum; 2JC3; -.
DR AlphaFoldDB; P29848; -.
DR SMR; P29848; -.
DR STRING; 99287.STM2440; -.
DR PaxDb; P29848; -.
DR EnsemblBacteria; AAL21334; AAL21334; STM2440.
DR GeneID; 1253962; -.
DR KEGG; stm:STM2440; -.
DR PATRIC; fig|99287.12.peg.2578; -.
DR HOGENOM; CLU_021018_1_0_6; -.
DR OMA; GIRRWPE; -.
DR PhylomeDB; P29848; -.
DR BioCyc; SENT99287:STM2440-MON; -.
DR BRENDA; 2.5.1.144; 5542.
DR BRENDA; 2.5.1.47; 5542.
DR SABIO-RK; P29848; -.
DR UniPathway; UPA00136; UER00200.
DR EvolutionaryTrace; P29848; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cysteine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..303
FT /note="Cysteine synthase B"
FT /id="PRO_0000167109"
FT BINDING 71
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 174..178
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 255
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"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:2JC3"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:2JC3"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2JC3"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:2JC3"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 254..269
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:2JC3"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:2JC3"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:2JC3"
SQ SEQUENCE 303 AA; 32645 MW; 95435A8C09209EFD CRC64;
MNTLEQTIGN TPLVKLQRLG PDNGSEIWVK LEGNNPAGSV KDRAALSMIV EAEKRGEIKP
GDVLIEATSG NTGIALAMIA ALKGYRMKLL MPDNMSQERR AAMRAYGAEL ILVTKEQGME
GARDLALAMS ERGEGKLLDQ FNNPDNPYAH YTTTGPEIWR QTSGRITHFV SSMGTTGTIT
GVSRFLREQE KPVTIVGLQP EEGSSIPGIR RWPAEYMPGI FNASLVDEVL DIHQNDAENT
MRELAVREGI FCGVSSGGAV AGALRVARAT PGAIVVAIIC DRGDRYLSTG VFGEEHFSQG
AGI
