CYSM_ECOLI
ID CYSM_ECOLI Reviewed; 303 AA.
AC P16703;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 184.
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=b2421, JW2414;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2188958; DOI=10.1128/jb.172.6.3351-3357.1990;
RA Sirko A., Hryniewicz M.M., Hulanicka D.M., Boeck A.;
RT "Sulfate and thiosulfate transport in Escherichia coli K-12: nucleotide
RT sequence and expression of the cysTWAM gene cluster.";
RL J. Bacteriol. 172:3351-3357(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF WILD-TYPE AND MUTANT CYSM-RKE IN
RP COMPLEX WITH PYRIDOXAL PHOSPHATE, AND SUBUNIT.
RX PubMed=15952768; DOI=10.1021/bi050485+;
RA Claus M.T., Zocher G.E., Maier T.H.P., Schulz G.E.;
RT "Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from
RT Escherichia coli.";
RL Biochemistry 44:8620-8626(2005).
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15952768}.
CC -!- INTERACTION:
CC P16703; P24182: accC; NbExp=3; IntAct=EBI-542376, EBI-542308;
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M32101; AAA23640.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75474.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16295.1; -; Genomic_DNA.
DR PIR; D35402; SYECBC.
DR RefSeq; NP_416916.1; NC_000913.3.
DR RefSeq; WP_001336044.1; NZ_LN832404.1.
DR PDB; 2BHS; X-ray; 2.67 A; A/B/C/D=1-303.
DR PDB; 2BHT; X-ray; 2.10 A; A/B/C/D=1-303.
DR PDB; 2V03; X-ray; 1.33 A; A=1-303.
DR PDBsum; 2BHS; -.
DR PDBsum; 2BHT; -.
DR PDBsum; 2V03; -.
DR AlphaFoldDB; P16703; -.
DR SMR; P16703; -.
DR BioGRID; 4259326; 6.
DR BioGRID; 851228; 13.
DR DIP; DIP-9383N; -.
DR IntAct; P16703; 21.
DR STRING; 511145.b2421; -.
DR SWISS-2DPAGE; P16703; -.
DR PaxDb; P16703; -.
DR PRIDE; P16703; -.
DR EnsemblBacteria; AAC75474; AAC75474; b2421.
DR EnsemblBacteria; BAA16295; BAA16295; BAA16295.
DR GeneID; 946888; -.
DR KEGG; ecj:JW2414; -.
DR KEGG; eco:b2421; -.
DR PATRIC; fig|1411691.4.peg.4310; -.
DR EchoBASE; EB0190; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_1_0_6; -.
DR InParanoid; P16703; -.
DR OMA; GIRRWPE; -.
DR PhylomeDB; P16703; -.
DR BioCyc; EcoCyc:ACSERLYB-MON; -.
DR BioCyc; MetaCyc:ACSERLYB-MON; -.
DR BRENDA; 2.5.1.47; 2026.
DR SABIO-RK; P16703; -.
DR UniPathway; UPA00136; UER00200.
DR EvolutionaryTrace; P16703; -.
DR PRO; PR:P16703; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:EcoCyc.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IMP:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IDA:EcoCyc.
DR GO; GO:0019345; P:cysteine biosynthetic process via S-sulfo-L-cysteine; IMP:EcoCyc.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:EcoCyc.
DR GO; GO:0019450; P:L-cysteine catabolic process to pyruvate; IMP:EcoCyc.
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_0000167108"
FT BINDING 71
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:15952768"
FT BINDING 174..178
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 255
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:15952768"
FT MOD_RES 41
FT /note="N6-(pyridoxal phosphate)lysine"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:2V03"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2BHS"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:2V03"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 254..269
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:2V03"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:2V03"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:2V03"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:2V03"
SQ SEQUENCE 303 AA; 32664 MW; 1C7FBCB943FCFE39 CRC64;
MSTLEQTIGN TPLVKLQRMG PDNGSEVWLK LEGNNPAGSV KDRAALSMIV EAEKRGEIKP
GDVLIEATSG NTGIALAMIA ALKGYRMKLL MPDNMSQERR AAMRAYGAEL ILVTKEQGME
GARDLALEMA NRGEGKLLDQ FNNPDNPYAH YTTTGPEIWQ QTGGRITHFV SSMGTTGTIT
GVSRFMREQS KPVTIVGLQP EEGSSIPGIR RWPTEYLPGI FNASLVDEVL DIHQRDAENT
MRELAVREGI FCGVSSGGAV AGALRVAKAN PDAVVVAIIC DRGDRYLSTG VFGEEHFSQG
AGI
