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 01-MAY-2013, entry version 130.
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; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2188958;
RA Sirko A., Hryniewicz M.M., Hulanicka D.M., Boeck A.;
RT "Sulfate and thiosulfate transport in Escherichia coli K-12:
RT nucleotide 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.,
RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT analysis of 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.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(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
RT MG1655 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
RP IN 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
CC the same reaction. Cysteine synthase B can also use thiosulfate in
CC place of sulfide to give cysteine thiosulfonate as a product.
CC -!- CATALYTIC ACTIVITY: O(3)-acetyl-L-serine + H(2)S = L-cysteine +
CC acetate.
CC -!- COFACTOR: Pyridoxal phosphate.
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
CC cysteine from L-serine: step 2/2.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family.
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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_000913.2.
DR RefSeq; YP_490657.1; NC_007779.1.
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 ProteinModelPortal; P16703; -.
DR SMR; P16703; 2-293.
DR DIP; DIP-9383N; -.
DR IntAct; P16703; 9.
DR MINT; MINT-1300981; -.
DR STRING; 511145.b2421; -.
DR SWISS-2DPAGE; P16703; -.
DR PaxDb; P16703; -.
DR EnsemblBacteria; AAC75474; AAC75474; b2421.
DR EnsemblBacteria; BAA16295; BAA16295; BAA16295.
DR GeneID; 12930332; -.
DR GeneID; 946888; -.
DR KEGG; ecj:Y75_p2382; -.
DR KEGG; eco:b2421; -.
DR PATRIC; 32120227; VBIEscCol129921_2516.
DR EchoBASE; EB0190; -.
DR EcoGene; EG10193; cysM.
DR eggNOG; COG0031; -.
DR HOGENOM; HOG000217394; -.
DR KO; K12339; -.
DR OMA; CEVALRI; -.
DR ProtClustDB; PRK11761; -.
DR BioCyc; EcoCyc:ACSERLYB-MONOMER; -.
DR BioCyc; ECOL316407:JW2414-MONOMER; -.
DR BioCyc; MetaCyc:ACSERLYB-MONOMER; -.
DR SABIO-RK; P16703; -.
DR UniPathway; UPA00136; UER00200.
DR EvolutionaryTrace; P16703; -.
DR Genevestigator; P16703; -.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:EcoCyc.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IMP:EcoCyc.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IDA:EcoCyc.
DR InterPro; IPR001216; Cys_synth_BS.
DR InterPro; IPR005856; Cys_synthKM.
DR InterPro; IPR005858; CysM.
DR InterPro; IPR001926; Trp_syn_b_sub_like_PLP_eny_SF.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; PyrdxlP-dep_enz_bsu; 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; Complete proteome;
KW Cysteine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1 303 Cysteine synthase B.
FT /FTId=PRO_0000167108.
FT REGION 174 178 Pyridoxal phosphate binding.
FT BINDING 71 71 Pyridoxal phosphate.
FT BINDING 255 255 Pyridoxal phosphate.
FT MOD_RES 41 41 N6-(pyridoxal phosphate)lysine.
FT HELIX 4 7
FT STRAND 13 15
FT STRAND 17 20
FT STRAND 22 24
FT STRAND 26 31
FT HELIX 32 34
FT HELIX 41 54
FT STRAND 63 67
FT HELIX 71 83
FT STRAND 86 92
FT HELIX 97 105
FT STRAND 109 113
FT TURN 115 117
FT HELIX 118 131
FT STRAND 134 137
FT TURN 140 142
FT HELIX 145 152
FT HELIX 154 161
FT TURN 162 164
FT STRAND 168 172
FT STRAND 174 176
FT HELIX 177 187
FT STRAND 189 191
FT STRAND 194 200
FT HELIX 214 216
FT HELIX 223 225
FT STRAND 227 232
FT HELIX 234 248
FT HELIX 254 269
FT STRAND 274 279
FT STRAND 281 283
FT HELIX 284 289
FT TURN 290 292
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
//
