GenomeNet

Database: UniProt/SWISS-PROT
Entry: CYSM_ECOLI
LinkDB: CYSM_ECOLI
Original site: 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   11-JUN-2014, entry version 138.
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 277:1453-1462(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
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-acetyl-L-serine + hydrogen sulfide = L-
CC       cysteine + 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs 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; 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   DIP; DIP-9383N; -.
DR   IntAct; P16703; 21.
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; RLQRLDC; -.
DR   OrthoDB; EOG6Q2SP8; -.
DR   PhylomeDB; P16703; -.
DR   BioCyc; EcoCyc:ACSERLYB-MONOMER; -.
DR   BioCyc; ECOL316407:JW2414-MONOMER; -.
DR   BioCyc; MetaCyc:ACSERLYB-MONOMER; -.
DR   UniPathway; UPA00136; UER00200.
DR   EvolutionaryTrace; P16703; -.
DR   PRO; PR: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; 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; 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
//
DBGET integrated database retrieval system