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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   26-NOV-2014, entry version 142.
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:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
CC       cysteine from L-serine: step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15952768}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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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_000913.3.
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   SMR; P16703; 2-293.
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   InParanoid; P16703; -.
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   SABIO-RK; P16703; -.
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; IPR005856; Cys_synthKM.
DR   InterPro; IPR005858; CysM.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PLP-dep.
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                                {ECO:0000269|PubMed:15952768}.
FT   BINDING     255    255       Pyridoxal phosphate.
FT                                {ECO:0000269|PubMed:15952768}.
FT   MOD_RES      41     41       N6-(pyridoxal phosphate)lysine.
FT   HELIX         4      7       {ECO:0000244|PDB:2V03}.
FT   STRAND       13     15       {ECO:0000244|PDB:2V03}.
FT   STRAND       17     20       {ECO:0000244|PDB:2V03}.
FT   STRAND       22     24       {ECO:0000244|PDB:2V03}.
FT   STRAND       26     31       {ECO:0000244|PDB:2V03}.
FT   HELIX        32     34       {ECO:0000244|PDB:2V03}.
FT   HELIX        41     54       {ECO:0000244|PDB:2V03}.
FT   STRAND       63     67       {ECO:0000244|PDB:2V03}.
FT   HELIX        71     83       {ECO:0000244|PDB:2V03}.
FT   STRAND       86     92       {ECO:0000244|PDB:2V03}.
FT   HELIX        97    105       {ECO:0000244|PDB:2V03}.
FT   STRAND      109    113       {ECO:0000244|PDB:2V03}.
FT   TURN        115    117       {ECO:0000244|PDB:2V03}.
FT   HELIX       118    131       {ECO:0000244|PDB:2V03}.
FT   STRAND      134    137       {ECO:0000244|PDB:2BHS}.
FT   TURN        140    142       {ECO:0000244|PDB:2V03}.
FT   HELIX       145    152       {ECO:0000244|PDB:2V03}.
FT   HELIX       154    161       {ECO:0000244|PDB:2V03}.
FT   TURN        162    164       {ECO:0000244|PDB:2V03}.
FT   STRAND      168    172       {ECO:0000244|PDB:2V03}.
FT   STRAND      174    176       {ECO:0000244|PDB:2V03}.
FT   HELIX       177    187       {ECO:0000244|PDB:2V03}.
FT   STRAND      189    191       {ECO:0000244|PDB:2V03}.
FT   STRAND      194    200       {ECO:0000244|PDB:2V03}.
FT   HELIX       214    216       {ECO:0000244|PDB:2V03}.
FT   HELIX       223    225       {ECO:0000244|PDB:2V03}.
FT   STRAND      227    232       {ECO:0000244|PDB:2V03}.
FT   HELIX       234    248       {ECO:0000244|PDB:2V03}.
FT   HELIX       254    269       {ECO:0000244|PDB:2V03}.
FT   STRAND      274    279       {ECO:0000244|PDB:2V03}.
FT   STRAND      281    283       {ECO:0000244|PDB:2V03}.
FT   HELIX       284    289       {ECO:0000244|PDB:2V03}.
FT   TURN        290    292       {ECO:0000244|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
//
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