Cysteine synthase B - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P16703 (CYSM_ECOLI)

Last modified February 9, 2010. Version 104. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Cysteine synthase B
      Short name=CSase B
    EC=2.5.1.47
Alternative name(s):
    O-acetylserine sulfhydrylase B
    O-acetylserine (thiol)-lyase B
      Short name=OAS-TL B

Gene names

Name:	cysM
Ordered Locus Names:	b2421, JW2414

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product.
Catalytic activity	O(3)-acetyl-L-serine + H₂S = L-cysteine + acetate.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
Subunit structure	Homodimer. Ref.5
Sequence similarities	Belongs to the cysteine synthase/cystathionine beta-synthase family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process from serine Inferred from direct assay. Source: UniProtKB
Molecular function	cysteine synthase activity Inferred from direct assay. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 303

303

Cysteine synthase B

PRO_0000167108

Regions

Region

174 – 178

Pyridoxal phosphate binding

Sites

Binding site

Pyridoxal phosphate

Binding site

255

Pyridoxal phosphate

Amino acid modifications

Modified residue

N6-(pyridoxal phosphate)lysine

Secondary structure

303

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P16703-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 1C7FBCB943FCFE39
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FASTA

303

32,664

        10         20         30         40         50         60 
MSTLEQTIGN TPLVKLQRMG PDNGSEVWLK LEGNNPAGSV KDRAALSMIV EAEKRGEIKP 

        70         80         90        100        110        120 
GDVLIEATSG NTGIALAMIA ALKGYRMKLL MPDNMSQERR AAMRAYGAEL ILVTKEQGME 

       130        140        150        160        170        180 
GARDLALEMA NRGEGKLLDQ FNNPDNPYAH YTTTGPEIWQ QTGGRITHFV SSMGTTGTIT 

       190        200        210        220        230        240 
GVSRFMREQS KPVTIVGLQP EEGSSIPGIR RWPTEYLPGI FNASLVDEVL DIHQRDAENT 

       250        260        270        280        290        300 
MRELAVREGI FCGVSSGGAV AGALRVAKAN PDAVVVAIIC DRGDRYLSTG VFGEEHFSQG 


AGI

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sulfate and thiosulfate transport in Escherichia coli K-12: nucleotide sequence and expression of the cysTWAM gene cluster." Sirko A., Hryniewicz M.M., Hulanicka D.M., Boeck A. J. Bacteriol. 172:3351-3357(1990) [PubMed: 2188958] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli." Claus M.T., Zocher G.E., Maier T.H.P., Schulz G.E. Biochemistry 44:8620-8626(2005) [PubMed: 15952768] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF WILD-TYPE AND MUTANT CYSM-RKE IN COMPLEX WITH PYRIDOXAL PHOSPHATE, SUBUNIT.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M32101 Genomic DNA. Translation: AAA23640.1.
U00096 Genomic DNA. Translation: AAC75474.1.
AP009048 Genomic DNA. Translation: BAA16295.1.

PIR

SYECBC. D35402.

RefSeq

AP_003015.1.
NP_416916.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BHS	X-ray	2.67	A/B/C/D	1-303	[»]
2BHT	X-ray	2.10	A/B/C/D	1-303	[»]
2V03	X-ray	1.33	A	1-303	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9383N.

STRING

P16703.

2-D gel databases

SWISS-2DPAGE

P16703.

Genome annotation databases

GeneID

946888.

GenomeReviews

Gene locus JW2414 in contig AP009048_GR.
Gene locus b2421 in contig U00096_GR.

KEGG

ecj:JW2414.
eco:b2421.

Organism-specific databases

EchoBASE

EB0190.

EcoGene

EG10193. cysM.

CMR

Search...

Phylogenomic databases

eggNOG

COG0031.

HOGENOM

HBG748215.

OMA

NSTQERK.

Enzyme and pathway databases

BioCyc

EcoCyc:ACSERLYB-MONOMER.
ECOL168927:B2421-MONOMER.
MetaCyc:ACSERLYB-MONOMER.

Gene expression databases

Genevestigator

P16703.

Family and domain databases

InterPro

IPR001216. Cys_synth_BS.
IPR005856. Cys_synthKM.
IPR005858. CysM.
IPR001926. PyrdxlP-dep_enz_bsu.
[Graphical view]

Pfam

PF00291. PALP. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01136. cysKM. 1 hit.
TIGR01138. cysM. 1 hit.

PROSITE

PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

CYSM_ECOLI

Accession

Primary (citable) accession number: P16703

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	February 9, 2010
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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