P0ABK5 (CYSK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cysteine synthase A
Short name=CSase A
EC=2.5.1.47

Alternative name(s):
O-acetylserine (thiol)-lyase A
Short name=OAS-TL A
O-acetylserine sulfhydrylase A
S-carboxymethylcysteine synthase
EC=4.5.1.5
Sulfate starvation-induced protein 5
Short name=SSI5

Gene names

Name:	cysK
Synonyms:	cysZ
Ordered Locus Names:	b2414, JW2407

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	O(3)-acetyl-L-serine + H2S = L-cysteine + acetate. Ref.6 3-chloro-L-alanine + thioglycolate = S-carboxymethyl-L-cysteine + chloride. Ref.6
Cofactor	Pyridoxal phosphate. Ref.6
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
Subunit structure	Homodimer. Ref.6
Induction	Repressed by sulfate or cysteine.
Sequence similarities	Belongs to the cysteine synthase/cystathionine beta-synthase family.
Biophysicochemical properties	Kinetic parameters: KM=40 mM for 3-chloro-L-alanine Ref.6 KM=15.4 mM for thioglycolate pH dependence: Optimum pH is 9-10.5. Temperature dependence: Optimum temperature is 50 degrees Celsius.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Lyase Transferase
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process from serine Inferred from direct assay. Source: EcoCyc
Cellular component	cysteine synthase complex Inferred from direct assay. Source: EcoCyc cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	L-cysteine desulfhydrase activity Inferred from mutant phenotype. Source: EcoCyc S-carboxymethylcysteine synthase activity Inferred from electronic annotation. Source: EC cysteine synthase activity Inferred from direct assay. Source: EcoCyc pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity Inferred from direct assay. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
	Chain	2 – 323	322	Cysteine synthase A		PRO_0000167086
Regions
	Region	177 – 181	5	Pyridoxal phosphate binding By similarity
Sites
	Binding site	8	1	Allosteric inhibitor By similarity
	Binding site	72	1	Pyridoxal phosphate By similarity
	Binding site	269	1	Allosteric inhibitor; via amide nitrogen By similarity
	Binding site	273	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	42	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	182	1	L → W in AAA23654. Ref.2
	Sequence conflict	186 – 187	2	SR → TP in AAA23654. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P0ABK5 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 20ADDE911845AE72	FASTA	323	34,490
	10 20 30 40 50 60 MSKIFEDNSL TIGHTPLVRL NRIGNGRILA KVESRNPSFS VKCRIGANMI WDAEKRGVLK 70 80 90 100 110 120 PGVELVEPTS GNTGIALAYV AAARGYKLTL TMPETMSIER RKLLKALGAN LVLTEGAKGM 130 140 150 160 170 180 KGAIQKAEEI VASNPEKYLL LQQFSNPANP EIHEKTTGPE IWEDTDGQVD VFIAGVGTGG 190 200 210 220 230 240 TLTGVSRYIK GTKGKTDLIS VAVEPTDSPV IAQALAGEEI KPGPHKIQGI GAGFIPANLD 250 260 270 280 290 300 LKLVDKVIGI TNEEAISTAR RLMEEEGILA GISSGAAVAA ALKLQEDESF TNKNIVVILP 310 320 SSGERYLSTA LFADLFTEKE LQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phylogeny of metabolic pathways: O-acetylserine sulphydrylase A is homologous to the tryptophan synthase beta subunit." Levy S., Danchin A. Mol. Microbiol. 2:777-783(1988) [PubMed: 3062311] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH." Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M. J. Bacteriol. 170:3150-3157(1988) [PubMed: 3290198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"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. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., 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.
[4]	"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.
[5]	"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.
[6]	"S-carboxymethylcysteine synthase from Escherichia coli." Kumagai H., Suzuki H., Shigematsu H., Tochikura T. Agric. Biol. Chem. 53:2481-2487(1989) Cited for: PROTEIN SEQUENCE OF 2-37, FUNCTION AS S-CARBOXYMETHYLCYSTEINE SYNTHASE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[8]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]	"Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli." Quadroni M., Staudenmann W., Kertesz M.A., James P. Eur. J. Biochem. 239:773-781(1996) [PubMed: 8774726] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11; 14-19; 36-42; 127-137 AND 236-242. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[10]	"Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases." Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., Watanabe C. Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993) [PubMed: 8506346] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-9.
[11]	"The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription." de Reuse H., Danchin A. J. Bacteriol. 170:3827-3837(1988) [PubMed: 2457575] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 315-323.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X12615 Genomic DNA. Translation: CAA31137.1. M21451 Genomic DNA. Translation: AAA23654.1. U00096 Genomic DNA. Translation: AAC75467.1. AP009048 Genomic DNA. Translation: BAA16288.1. M21994 Genomic DNA. Translation: AAA24383.1.
PIR	SYECAC. E65015.
RefSeq	NP_416909.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0ABK5.
SMR	P0ABK5. Positions 2-305.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-36170N.
IntAct	P0ABK5. 15 interactions.
MINT	MINT-1240013.
2D gel databases
SWISS-2DPAGE	P0ABK5.
2DBase-Ecoli	P0ABK5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000003304; EBESCP00000003304; EBESCG00000002708. EBESCT00000015969; EBESCP00000015260; EBESCG00000015029.
GeneID	946877.
GenomeReviews	Gene locus JW2407 in contig AP009048_GR. Gene locus b2414 in contig U00096_GR.
KEGG	ecj:JW2407. eco:b2414.
PATRIC	32120211. VBIEscCol129921_2508.
Organism-specific databases
EchoBASE	EB0189.
EcoGene	EG10192. cysK.
Phylogenomic databases
eggNOG	COG0031.
GeneTree	EBGT00050000009701.
HOGENOM	HBG748215.
OMA	AHSIGNT.
PhylomeDB	P0ABK5.
ProtClustDB	PRK10717.
Enzyme and pathway databases
BioCyc	EcoCyc:ACSERLYA-MONOMER. MetaCyc:ACSERLYA-MONOMER.
Gene expression databases
Genevestigator	P0ABK5.
Family and domain databases
InterPro	IPR001216. Cys_synth_BS. IPR005856. Cys_synthKM. IPR005859. CysK. IPR001926. PyrdxlP-dep_enz_bsu. [Graphical view]
KO	K01738.
Pfam	PF00291. PALP. 1 hit. [Graphical view]
SUPFAM	SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMs	TIGR01139. CysK. 1 hit. TIGR01136. CysKM. 1 hit.
PROSITE	PS00901. CYS_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSK_ECOLI

Accession

Primary (citable) accession number: P0ABK5
Secondary accession number(s): P11096, P21546

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program