Reviewed, UniProtKB/Swiss-Prot P0A1E3 (CYSK_SALTY)

Names and origin

Protein names

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

Gene names

Name:	cysK
Ordered Locus Names:	STM2430

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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)

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.3
Sequence similarities	Belongs to the cysteine synthase/cystathionine beta-synthase family.

Ontologies

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 323

322

Cysteine synthase A

PRO_0000167089

Regions

Region

177 – 181

5

Pyridoxal phosphate binding

Sites

Binding site

8

1

Allosteric inhibitor

Binding site

72

1

Pyridoxal phosphate

Binding site

269

1

Allosteric inhibitor; via amide nitrogen

Binding site

273

1

Pyridoxal phosphate

Amino acid modifications

Modified residue

42

1

N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict

70

1

S → N in AAA27051. Ref.1

Sequence conflict

267 – 268

2

GI → VF in AAA27051. Ref.1

Secondary structure

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323

Helix Strand Turn

Details...

Beta strand

5 – 7

3

Helix

8 – 11

4

Beta strand

17 – 19

3

Beta strand

21 – 23

3

Beta strand

28 – 32

5

Helix

43 – 55

13

Beta strand

64 – 68

5

Helix

72 – 84

13

Beta strand

88 – 93

6

Helix

98 – 106

9

Beta strand

110 – 114

5

Helix

116 – 118

3

Helix

119 – 133

15

Turn

135 – 137

3

Beta strand

138 – 140

3

Turn

143 – 145

3

Helix

148 – 155

8

Helix

157 – 164

8

Turn

165 – 167

3

Beta strand

171 – 175

5

Beta strand

177 – 179

3

Helix

180 – 190

11

Beta strand

199 – 205

7

Helix

210 – 215

6

Helix

241 – 243

3

Beta strand

246 – 250

5

Helix

252 – 266

15

Helix

272 – 284

13

Helix

288 – 290

3

Beta strand

295 – 299

5

Helix

303 – 306

4

Helix

310 – 313

4

Helix

318 – 321

4

Sequences

	Sequence		Length	Mass (Da)
	P0A1E3-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: CE74168FAAE99B9E	FASTA	323	34,536
	10 20 30 40 50 60 MSKIYEDNSL TIGHTPLVRL NRIGNGRILA KVESRNPSFS VKCRIGANMI WDAEKRGVLK 70 80 90 100 110 120 PGVELVEPTS GNTGIALAYV AAARGYKLTL TMPETMSIER RKLLKALGAN LVLTEGAKGM 130 140 150 160 170 180 KGAIQKAEEI VASDPQKYLL LQQFSNPANP EIHEKTTGPE IWEDTDGQVD VFISGVGTGG 190 200 210 220 230 240 TLTGVTRYIK GTKGKTDLIT VAVEPTDSPV IAQALAGEEI KPGPHKIQGI GAGFIPGNLD 250 260 270 280 290 300 LKLIDKVVGI TNEEAISTAR RLMEEEGILA GISSGAAVAA ALKLQEDESF TNKNIVVILP 310 320 SSGERYLSTA LFADLFTEKE LQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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], PROTEIN SEQUENCE OF 2-16 AND 321-323. Strain: LT2.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium." Burkhard P., Rao G.S.J., Hohenester E., Schnackerz K.D., Cook P.F., Jansonius J.N. J. Mol. Biol. 283:121-133(1998) [PubMed: 9761678] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, SUBUNIT, SEQUENCE REVISION TO 267-268.
[4]	"Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium." Burkhard P., Tai C.-H., Ristroph C.M., Cook P.F., Jansonius J.N. J. Mol. Biol. 291:941-953(1999) [PubMed: 10452898] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) MUTANT ALA-42 IN COMPLEX WITH PYRIDOXAL PHOSPHATE.
[5]	"Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound." Burkhard P., Tai C.-H., Jansonius J.N., Cook P.F. J. Mol. Biol. 303:279-286(2000) [PubMed: 11023792] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, ALLOSTERIC REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M21450 Genomic DNA. Translation: AAA27051.1.
AE006468 Genomic DNA. Translation: AAL21324.1.

PIR

SYEBAC. B28181.

RefSeq

NP_461365.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D6S	X-ray	2.30	A/B	2-323	[»]
1FCJ	X-ray	2.00	A/B/C/D	2-323	[»]
1OAS	X-ray	2.20	A/B	2-323	[»]

ModBase

Search...

Proteomic databases

PRIDE

P0A1E3.

Genome annotation databases

GeneID

1253952.

GenomeReviews

Gene locus STM2430 in contig AE006468_GR.

KEGG

stm:STM2430.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG748215.

OMA

KYFMPGQ.

Enzyme and pathway databases

BioCyc

STYP99287:STM2430-MONOMER.

BRENDA

2.5.1.47. 2.

Family and domain databases

InterPro

IPR001216. Cys_synth_BS.
IPR005856. Cys_synthKM.
IPR005859. CysK.
IPR001926. PyrdxlP-dep_enz_bsu.
[Graphical view]

Pfam

PF00291. PALP. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01139. cysK. 1 hit.
TIGR01136. cysKM. 1 hit.

PROSITE

PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CYSK_SALTY

Accession

Primary (citable) accession number: P0A1E3
Secondary accession number(s): P12674

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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