P47998 (CYSK1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cysteine synthase
EC=2.5.1.47

Alternative name(s):
At.OAS.5-8
CSase A
Short name=CS-A
Cys-3A
O-acetylserine (thiol)-lyase
Short name=OAS-TL A
O-acetylserine sulfhydrylase

Gene names

Name:	OASA1
Synonyms:	OAS1, OASS
Ordered Locus Names:	At4g14880
ORF Names:	dl3480c

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	O(3)-acetyl-L-serine + H2S = L-cysteine + acetate.
Cofactor	Pyridoxal phosphate. Ref.11
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
Subunit structure	Homodimer. Interacts with SAT1 to form the cysteine synthase complex. Ref.10 Ref.11
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the cysteine synthase/cystathionine beta-synthase family.
Biophysicochemical properties	Kinetic parameters: KM=1.4 mM for O-acetylserine (at pH 7.0 and 25 degrees Celsius) Ref.10 KM=0.22 mM for Na2S (at pH 7.0 and 25 degrees Celsius)

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	aging Inferred from mutant phenotype. Source: TAIR cysteine biosynthetic process from serine Traceable author statement Ref.4. Source: TAIR response to cadmium ion Inferred from direct assay. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR cytosol Inferred from direct assay. Source: TAIR nucleus Inferred from direct assay. Source: TAIR peroxisome Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR vacuolar membrane Inferred from direct assay. Source: TAIR
Molecular function	cysteine synthase activity Inferred from direct assay Ref.4. Source: TAIR protein binding Inferred from physical interaction. Source: TAIR 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

Chain

1 – 322

322

Cysteine synthase

PRO_0000167116

Regions

Region

181 – 185

5

Pyridoxal phosphate binding

Region

217 – 222

6

SAT1 binding

Sites

Binding site

77

1

Pyridoxal phosphate

Binding site

269

1

Pyridoxal phosphate

Amino acid modifications

Modified residue

46

1

N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis

46

1

K → A: No cysteine synthase activity. Ref.10

Mutagenesis

74

1

T → A: Strong reduction of cysteine synthase activity. Ref.10

Mutagenesis

74

1

T → S: Reduction of cysteine synthase activity. Ref.10

Mutagenesis

75

1

S → A, N or T: Strong reduction of cysteine synthase activity. Ref.10

Mutagenesis

77

1

N → A: Reduction of cysteine synthase activity. Ref.10

Mutagenesis

77

1

N → D: Strong reduction of cysteine synthase activity. Ref.10

Mutagenesis

78

1

T → A or S: Reduction of cysteine synthase activity. Ref.10

Mutagenesis

147

1

Q → A or E: Strong reduction of cysteine synthase activity. Ref.10

Mutagenesis

157

1

H → Q or N: Slight reduction of cysteine synthase activity. Ref.10

Mutagenesis

182

1

T → A or S: Slight reduction of cysteine synthase activity. Ref.10

Mutagenesis

185

1

T → A or S: Strong reduction of cysteine synthase activity. Ref.10

Mutagenesis

217

1

K → A: Impaired interaction with SAT1. Ref.10

Mutagenesis

221

1

H → A: Impaired interaction with SAT1. Ref.10

Mutagenesis

222

1

K → A: Impaired interaction with SAT1. Ref.10

Mutagenesis

269

1

S → A: Strong reduction of cysteine synthase activity. Ref.10

Mutagenesis

269

1

S → T: Reduction of cysteine synthase activity. Ref.10

Sequence conflict

20

1

Missing in AAK76499. Ref.8

Sequence conflict

273

1

A → E in CAA58893. Ref.3

Secondary structure

1

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322

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Helix

9 – 12

4

Beta strand

18 – 20

3

Helix

23 – 25

3

Beta strand

29 – 36

8

Helix

37 – 39

3

Helix

46 – 59

14

Turn

65 – 67

3

Beta strand

69 – 73

5

Helix

77 – 89

13

Beta strand

92 – 98

7

Helix

103 – 111

9

Beta strand

115 – 119

5

Helix

121 – 123

3

Helix

124 – 138

15

Beta strand

142 – 144

3

Turn

147 – 149

3

Helix

152 – 159

8

Helix

161 – 168

8

Turn

169 – 171

3

Beta strand

175 – 179

5

Beta strand

181 – 183

3

Helix

184 – 196

13

Beta strand

201 – 207

7

Helix

208 – 210

3

Helix

212 – 214

3

Helix

237 – 239

3

Beta strand

241 – 246

6

Helix

248 – 262

15

Helix

268 – 281

14

Helix

284 – 286

3

Beta strand

290 – 295

6

Helix

299 – 302

4

Helix

306 – 308

3

Helix

309 – 316

8

Sequences

	Sequence		Length	Mass (Da)
	P47998 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 5B3E7F3D9DA5908B	FASTA	322	33,805
	10 20 30 40 50 60 MASRIAKDVT ELIGNTPLVY LNNVAEGCVG RVAAKLEMME PCSSVKDRIG FSMISDAEKK 70 80 90 100 110 120 GLIKPGESVL IEPTSGNTGV GLAFTAAAKG YKLIITMPAS MSTERRIILL AFGVELVLTD 130 140 150 160 170 180 PAKGMKGAIA KAEEILAKTP NGYMLQQFEN PANPKIHYET TGPEIWKGTG GKIDGFVSGI 190 200 210 220 230 240 GTGGTITGAG KYLKEQNANV KLYGVEPVES AILSGGKPGP HKIQGIGAGF IPSVLNVDLI 250 260 270 280 290 300 DEVVQVSSDE SIDMARQLAL KEGLLVGISS GAAAAAAIKL AQRPENAGKL FVAIFPSFGE 310 320 RYLSTVLFDA TRKEAEAMTF EA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana." Hell R., Bork C., Bogdanova N., Frolov I., Hauschild R. FEBS Lett. 351:257-262(1994) [PubMed: 8082776] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Leaf.
[2]	Hell R. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"A new member of the cytosolic O-acetylserine(thiol)lyase gene family in Arabidopsis thaliana." Barroso C., Vega J.M., Gotor C. FEBS Lett. 363:1-5(1995) [PubMed: 7729527] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Genomic and functional characterization of the oas gene family encoding O-acetylserine (thiol) lyases, enzymes catalyzing the final step in cysteine biosynthesis in Arabidopsis thaliana." Jost R., Berkowitz O., Wirtz M., Hopkins L., Hawkesford M.J., Hell R. Gene 253:237-247(2000) [PubMed: 10940562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[5]	"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana." Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N. Nature 391:485-488(1998) [PubMed: 9461215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[6]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[7]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[8]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[9]	"Arabidopsis ORF clones." Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[10]	"Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of o-acetylserine sulfhydrylase from Arabidopsis thaliana." Bonner E.R., Cahoon R.E., Knapke S.M., Jez J.M. J. Biol. Chem. 280:38803-38813(2005) [PubMed: 16166087] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-46, SUBUNIT, INTERACTION WITH SAT1, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-46; THR-74; SER-75; ASN-77; THR-78; GLN-147; HIS-157; THR-182; THR-185; LYS-217; HIS-221; LYS-222 AND SER-269.
[11]	"Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex." Francois J.A., Kumaran S., Jez J.M. Plant Cell 18:3647-3655(2006) [PubMed: 17194764] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 3-322, COFACTOR, SUBUNIT, INTERACTION WITH SAT1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X80376 mRNA. Translation: CAA56593.2.
X84097 mRNA. Translation: CAA58893.1.
AJ272027 Genomic DNA. Translation: CAB72932.1.
Z97337 Genomic DNA. Translation: CAB10267.1.
AL161540 Genomic DNA. Translation: CAB78530.1.
CP002687 Genomic DNA. Translation: AEE83512.1.
CP002687 Genomic DNA. Translation: AEE83513.1.
CP002687 Genomic DNA. Translation: AEE83514.1.
CP002687 Genomic DNA. Translation: AEE83515.1.
AY045825 mRNA. Translation: AAK76499.1.
BT025878 mRNA. Translation: ABF85780.1.

IPI

IPI00519731.

PIR

A71412.
S48694.

RefSeq

NP_001190732.1. NM_001203803.1.
NP_001190733.1. NM_001203804.1.
NP_193224.1. NM_117574.3.
NP_849386.1. NM_179055.3.

UniGene

At.30.
At.34389.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z7W	X-ray	2.20	A	1-322	[»]
1Z7Y	X-ray	2.70	A	1-322	[»]
2ISQ	X-ray	2.80	A	3-322	[»]

ProteinModelPortal

P47998.

SMR

P47998. Positions 3-322.

ModBase

Search...

Protein-protein interaction databases

IntAct

P47998. 4 interactions.

STRING

P47998.

Proteomic databases

PRIDE

P47998.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT4G14880.1; AT4G14880.1; AT4G14880.
AT4G14880.2; AT4G14880.2; AT4G14880.
AT4G14880.3; AT4G14880.3; AT4G14880.
AT4G14880.4; AT4G14880.4; AT4G14880.

GeneID

827145.

KEGG

ath:AT4G14880.

Organism-specific databases

TAIR

At4g14880.

Phylogenomic databases

eggNOG

KOG1252.

InParanoid

P47998.

OMA

SCGERYM.

PhylomeDB

P47998.

ProtClustDB

PLN02565.

Gene expression databases

ArrayExpress

P47998.

Genevestigator

P47998.

GermOnline

AT4G14880. Arabidopsis thaliana.

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

CYSK1_ARATH

Accession

Primary (citable) accession number: P47998
Secondary accession number(s): O23343 , Q1EC56, Q42570, Q94AS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program