Q43725 (CYSKM_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cysteine synthase, mitochondrial
EC=2.5.1.47

Alternative name(s):
CSase C
Short name=AtCS-C
Short name=CS-C
O-acetylserine (thiol)-lyase
O-acetylserine sulfhydrylase
OAS-TL C

Gene names

Name:	OASC
Synonyms:	ACS 1
Ordered Locus Names:	At3g59760
ORF Names:	F24G16.30

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	430 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.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the cysteine synthase/cystathionine beta-synthase family.
Sequence caution	The sequence CAA57498.1 differs from that shown. Reason: Frameshift at positions 5, 424 and 426. The sequence CAB75795.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cysteine synthase activity Inferred from electronic annotation. Source: EC transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SAT3	Q39218	4	EBI-1633616,EBI-1633440

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q43725-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion Potential

Chain

? – 430

Cysteine synthase, mitochondrial

PRO_0000006353

Regions

Region

289 – 293

5

Pyridoxal phosphate binding By similarity

Compositional bias

49 – 54

6

Poly-Ser

Compositional bias

380 – 385

6

Poly-Ala

Sites

Binding site

185

1

Pyridoxal phosphate By similarity

Binding site

377

1

Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue

154

1

N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict

49

1

Missing in CAA57498. Ref.1

Sequence conflict

49

1

Missing in CAB71290. Ref.5

Sequence conflict

73

1

A → G in CAA57498. Ref.1

Sequence conflict

195

1

Missing Ref.1

Sequence conflict

314

1

E → R in CAA57498. Ref.1

Sequence conflict

356 – 357

2

SE → ISKL in CAA57498. Ref.1

Sequence conflict

385

1

Missing in CAA57498. Ref.1

Sequence conflict

409

1

Missing in CAA57498. Ref.1

Secondary structure

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430

Helix Strand Turn

Details...

Beta strand

114 – 116

3

Helix

117 – 120

4

Beta strand

126 – 128

3

Helix

131 – 133

3

Beta strand

137 – 144

8

Helix

145 – 147

3

Helix

155 – 167

13

Turn

173 – 175

3

Beta strand

177 – 181

5

Helix

185 – 197

13

Beta strand

200 – 206

7

Helix

211 – 219

9

Beta strand

223 – 227

5

Helix

229 – 231

3

Helix

232 – 246

15

Beta strand

250 – 252

3

Turn

255 – 257

3

Helix

260 – 267

8

Helix

269 – 276

8

Beta strand

281 – 287

7

Beta strand

289 – 291

3

Helix

292 – 304

13

Beta strand

308 – 315

8

Helix

316 – 318

3

Helix

320 – 322

3

Turn

345 – 347

3

Beta strand

349 – 354

6

Helix

356 – 370

15

Helix

376 – 388

13

Helix

392 – 394

3

Beta strand

398 – 403

6

Helix

407 – 410

4

Helix

414 – 422

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 16, 2004. Version 3. Checksum: 9DDEB1B8E314E143	FASTA	430	45,815
	10 20 30 40 50 60 MVAMIMASRF NREAKLASQI LSTLLGNRSC YTSMAATSSS ALLLNPLTSS SSSSTLRRFR 70 80 90 100 110 120 CSPEISSLSF SSASDFSLAM KRQSRSFADG SERDPSVVCE AVKRETGPDG LNIADNVSQL 130 140 150 160 170 180 IGKTPMVYLN SIAKGCVANI AAKLEIMEPC CSVKDRIGYS MVTDAEQKGF ISPGKSVLVE 190 200 210 220 230 240 PTSGNTGIGL AFIAASRGYR LILTMPASMS MERRVLLKAF GAELVLTDPA KGMTGAVQKA 250 260 270 280 290 300 EEILKNTPDA YMLQQFDNPA NPKIHYETTG PEIWDDTKGK VDIFVAGIGT GGTITGVGRF 310 320 330 340 350 360 IKEKNPKTQV IGVEPTESDI LSGGKPGPHK IQGIGAGFIP KNLDQKIMDE VIAISSEEAI 370 380 390 400 410 420 ETAKQLALKE GLMVGISSGA AAAAAIKVAK RPENAGKLIA VVFPSFGERY LSTPLFQSIR 430 EEVEKMQPEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine(thiol)lyase) from Arabidopsis thaliana." Hesse H., Lipke J., Altmann T., Hofgen R. Amino Acids 16:113-131(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Flower.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-430. Strain: cv. Columbia.
[6]	"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins." Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Strain: cv. Landsberg erecta.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X81973 mRNA. Translation: CAA57498.1. Frameshift.
AL138647 Genomic DNA. Translation: CAB75795.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79963.1.
AY099721 mRNA. Translation: AAM20572.1.
AY128885 mRNA. Translation: AAM91285.1.
AJ271727 mRNA. Translation: CAB71290.1.

IPI

IPI00530032.

PIR

T47800.
T52650.

RefSeq

NP_191535.2. NM_115838.5.

UniGene

At.25336.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4AEC	X-ray	2.40	A/B	1-430	[»]

ProteinModelPortal

Q43725.

SMR

Q43725. Positions 102-423.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40500N.

IntAct

Q43725. 3 interactions.

Proteomic databases

PaxDb

Q43725.

PRIDE

Q43725.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT3G59760.3; AT3G59760.3; AT3G59760.

GeneID

825145.

KEGG

ath:AT3G59760.

Organism-specific databases

TAIR

At3g59760.

Phylogenomic databases

eggNOG

COG0031.

HOGENOM

HOG000217394.

InParanoid

Q43725.

KO

K01738.

PhylomeDB

Q43725.

ProtClustDB

PLN03013.

Enzyme and pathway databases

BioCyc

MetaCyc:AT3G59760-MONOMER.

UniPathway

UPA00136; UER00200.

Gene expression databases

ArrayExpress

Q43725.

Genevestigator

Q43725.

Family and domain databases

InterPro

IPR001216. Cys_synth_BS.
IPR005856. Cys_synthKM.
IPR005859. CysK.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]

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

CYSKM_ARATH

Accession

Primary (citable) accession number: Q43725
Secondary accession number(s): Q8L4A2, Q9M1Z8, Q9M440

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 16, 2004
Last modified:	May 1, 2013
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program