Reviewed, UniProtKB/Swiss-Prot Q43725 (CYSKM_ARATH)

Names and origin

Protein names

Recommended name:
    Cysteine synthase, mitochondrial
    EC=2.5.1.47
Alternative name(s):
    O-acetylserine sulfhydrylase
    CSase C
      Short name=CS-C
      Short name=AtCS-C
    O-acetylserine (thiol)-lyase
    OAS-TL C

Gene names

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

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › 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. Ref.5
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	Complete proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro pollen tube development Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast Inferred from direct assay. Source: TAIR mitochondrion Ref.4 Ref.5 Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from direct assay. Source: TAIR cysteine synthase activity Ref.4 Inferred from direct assay. Source: TAIR pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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.4
	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

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: 10319184] [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: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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.
[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 [MRNA] OF 43-430. Strain: cv. Columbia.
[5]	"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: 14671022] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X81973 mRNA. Translation: CAA57498.1. Frameshift. AL138647 Genomic DNA. Translation: CAB75795.1. Sequence problems. AY099721 mRNA. Translation: AAM20572.1. AY128885 mRNA. Translation: AAM91285.1. AJ271727 mRNA. Translation: CAB71290.1.
IPI	IPI00530032.
PIR	T47800. T52650.
RefSeq	NP_191535.2.
UniGene	At.25336
3D structure databases
HSSP	HSSP built from PDB template 1OAS based on UniProtKB P12674.
SMR	Q43725. Positions 113-429.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q43725. 3 interactions.
STRING	Q43725.
Proteomic databases
PRIDE	Q43725.
Genome annotation databases
GeneID	825145.
GenomeReviews	Gene locus AT3G59760 in contig BA000014_GR.
KEGG	ath:AT3G59760.
NMPDR	fig|3702.1.peg.17330.
Organism-specific databases
TAIR	At3g59760.
Enzyme and pathway databases
BRENDA	2.5.1.47. 302.
Gene expression databases
ArrayExpress	Q43725.
Genevestigator	Q43725.
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

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:	November 3, 2009
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)