Cysteine synthase, chloroplastic/chromoplastic precursor - Arabidopsis thaliana (Mouse-ear cress)

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P47999 (CYSKP_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cysteine synthase, chloroplastic/chromoplastic
EC=2.5.1.47

Alternative name(s):
At.OAS.7-4
CSase B
Short name=AtCS-B
Short name=CS-B
O-acetylserine (thiol)-lyase
O-acetylserine sulfhydrylase
OAS-TL B
cpACS1

Gene names

Name:	OASB
Ordered Locus Names:	At2g43750
ORF Names:	F18O19.14

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	392 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.
Subunit structure	Homodimer.
Subcellular location	Plastid › chloroplast stroma. Plastid › chromoplast.
Sequence similarities	Belongs to the cysteine synthase/cystathionine beta-synthase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Cellular component	Chloroplast Chromoplast Plastid
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro response to cadmium ion Inferred from expression pattern. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast envelope Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR chromoplast Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: TAIR
Molecular function	cysteine synthase activity Inferred from direct assay Ref.4. 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

Transit peptide

1 – 60

Chloroplast and chromoplast By similarity

Chain

61 – 392

332

Cysteine synthase, chloroplastic/chromoplastic

PRO_0000006349

Regions

Region

251 – 255

Pyridoxal phosphate binding By similarity

Compositional bias

342 – 347

Poly-Ala

Sites

Binding site

147

Pyridoxal phosphate By similarity

Binding site

339

Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue

116

N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict

232

G → N in CAA57344. Ref.3

Sequence conflict

288

P → T in CAA57344. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P47999 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: B1220F01E8E31A12
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FASTA

392

41,656

        10         20         30         40         50         60 
MAATSSSAFL LNPLTSRHRP FKYSPELSSL SLSSRKAAAF DVSSAAFTLK RQSRSDVVCK 

        70         80         90        100        110        120 
AVSIKPEAGV EGLNIADNAA QLIGKTPMVY LNNVVKGCVA SVAAKLEIME PCCSVKDRIG 

       130        140        150        160        170        180 
YSMITDAEEK GLITPGKSVL VESTSGNTGI GLAFIAASKG YKLILTMPAS MSLERRVLLR 

       190        200        210        220        230        240 
AFGAELVLTE PAKGMTGAIQ KAEEILKKTP NSYMLQQFDN PANPKIHYET TGPEIWEDTR 

       250        260        270        280        290        300 
GKIDILVAGI GTGGTITGVG RFIKERKPEL KVIGVEPTES AILSGGKPGP HKIQGIGAGF 

       310        320        330        340        350        360 
VPKNLDLAIV DEYIAISSEE AIETSKQLAL QEGLLVGISS GAAAAAAIQV AKRPENAGKL 

       370        380        390 
IAVVFPSFGE RYLSTQLFQS IREECEQMQP EL

« Hide

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 [MRNA].
[3]	"Molecular cloning of a cysteine synthase cDNA from Arabidopsis thaliana." Hesse H., Altmann T. Plant Physiol. 108:851-852(1995) [PubMed: 7610184] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [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 [GENOMIC DNA]. Strain: cv. Columbia.
[5]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[6]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[7]	"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. Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[8]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X80377 mRNA. Translation: CAA56594.2. X81698 mRNA. Translation: CAA57344.1. AJ271728 Genomic DNA. Translation: CAB71292.1. AC002333 Genomic DNA. Translation: AAB64031.1. CP002685 Genomic DNA. Translation: AEC10317.1. CP002685 Genomic DNA. Translation: AEC10318.1. AY065375 mRNA. Translation: AAL38816.1. AY096681 mRNA. Translation: AAM20315.1. AY086156 mRNA. Translation: AAM63361.1.
IPI	IPI00529374.
PIR	A84870. S48695.
RefSeq	NP_001189745.1. NM_001202816.1. NP_181903.1. NM_129937.3.
UniGene	At.20491. At.72689.
3D structure databases
ProteinModelPortal	P47999.
SMR	P47999. Positions 75-391.
ModBase	Search...
Protein-protein interaction databases
IntAct	P47999. 1 interaction.
STRING	P47999.
2D gel databases
SWISS-2DPAGE	P47999.
Proteomic databases
PRIDE	P47999.
ProMEX	P47999.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G43750.1; AT2G43750.1; AT2G43750. AT2G43750.2; AT2G43750.2; AT2G43750.
GeneID	818978.
GenomeReviews	Gene locus AT2G43750 in contig CT485783_GR.
KEGG	ath:AT2G43750.
Organism-specific databases
TAIR	At2g43750.
Phylogenomic databases
eggNOG	KOG1252.
HOGENOM	HBG748215.
InParanoid	P47999.
OMA	VVIVPSF.
PhylomeDB	P47999.
ProtClustDB	CLSN2912905.
Gene expression databases
ArrayExpress	P47999.
Genevestigator	P47999.
GermOnline	AT2G43750. 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

CYSKP_ARATH

Accession

Primary (citable) accession number: P47999
Secondary accession number(s): O22828, Q42568

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	December 1, 2000
Last modified:	December 14, 2011
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents