P37887 (CYSK_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cysteine synthase
Short name=CSase
EC=2.5.1.47

Alternative name(s):
O-acetylserine (thiol)-lyase
Short name=OAS-TL
Superoxide-inducible protein 11
Short name=SOI11

Gene names

Name:	cysK
Ordered Locus Names:	BSU00730

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	308 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	Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression. Ref.7
Catalytic activity	O(3)-acetyl-L-serine + H2S = L-cysteine + acetate. Ref.6
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
Subunit structure	Homodimer. Forms CymR2:CysK2 or CymR4:CysK4 complexes in the absence of O-acetylserine. Ref.7
Induction	Highly expressed in the presence of methionine, but poorly expressed in the presence of cystine. Also induced by superoxide. Repressed both by sulfate and cysteine. Ref.5 Ref.7
Disruption phenotype	Grows very slowly with sulfate, butanesulfonate or cystine as sole sulfur source. Ref.5 Ref.6
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	Complete proteome Direct protein sequencing Reference proteome
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.3 Ref.4
	Chain	2 – 308	307	Cysteine synthase		PRO_0000167081
Regions
	Region	179 – 183	5	Pyridoxal phosphate binding By similarity
Sites
	Binding site	75	1	Pyridoxal phosphate By similarity
	Binding site	267	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	45	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37887 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 79350923DF2B73CA	FASTA	308	32,820
	10 20 30 40 50 60 MVRVANSITE LIGNTPIVKL NRLADENSAD VYLKLEYMNP GSSVKDRIGL AMIEAAEKEG 70 80 90 100 110 120 KLKAGNTIIE PTSGNTGIGL AMVAAAKGLK AILVMPDTMS MERRNLLRAY GAELVLTPGA 130 140 150 160 170 180 EGMKGAIKKA EELAEKHGYF VPQQFNNPSN PEIHRQTTGK EIVEQFGDDQ LDAFVAGIGT 190 200 210 220 230 240 GGTITGAGEV LKEAYPSIKI YAVEPSDSPV LSGGKPGPHK IQGIGAGFVP DILNTEVYDE 250 260 270 280 290 300 IFPVKNEEAF EYARRAAREE GILGGISSGA AIYAALQVAK KLGKGKKVLA IIPSNGERYL STPLYQFD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Cold shock stress-induced proteins in Bacillus subtilis." Graumann P., Schroeder K., Schmid R., Marahiel M.A. J. Bacteriol. 178:4611-4619(1996) [PubMed: 8755892] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14. Strain: 168 / JH642.
[4]	"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis." Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M. Electrophoresis 18:1451-1463(1997) [PubMed: 9298659] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14. Strain: 168 / IS58.
[5]	"Functional analysis of the Bacillus subtilis cysK and cysJI genes." van der Ploeg J.R., Barone M., Leisinger T. FEMS Microbiol. Lett. 201:29-35(2001) [PubMed: 11445163] [Abstract] Cited for: DETERMINATION OF THE TRANSCRIPTIONAL START SITE, DISRUPTION PHENOTYPE, INDUCTION. Strain: 168 / BGSC1A1.
[6]	"Conversion of methionine to cysteine in Bacillus subtilis and its regulation." Hullo M.-F., Auger S., Soutourina O., Barzu O., Yvon M., Danchin A., Martin-Verstraete I. J. Bacteriol. 189:187-197(2007) [PubMed: 17056751] [Abstract] Cited for: CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. Strain: 168.
[7]	"The CymR regulator in complex with the enzyme CysK controls cysteine metabolism in Bacillus subtilis." Tanous C., Soutourina O., Raynal B., Hullo M.-F., Mervelet P., Gilles A.-M., Noirot P., Danchin A., England P., Martin-Verstraete I. J. Biol. Chem. 283:35551-35560(2008) [PubMed: 18974048] [Abstract] Cited for: FUNCTION AS A REGULATOR OF CYMR ACTIVITY, INDUCTION, SUBUNIT, INTERACTION WITH CYMR. Strain: 168.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D26185 Genomic DNA. Translation: BAA05308.1. AL009126 Genomic DNA. Translation: CAB11849.1.
PIR	S66103.
RefSeq	NP_387954.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P37887.
SMR	P37887. Positions 1-308.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000001165; EBBACP00000001165; EBBACG00000001163.
GeneID	936636.
GenomeReviews	Gene locus BSU00730 in contig AL009126_GR.
KEGG	bsu:BSU00730.
NMPDR	fig|224308.1.peg.73.
PATRIC	18971621. VBIBacSub10457_0074.
Organism-specific databases
GenoList	BSU00730. [Micado]
Phylogenomic databases
GeneTree	EBGT00070000031817.
HOGENOM	HBG748215.
OMA	TALYEFD.
PhylomeDB	P37887.
ProtClustDB	CLSK886569.
Enzyme and pathway databases
BioCyc	BSUB:BSU00730-MONOMER.
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

CYSK_BACSU

Accession

Primary (citable) accession number: P37887

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program