O32978 (CYSK_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
O-acetylserine sulfhydrylase
Short name=OAS sulfhydrylase
Short name=OASS
EC=2.5.1.47

Alternative name(s):
Cysteine synthase A
Short name=CSase A
O-acetylserine (thiol)-lyase A
Short name=OAS-TL A
O-acetylserine-specific cysteine synthase
Sulfide-dependent cysteine synthase

Gene names

Name:	cysK
Ordered Locus Names:	ML0839
ORF Names:	MLCB22.47

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	310 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide By similarity.
Catalytic activity	O(3)-acetyl-L-serine + H2S = L-cysteine + acetate.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
Subunit structure	Homodimer By similarity.
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
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
	Chain	1 – 310	310	O-acetylserine sulfhydrylase		PRO_0000167093
Regions
	Region	178 – 182	5	Pyridoxal phosphate binding By similarity
Sites
	Binding site	74	1	Pyridoxal phosphate By similarity
	Binding site	266	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	44	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O32978 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 6D94127327ABCB36	FASTA	310	32,661
	10 20 30 40 50 60 MSIAEDVTQL VGNTPLVRLR RVTEGALADV VAKLESFNPA NSVKDRIGVA MIDTAEEAGL 70 80 90 100 110 120 IKPDTVILEP TSGNTGIALA MVCAARGYHC VLTMPETMSI ERRMLLRAYG AELILTPGAD 130 140 150 160 170 180 GMSGAIAKAE ELAKSDKRYF IPQQFENPAN PAIHAATTAE EVWRDTDGKV DIFVSGIGTG 190 200 210 220 230 240 GTITGVARII KERRPATQFV AVEPAASPVL SGGQKGPHPI QGIGAGFVPS VLVLDLVDEI 250 260 270 280 290 300 VTVGNEEALD LARRLAKEEG LLVGISAGAA VCAALHVARR PENTGKLIVV VLPDFGERYL 310 STMLFADLAN

References

[1]

"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z98741 Genomic DNA. Translation: CAB11412.1. AL583919 Genomic DNA. Translation: CAC30349.1.
PIR	T44912.
RefSeq	NP_301633.1. NC_002677.1.
3D structure databases
ProteinModelPortal	O32978.
SMR	O32978. Positions 1-306.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000028183; EBMYCP00000027789; EBMYCG00000028178.
GeneID	909810.
GenomeReviews	Gene locus ML0839 in contig AL450380_GR.
KEGG	mle:ML0839.
NMPDR	fig|272631.1.peg.505.
PATRIC	18053218. VBIMycLep78757_1554.
Organism-specific databases
Leproma	ML0839.
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000015764.
HOGENOM	HBG748215.
OMA	VVIVPSF.
ProtClustDB	CLSK799368.
Enzyme and pathway databases
BioCyc	MLEP272631:ML0839-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_MYCLE

Accession

Primary (citable) accession number: O32978

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program