P63874 (CYSM_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
O-phosphoserine sulfhydrylase
Short name=OPS sulfhydrylase
EC=2.5.1.65
EC=2.5.1.n5

Alternative name(s):
CysO-thiocarboxylate-dependent cysteine synthase
Cysteine synthase B
Short name=CSase B
O-phosphoserine-specific cysteine synthase

Gene names

Name:	cysM
Ordered Locus Names:	Mb1371

Organism

Mycobacterium bovis [Complete proteome] [HAMAP]

Taxonomic identifier

1765 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency By similarity.
Catalytic activity	O-phospho-L-serine + H2S = L-cysteine + phosphate. O-phospho-L-serine + [CysO]-SH = [CysO]-L-cysteine + phosphate.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis.
Subunit structure	Homodimer By similarity.
Domain	The five C-terminal amino acid residues are inserted into the active site cleft in the closed conformation, protect the aminoacrylate intermediate and are involved in sulfur donor selectivity 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	O-phosphoserine sulfhydrylase activity Inferred from electronic annotation. Source: EC cysteine synthase activity Inferred from electronic annotation. Source: InterPro pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 323	323	O-phosphoserine sulfhydrylase		PRO_0000167113
Regions
	Region	184 – 188	5	Pyridoxal phosphate binding By similarity
Sites
	Binding site	81	1	Pyridoxal phosphate By similarity
	Binding site	220	1	Substrate By similarity
	Binding site	265	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	51	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P63874 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: B743231FEFA87573	FASTA	323	34,438
	10 20 30 40 50 60 MTRYDSLLQA LGNTPLVGLQ RLSPRWDDGR DGPHVRLWAK LEDRNPTGSI KDRPAVRMIE 70 80 90 100 110 120 QAEADGLLRP GATILEPTSG NTGISLAMAA RLKGYRLICV MPENTSVERR QLLELYGAQI 130 140 150 160 170 180 IFSAAEGGSN TAVATAKELA ATNPSWVMLY QYGNPANTDS HYCGTGPELL ADLPEITHFV 190 200 210 220 230 240 AGLGTTGTLM GTGRFLREHV ANVKIVAAEP RYGEGVYALR NMDEGFVPEL YDPEILTARY 250 260 270 280 290 300 SVGAVDAVRR TRELVHTEGI FAGISTGAVL HAALGVGAGA LAAGERADIA LVVADAGWKY 310 320 LSTGAYAGSL DDAETALEGQ LWA

References

[1]

"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248338 Genomic DNA. Translation: CAD94232.1.
RefSeq	NP_855025.1. NC_002945.3.
3D structure databases
ProteinModelPortal	P63874.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000014909; EBMYCP00000014744; EBMYCG00000014906.
GeneID	1090662.
GenomeReviews	Gene locus Mb1371 in contig BX248333_GR.
KEGG	mbo:Mb1371.
PATRIC	18004709. VBIMycBov88188_1503.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000015764.
HOGENOM	HBG748215.
OMA	YSVGPRE.
ProtClustDB	CLSK871928.
Enzyme and pathway databases
BioCyc	MBOV233413:MB1371-MONOMER.
Family and domain databases
InterPro	IPR001216. Cys_synth_BS. IPR005856. Cys_synthKM. IPR001926. PyrdxlP-dep_enz_bsu. [Graphical view]
KO	K12339.
Pfam	PF00291. PALP. 1 hit. [Graphical view]
SUPFAM	SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMs	TIGR01136. CysKM. 1 hit.
PROSITE	PS00901. CYS_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSM_MYCBO

Accession

Primary (citable) accession number: P63874
Secondary accession number(s): Q10624

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program