Reviewed, UniProtKB/Swiss-Prot Q6FAL8 (MSRB_ACIAD)

Names and origin

Protein names

Recommended name:
    Peptide methionine sulfoxide reductase msrB
    EC=1.8.4.12
Alternative name(s):
    Peptide-methionine (R)-S-oxide reductase

Gene names

Name:	msrB
Ordered Locus Names:	ACIAD2086

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	139 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin. HAMAP MF_01400
Cofactor	Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein By similarity.
Sequence similarities	Belongs to the msrB Met sulfoxide reductase family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	peptide-methionine (R)-S-oxide reductase activity Inferred from electronic annotation. Source: EC peptide-methionine-(S)-S-oxide reductase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding 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 – 139	139	Peptide methionine sulfoxide reductase msrB HAMAP MF_01400		PRO_1000068261
Sites
	Active site	119	1	Nucleophile By similarity
	Metal binding	47	1	Zinc By similarity
	Metal binding	50	1	Zinc By similarity
	Metal binding	96	1	Zinc By similarity
	Metal binding	99	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FAL8-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 781AE7B9E2068C3F	FASTA	139	15,964
	10 20 30 40 50 60 MGKLNKTERE WQRELSPEEY RITRQKGTEP AFTGQYWNTK QSGTYVCRCC GTELFSSISK 70 80 90 100 110 120 YDSGCGWPSF YKPINTTAIE EHDDFSHGMV RTEIVCHHCD AHLGHVFEDG PQPTGLRYCV 130 NSASLQLKTD EKNDEETYP

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR543861 Genomic DNA. Translation: CAG68895.1.
RefSeq	YP_046717.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2879149.
GenomeReviews	Gene locus ACIAD2086 in contig CR543861_GR.
KEGG	aci:ACIAD2086.
NMPDR	fig|62977.3.peg.1979.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6FAL8.
OMA	Q6FAL8. FTGRYWD.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD2086-MON.
Family and domain databases
HAMAP	MF_01400. [Tree]
InterPro	IPR002579. Methionine_sulphoxide_MsrB. [Graphical view]
Gene3D	G3DSA:2.170.150.20. MsrB. 1 hit.
Pfam	PF01641. SelR. 1 hit. [Graphical view]
ProDom	PD004057. DUF25. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00357. MsrB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MSRB_ACIAD

Accession

Primary (citable) accession number: Q6FAL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)