Reviewed, UniProtKB/Swiss-Prot Q1QVV7 (MTNN_CHRSD)

Names and origin

Protein names

Recommended name:
    5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
      Short name=MTA/SAH nucleosidase
      Short name=MTAN
    EC=3.2.2.9
Alternative name(s):
    5'-methylthioadenosine nucleosidase
      Short name=MTA nucleosidase
    S-adenosylhomocysteine nucleosidase
      Short name=SAH nucleosidase
      Short name=AdoHcy nucleosidase
      Short name=SRH nucleosidase

Gene names

Name:	mtnN
Ordered Locus Names:	Csal_2050

Organism

Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]

Taxonomic identifier

290398 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Halomonadaceae › Chromohalobacter

Protein attributes

Sequence length	235 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively By similarity. HAMAP MF_01684
Catalytic activity	S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine. HAMAP MF_01684 S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine. HAMAP MF_01684
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. HAMAP MF_01684
Sequence similarities	Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-methionine biosynthetic process from S-adenosylmethionine Inferred from electronic annotation. Source: HAMAP L-methionine salvage from methylthioadenosine Inferred from electronic annotation. Source: InterPro nucleoside catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	adenosylhomocysteine nucleosidase activity Inferred from electronic annotation. Source: HAMAP methylthioadenosine nucleosidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 235	235	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684		PRO_0000359285
Regions
	Region	175 – 176	2	Substrate binding By similarity
Sites
	Active site	13	1	Proton acceptor By similarity
	Binding site	79	1	Substrate; via amide nitrogen By similarity
	Binding site	199	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1QVV7-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 9EDDFC6D36158C81	FASTA	235	25,016
	10 20 30 40 50 60 MRKIAIIGAM AEEVERLASH LENRQTRQHA GSTFHSGHLH GVEVVILQSG IGKVNAAVGT 70 80 90 100 110 120 TQLLEAYQPD AVINTGSAGG FGVDLDVGDV VISSEVRHHD VDAVVFGYEY GQVPQMPAAY 130 140 150 160 170 180 APDPHLVNVA RECIEGLGEL RVAEGLICTG DIFMADKAAV DQARERFPSM LAAEMEAAAI 190 200 210 220 230 AQTCHLYGCP FVVIRALSDI AGKESDLSFQ AFIEKAATHS AMMVEAMVKR LGTAS

References

[1]

"Complete sequence of Chromohalobacter salexigens DSM 3043." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., Canovas D., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000285 Genomic DNA. Translation: ABE59401.1.
RefSeq	YP_574100.1.
3D structure databases
SMR	Q1QVV7. Positions 3-231.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1QVV7.
Genome annotation databases
GeneID	4025950.
GenomeReviews	Gene locus Csal_2050 in contig CP000285_GR.
KEGG	csa:Csal_2050.
NMPDR	fig|290398.4.peg.1649.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0775.
HOGENOM	HBG367723.
OMA	TPFVIIR.
Enzyme and pathway databases
BioCyc	CSAL290398:CSAL_2050-MONOMER.
Family and domain databases
HAMAP	MF_01684. Salvage_tnN. [Tree]
InterPro	IPR010049. MTA_SAH_Nsdase. IPR000845. Nucleoside_phosphorylase. IPR018017. Nucleoside_phosphorylase_1. [Graphical view]
PANTHER	PTHR21234. PNP_UDP. 1 hit.
Pfam	PF01048. PNP_UDP_1. 1 hit. [Graphical view]
TIGRFAMs	TIGR01704. MTA/SAH-Nsdase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTNN_CHRSD

Accession

Primary (citable) accession number: Q1QVV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	May 16, 2006
Last modified:	February 9, 2010
This is version 30 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)