Q89VT5 (MTAP_BRADU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-methyl-5'-thioadenosine phosphorylase
EC=2.4.2.28

Alternative name(s):
5'-methylthioadenosine phosphorylase
Short name=MTA phosphorylase
Short name=MTAP

Gene names

Name:	mtnP
Ordered Locus Names:	blr0960

Organism

Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]

Taxonomic identifier

224911 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium › Bradyrhizobium diazoefficiens

Protein attributes

Sequence length	291 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates By similarity. HAMAP-Rule MF_01963
Catalytic activity	S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_01963
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route): step 1/1. HAMAP-Rule MF_01963
Subunit structure	Homohexamer. Dimer of a homotrimer By similarity. HAMAP-Rule MF_01963
Sequence similarities	Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.

Ontologies

Keywords
Biological process	Purine salvage
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-methionine salvage from methylthioadenosine Inferred from electronic annotation. Source: UniProtKB-HAMAP purine ribonucleoside salvage Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	S-methyl-5-thioadenosine phosphorylase activity Inferred from electronic annotation. Source: UniProtKB-HAMAP phosphorylase activity 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 – 291	291	S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963		PRO_0000415090
Regions
	Region	54 – 55	2	Phosphate binding By similarity
	Region	87 – 88	2	Phosphate binding By similarity
	Region	209 – 211	3	Substrate binding By similarity
Sites
	Binding site	12	1	Phosphate By similarity
	Binding site	185	1	Substrate; via amide nitrogen By similarity
	Binding site	186	1	Phosphate By similarity
	Site	167	1	Important for substrate specificity By similarity
	Site	222	1	Important for substrate specificity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89VT5 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 4C5769311BFC605E	FASTA	291	31,461
	10 20 30 40 50 60 MTQAVLGIIG GSGIYDLPGL EGAHEEVIKS PWGEPSAPLR RGTIAGLPIV FLPRHDKGHR 70 80 90 100 110 120 LSPSDINYRA NIDVLKRAGV TDLISLSACG SFKEEMPPGT FVLVDQFVDR THKRESSFFG 130 140 150 160 170 180 RGCVAHVSMA HPVSPRLRIH LAAAAEAEGI AIARGGTYVC MEGPQFSTYA ESMTYKTSGY 190 200 210 220 230 240 SVIGMTNMPE AKLAREAEIC YATVAMVTDF DCWHPDHDAV TVQDIIRVLT SNADKAKALV 250 260 270 280 290 ARLAKDFPRE HEPCPIGSDR ALDTALITAP EARDPELLKK LDAVAGRVLR G

References

[1]

"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110." Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S. DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000040 Genomic DNA. Translation: BAC46225.1.
RefSeq	NP_767600.1. NC_004463.1.
3D structure databases
ProteinModelPortal	Q89VT5.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	224911.blr0960.
Proteomic databases
PRIDE	Q89VT5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAC46225; BAC46225; BAC46225.
GeneID	1048928.
KEGG	bja:blr0960.
PATRIC	21185422. VBIBraJap65052_0982.
Phylogenomic databases
HOGENOM	HOG000228986.
KO	K00772.
OMA	MTNHTEA.
OrthoDB	EOG6KHFXC.
ProtClustDB	PRK08931.
Enzyme and pathway databases
BioCyc	BJAP224911:GJEJ-969-MONOMER.
UniPathway	UPA00904; UER00873.
Family and domain databases
Gene3D	3.40.50.1580. 1 hit.
HAMAP	MF_01963. MTAP.
InterPro	IPR010044. MTAP. IPR000845. Nucleoside_phosphorylase_d. IPR001369. PNP/MTAP. [Graphical view]
PANTHER	PTHR11904. PTHR11904. 1 hit.
Pfam	PF01048. PNP_UDP_1. 1 hit. [Graphical view]
SUPFAM	SSF53167. SSF53167. 1 hit.
TIGRFAMs	TIGR01694. MTAP. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTAP_BRADU

Accession

Primary (citable) accession number: Q89VT5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 25, 2012
Last sequence update:	June 1, 2003
Last modified:	April 16, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program