Reviewed, UniProtKB/Swiss-Prot P45113 (MTNN_HAEIN)

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:	HI1216

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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	methionine biosynthetic process from S-adenosylmethionine Inferred from electronic annotation. Source: HAMAP methionine salvage 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 – 229	229	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684		PRO_0000164442
Regions
	Region	173 – 174	2	Substrate binding By similarity
Sites
	Active site	12	1	Proton acceptor By similarity
	Binding site	78	1	Substrate; via amide nitrogen By similarity
	Binding site	152	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	197	1	Substrate By similarity
Experimental info
	Sequence conflict	20	1	M → T in AAS91661. Ref.1
	Sequence conflict	42	1	D → N in AAS91661. Ref.1
	Sequence conflict	70	1	C → F in AAS91661. Ref.1
	Sequence conflict	202	1	K → E in AAS91661. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P45113-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 37DC08101E193EA4	FASTA	229	23,965
	10 20 30 40 50 60 MKIGIVGAMA QEVEILKNLM ADRTETRVAS AVIFEGKING KDVALLQSGI GKVAAAIGTT 70 80 90 100 110 120 ALLQLAKPDC VINTGSAGGV AKGLKVGDIV ISDETRYHDA DVTAFGYEKG QLPANPAAFL 130 140 150 160 170 180 SDKKLADLAQ EIAEKQGQSV KRGLICSGDS FINSEDKIAQ IKADFPNVTG VEMEATAIAQ 190 200 210 220 VCYAFNVPFV VVRAISDGGD GKASMSFEEF LPLAAKQSSA LVLGMIDRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a haem-utilization protein (Hup) in Haemophilus influenzae." Morton D.J., Smith A., Ren Z., Madore L.L., VanWagoner T.M., Seale T.W., Whitby P.W., Stull T.L. Microbiology 150:3923-3933(2004) [PubMed: 15583146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: E1a.
[2]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY525146 Genomic DNA. Translation: AAS91661.1. L42023 Genomic DNA. Translation: AAC22869.1.
PIR	C64169.
RefSeq	NP_439372.1.
3D structure databases
HSSP	HSSP built from PDB template 1JYS based on UniProtKB P24247.
ModBase	Search...
Genome annotation databases
GeneID	950160.
GenomeReviews	Gene locus HI1216 in contig L42023_GR.
KEGG	hin:HI1216.
NMPDR	fig|71421.1.peg.1162.
TIGR	HI1216.
Phylogenomic databases
HOGENOM	P45113.
OMA	AQVCHQF.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1216-MON.
BRENDA	3.2.2.9. 109.
Family and domain databases
HAMAP	MF_01684. [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_HAEIN

Accession

Primary (citable) accession number: P45113
Secondary accession number(s): Q5SF30

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 57 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)