Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A2BIU4

- MTAP_HYPBU

UniProt

A2BIU4 - MTAP_HYPBU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

mtnP

Organism
Hyperthermus butylicus (strain DSM 5456 / JCM 9403)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201PhosphateUniRule annotation
Sitei175 – 1751Important for substrate specificityUniRule annotation
Binding sitei194 – 1941Substrate; via amide nitrogenUniRule annotation
Binding sitei195 – 1951PhosphateUniRule annotation
Sitei229 – 2291Important for substrate specificityUniRule annotation

GO - Molecular functioni

  1. phosphorylase activity Source: InterPro
  2. S-methyl-5-thioadenosine phosphorylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. L-methionine biosynthetic process from methylthioadenosine Source: UniProtKB-HAMAP
  2. purine ribonucleoside salvage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

BioCyciHBUT415426:GC56-22-MONOMER.
UniPathwayiUPA00904; UER00873.

Names & Taxonomyi

Protein namesi
Recommended name:
S-methyl-5'-thioadenosine phosphorylaseUniRule annotation (EC:2.4.2.28UniRule annotation)
Alternative name(s):
5'-methylthioadenosine phosphorylaseUniRule annotation
Short name:
MTA phosphorylaseUniRule annotation
Short name:
MTAPUniRule annotation
Gene namesi
Name:mtnPUniRule annotation
Ordered Locus Names:Hbut_0022
OrganismiHyperthermus butylicus (strain DSM 5456 / JCM 9403)
Taxonomic identifieri415426 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus
ProteomesiUP000002593: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 274274S-methyl-5'-thioadenosine phosphorylasePRO_0000415104Add
BLAST

Interactioni

Subunit structurei

Homohexamer. Dimer of a homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi415426.Hbut_0022.

Structurei

3D structure databases

ProteinModelPortaliA2BIU4.
SMRiA2BIU4. Positions 7-274.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni62 – 632Phosphate bindingUniRule annotation
Regioni95 – 962Phosphate bindingUniRule annotation
Regioni218 – 2203Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0005.
HOGENOMiHOG000228987.
KOiK00772.
OMAiCEAQLCY.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01694. MTAP. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2BIU4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPDFPPKPSV KADIAIIGGS GLYDPGVLEN AKEYKIYTPY GEPSDYIIVG
60 70 80 90 100
ELGGKRVAFL PRHGRGHRIP PHKINYRANI WALKMLGVKW VIAVSAVGSL
110 120 130 140 150
REDYKPGDIV VPDQFIDMTK SRVYTFFDEG IVAHVSMADP FCEHLRQEII
160 170 180 190 200
STARELGYRV HPRGTYICIE GPRFSTRAES RVWREVFKAD IIGMTLVPEV
210 220 230 240 250
NLACEAQLCY ATIALVTDYD VWAERPVTAE EVARVMKENT EKAKKILYKL
260 270
IPRLPPEPDK ARCSCCSSLE TALL
Length:274
Mass (Da):30,784
Last modified:February 20, 2007 - v1
Checksum:i305ED09C45DDCE01
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000493 Genomic DNA. Translation: ABM79900.1.
RefSeqiYP_001012245.1. NC_008818.1.

Genome annotation databases

EnsemblBacteriaiABM79900; ABM79900; Hbut_0022.
GeneIDi4782054.
KEGGihbu:Hbut_0022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000493 Genomic DNA. Translation: ABM79900.1 .
RefSeqi YP_001012245.1. NC_008818.1.

3D structure databases

ProteinModelPortali A2BIU4.
SMRi A2BIU4. Positions 7-274.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 415426.Hbut_0022.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM79900 ; ABM79900 ; Hbut_0022 .
GeneIDi 4782054.
KEGGi hbu:Hbut_0022.

Phylogenomic databases

eggNOGi COG0005.
HOGENOMi HOG000228987.
KOi K00772.
OMAi CEAQLCY.

Enzyme and pathway databases

UniPathwayi UPA00904 ; UER00873 .
BioCyci HBUT415426:GC56-22-MONOMER.

Family and domain databases

Gene3Di 3.40.50.1580. 1 hit.
HAMAPi MF_01963. MTAP.
InterProi IPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view ]
PANTHERi PTHR11904. PTHR11904. 1 hit.
Pfami PF01048. PNP_UDP_1. 1 hit.
[Graphical view ]
SUPFAMi SSF53167. SSF53167. 1 hit.
TIGRFAMsi TIGR01694. MTAP. 1 hit.
PROSITEi PS01240. PNP_MTAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
    Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
    Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 5456 / JCM 9403.

Entry informationi

Entry nameiMTAP_HYPBU
AccessioniPrimary (citable) accession number: A2BIU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: February 20, 2007
Last modified: October 29, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3