SubmitCancel

Skip Header

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

Q7RZA5

- MTAP_NEUCR

UniProt

Q7RZA5 - MTAP_NEUCR

(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
NCU03963, NCU03963.1
Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
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 By similarity.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 – 201Phosphate By similarity
Sitei179 – 1791Important for substrate specificity By similarity
Binding sitei197 – 1971Substrate; via amide nitrogen By similarity
Binding sitei198 – 1981Phosphate By similarity
Sitei235 – 2351Important for substrate specificity By similarity

GO - Molecular functioni

  1. mRNA binding Source: EnsemblFungi
  2. phosphorylase activity Source: InterPro
  3. S-methyl-5-thioadenosine phosphorylase activity Source: UniProtKB-HAMAP

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

UniPathwayiUPA00904; UER00873.

Names & Taxonomyi

Protein namesi
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
Short name:
MTAPase
Gene namesi
ORF Names:NCU03963, NCU03963.1
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 5, Linkage Group VI

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310S-methyl-5'-thioadenosine phosphorylaseUniRule annotationPRO_0000415131Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi5141.NCU03963.1.

Structurei

3D structure databases

ProteinModelPortaliQ7RZA5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni62 – 632Phosphate binding By similarity
Regioni95 – 962Phosphate binding By similarity
Regioni221 – 2233Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0005.
HOGENOMiHOG000228986.
KOiK00772.
OMAiCEAQLCY.
OrthoDBiEOG77DJGM.

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.

Q7RZA5-1 [UniParc]FASTAAdd to Basket

« Hide

MENLPTTYDG PVHIAVIGGT GLSKLEGYVP VAALNPTTPW GSPSSPLMIF    50
EHNGHAVAFL ARHGLYHQLA PHEVPARANI AALRSIGVRT IIAFSAVGSL 100
REEIKPMDFV IPDQIIDRTK GIRPFTFYEG GVVGHVGFAD PFDAGLAQVV 150
EKCASAMKGD GVVLHNKGTI ICMEGPAFST RAESHMYRSW GGSVINMSAL 200
PEAKLAREAE LAYQMICMAT DYDCWRDEAG EDVDVAMVMK YMAANGENAK 250
HLVGAVLDEL LKQDNSDLVL AKKWQGSAQG AVKFMTKPEG RDPEAMKRVE 300
FLFPGFWEQN 310
Length:310
Mass (Da):33,720
Last modified:December 15, 2003 - v1
Checksum:iB041C35866DF28D0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CM002241 Genomic DNA. Translation: EAA28366.1.
RefSeqiXP_957602.1. XM_952509.2.
UniGeneiNcr.19060.

Genome annotation databases

EnsemblFungiiEFNCRT00000003734; EFNCRP00000003734; EFNCRG00000003730.
GeneIDi3873724.
KEGGincr:NCU03963.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CM002241 Genomic DNA. Translation: EAA28366.1 .
RefSeqi XP_957602.1. XM_952509.2.
UniGenei Ncr.19060.

3D structure databases

ProteinModelPortali Q7RZA5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5141.NCU03963.1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EFNCRT00000003734 ; EFNCRP00000003734 ; EFNCRG00000003730 .
GeneIDi 3873724.
KEGGi ncr:NCU03963.

Phylogenomic databases

eggNOGi COG0005.
HOGENOMi HOG000228986.
KOi K00772.
OMAi CEAQLCY.
OrthoDBi EOG77DJGM.

Enzyme and pathway databases

UniPathwayi UPA00904 ; UER00873 .

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 sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiMTAP_NEUCR
AccessioniPrimary (citable) accession number: Q7RZA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: December 15, 2003
Last modified: June 11, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

Similar proteinsi