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Q2FTS5 (AMPPA_METHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AMP phosphorylase

Short name=AMPpase
EC=2.4.2.-
Alternative name(s):
Nucleoside monophosphate phosphorylase
Short name=NMP phosphorylase
Gene names
Ordered Locus Names:Mhun_2262
OrganismMethanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) [Reference proteome] [HAMAP]
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

Protein attributes

Sequence length516 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO By similarity. HAMAP-Rule MF_02132

Catalytic activity

AMP + phosphate = D-ribose 1,5-bisphosphate + adenine. HAMAP-Rule MF_02132

CMP + phosphate = D-ribose 1,5-bisphosphate + cytosine. HAMAP-Rule MF_02132

UMP + phosphate = D-ribose 1,5-bisphosphate + uracile. HAMAP-Rule MF_02132

Sequence similarities

Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 516516AMP phosphorylase HAMAP-Rule MF_02132
PRO_0000314730

Regions

Nucleotide binding195 – 2006AMP By similarity

Sites

Active site2571Proton donor By similarity
Binding site1691AMP; via amide nitrogen By similarity
Binding site2041AMP; via amide nitrogen By similarity
Binding site2651AMP By similarity
Binding site2891AMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2FTS5 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: D083C5B88381B8AC

FASTA51655,655
        10         20         30         40         50         60 
MRLTVRLVDI AARGILLHHN DAKSLGVLAG DRIVISSPVT GKATVDYVET TGTLIDQGRI 

        70         80         90        100        110        120 
GVYHHTNEQL TLTENEVVEV RVADRPVSLD YIKKKMEGEK LTREDIRAIV ADIVQDTLSP 

       130        140        150        160        170        180 
SEITAFVVSS YINQLDMDEI ESLTRAMVET GDQLSFHAGP IVDKHSIGGV PGNKISLIVV 

       190        200        210        220        230        240 
PIIAASGLLI PKTSSRAITG AGGTADLMEV LAPVEFSASE VQEMTIKTGG VIVWGGATNI 

       250        260        270        280        290        300 
APADDKIIIQ EYPFKIDQIG QMIASVMAKK FAVGADVVAI DIPVGKYCKV HTIEEGKKLA 

       310        320        330        340        350        360 
RQFIDLGERL NMRVECALTY GDAPVGRAIG PKLEIKEALS VLEGSDSPRS LIQKSCVIAG 

       370        380        390        400        410        420 
IALELAGKAN RGEGANLALE ILRSGKALKK FLDIIAVQGG TPDVSSEKIT VGEHFYTVRA 

       430        440        450        460        470        480 
DSTGYVIDLN NHSLITIART AGAPADHGAG LYLHAKHGTS LSKGDPIFTI YADRKWRLEK 

       490        500        510 
AIEEARRLRP VMVEGMLIDR VPNVREWVPG RSRNLE 

« Hide

References

[1]"Complete sequence of Methanospirillum hungatei JF-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27890 / DSM 864 / NBRC 100397 / JF-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000254 Genomic DNA. Translation: ABD41967.1.
RefSeqYP_503686.1. NC_007796.1.

3D structure databases

ProteinModelPortalQ2FTS5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323259.Mhun_2262.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD41967; ABD41967; Mhun_2262.
GeneID3924224.
KEGGmhu:Mhun_2262.

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000252767.
KOK00758.
OMACHSEGFE.
ProtClustDBPRK04350.

Enzyme and pathway databases

BioCycMHUN323259:GH0L-2287-MONOMER.

Family and domain databases

Gene3D3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPMF_02132. AMP_phosphorylase.
InterProIPR017713. AMP_phosphorylase.
IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR013102. PYNP_C.
IPR000053. Pyrmidine_PPase.
IPR017872. Pyrmidine_PPase_CS.
IPR013466. Thymidine/AMP_Pase.
[Graphical view]
PANTHERPTHR10515. PTHR10515. 1 hit.
PfamPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
PIRSFPIRSF000478. TP_PyNP. 1 hit.
SMARTSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsTIGR03327. AMP_phos. 1 hit.
TIGR02645. ARCH_P_rylase. 1 hit.
PROSITEPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPPA_METHJ
AccessionPrimary (citable) accession number: Q2FTS5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 21, 2006
Last modified: February 19, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families