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Protein

AMP deaminase 1

Gene

Ampd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

AMP deaminase plays a critical role in energy metabolism.

Catalytic activityi

AMP + H2O = IMP + NH3.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathway:iIMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from AMP.
Proteins known to be involved in this subpathway in this organism are:
  1. AMP deaminase 1 (Ampd1), AMP deaminase 3 (Ampd3), AMP deaminase 2 (Ampd2)
This subpathway is part of the pathway IMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from AMP, the pathway IMP biosynthesis via salvage pathway and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi301 – 3011Zinc; catalyticBy similarity
Metal bindingi303 – 3031Zinc; catalyticBy similarity
Binding sitei303 – 3031SubstrateBy similarity
Metal bindingi570 – 5701Zinc; catalyticBy similarity
Binding sitei573 – 5731SubstrateBy similarity
Active sitei592 – 5921Proton acceptorPROSITE-ProRule annotation
Metal bindingi647 – 6471Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_345398. Purine salvage.
UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase 1 (EC:3.5.4.6)
Alternative name(s):
AMP deaminase isoform M
Myoadenylate deaminase
Gene namesi
Name:Ampd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:88015. Ampd1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 745745AMP deaminase 1PRO_0000269718Add
BLAST

Proteomic databases

MaxQBiQ3V1D3.
PaxDbiQ3V1D3.
PRIDEiQ3V1D3.

PTM databases

PhosphoSiteiQ3V1D3.

Expressioni

Gene expression databases

CleanExiMM_AMPD1.
ExpressionAtlasiQ3V1D3. baseline and differential.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ3V1D3. 1 interaction.
STRINGi10090.ENSMUSP00000088217.

Structurei

3D structure databases

ProteinModelPortaliQ3V1D3.
SMRiQ3V1D3. Positions 565-652.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni372 – 3776Substrate bindingBy similarity
Regioni648 – 6514Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiQ3V1D3.
KOiK01490.
OMAiYVYPNEA.
OrthoDBiEOG70ZZMQ.
TreeFamiTF300439.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029770. AMPD1.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF1. PTHR11359:SF1. 1 hit.
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3V1D3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS
60 70 80 90 100
LHEMQAHIFH MENLSMDGRR KRRFQGRKTV NLSIPQSETS STKLSHIEEF
110 120 130 140 150
ISSSPTYESV PDFQRVQITG DYASGVTVED FEVVCKGLYR ALCIREKYMQ
160 170 180 190 200
KSFQRFPKTP SKYLRNIDGE ALVGNESFYP VFTPPPKKGE DPFRTEDLPA
210 220 230 240 250
NLGYHLKMKA GVIYIYPDEA AANRDEPKPY PYPNLDDFLD DMNFLLALIA
260 270 280 290 300
QGPVKTYAHR RLKFLSSKFQ VHQMLNEMDE LKELKNNPHR DFYNCRKVDT
310 320 330 340 350
HIHAAACMNQ KHLLRFIKKS YHIDADRVVY STKEKSLTLK ELFAKLNMHP
360 370 380 390 400
YDLTVDSLDV HAGRQTFQRF DKFNDKYNPV GASELRDLYL KTDNYINGEY
410 420 430 440 450
FATIIKEVGA DLVEAKYQHA EPRLSIYGRS PDEWNKLSSW FVCNRIYCPN
460 470 480 490 500
MTWMIQVPRI YDVFRSKNFL PHFGKMLENI FLPVFEATIN PQAHPDLSVF
510 520 530 540 550
LKHITGFDSV DDESKHSGHM FSSKSPKPEE WTMENNPSYT YYAYYMYANI
560 570 580 590 600
TVLNSLRKER GMNTFLFRPH CGEAGALTHL MTAFMIADNI SHGLNLKKSP
610 620 630 640 650
VLQYLFFLAQ IPIAMSPLSN NSLFLEYAKN PFLDFLQKGL MISLSTDDPM
660 670 680 690 700
QFHFTKEPLM EEYAIAAQVF KLSTCDMCEV ARNSVLQCGI SHEEKAKFLG
710 720 730 740
NNYLEEGPVG NDIRRTNVAQ IRMAYRYETW CYELNLIAEG LKATE
Length:745
Mass (Da):86,105
Last modified:September 18, 2013 - v2
Checksum:i4595A57908A13239
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti226 – 2261E → D in BAE21218 (PubMed:16141072).Curated
Sequence conflicti534 – 5341E → G in BAE21218 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK132524 mRNA. Translation: BAE21218.1.
AC150894 Genomic DNA. No translation available.
AC163297 Genomic DNA. No translation available.
CCDSiCCDS38571.1.
RefSeqiNP_001028475.2. NM_001033303.2.
UniGeneiMm.331272.

Genome annotation databases

EnsembliENSMUST00000090715; ENSMUSP00000088217; ENSMUSG00000070385.
GeneIDi229665.
KEGGimmu:229665.
UCSCiuc008qso.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK132524 mRNA. Translation: BAE21218.1.
AC150894 Genomic DNA. No translation available.
AC163297 Genomic DNA. No translation available.
CCDSiCCDS38571.1.
RefSeqiNP_001028475.2. NM_001033303.2.
UniGeneiMm.331272.

3D structure databases

ProteinModelPortaliQ3V1D3.
SMRiQ3V1D3. Positions 565-652.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ3V1D3. 1 interaction.
STRINGi10090.ENSMUSP00000088217.

PTM databases

PhosphoSiteiQ3V1D3.

Proteomic databases

MaxQBiQ3V1D3.
PaxDbiQ3V1D3.
PRIDEiQ3V1D3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090715; ENSMUSP00000088217; ENSMUSG00000070385.
GeneIDi229665.
KEGGimmu:229665.
UCSCiuc008qso.1. mouse.

Organism-specific databases

CTDi270.
MGIiMGI:88015. Ampd1.

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiQ3V1D3.
KOiK01490.
OMAiYVYPNEA.
OrthoDBiEOG70ZZMQ.
TreeFamiTF300439.

Enzyme and pathway databases

UniPathwayiUPA00591; UER00663.
ReactomeiREACT_345398. Purine salvage.

Miscellaneous databases

NextBioi379583.
PROiQ3V1D3.
SOURCEiSearch...

Gene expression databases

CleanExiMM_AMPD1.
ExpressionAtlasiQ3V1D3. baseline and differential.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029770. AMPD1.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF1. PTHR11359:SF1. 1 hit.
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiAMPD1_MOUSE
AccessioniPrimary (citable) accession number: Q3V1D3
Secondary accession number(s): F8VPY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: September 18, 2013
Last modified: July 22, 2015
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.