AMPD_SCHPO
ID AMPD_SCHPO Reviewed; 831 AA.
AC P50998; Q9URV7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=AMP deaminase;
DE EC=3.5.4.6;
DE AltName: Full=Myoadenylate deaminase;
GN Name=ada1; ORFNames=SPBC106.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RA Rochet M., Levesque H., Gaillardin C.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [4]
RP CATALYTIC ACTIVITY.
RX PubMed=8440738; DOI=10.1016/s0021-9258(18)53645-0;
RA Sollitti P., Merkler D.J., Estupinan B., Schramm V.L.;
RT "Yeast AMP deaminase. Catalytic activity in Schizosaccharomyces pombe and
RT chromosomal location in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 268:4549-4555(1993).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-84; SER-758; SER-776;
RP SER-780 AND SER-782, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: AMP deaminase plays a critical role in energy metabolism.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6;
CC Evidence={ECO:0000269|PubMed:8440738};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from AMP: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
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DR EMBL; X91498; CAA62797.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CU329671; CAB53720.2; -; Genomic_DNA.
DR PIR; T39261; T39261.
DR RefSeq; NP_595153.2; NM_001021062.2.
DR AlphaFoldDB; P50998; -.
DR SMR; P50998; -.
DR BioGRID; 276642; 76.
DR STRING; 4896.SPBC106.04.1; -.
DR iPTMnet; P50998; -.
DR MaxQB; P50998; -.
DR PaxDb; P50998; -.
DR PRIDE; P50998; -.
DR EnsemblFungi; SPBC106.04.1; SPBC106.04.1:pep; SPBC106.04.
DR GeneID; 2540105; -.
DR KEGG; spo:SPBC106.04; -.
DR PomBase; SPBC106.04; ada1.
DR VEuPathDB; FungiDB:SPBC106.04; -.
DR eggNOG; KOG1096; Eukaryota.
DR HOGENOM; CLU_003782_2_2_1; -.
DR InParanoid; P50998; -.
DR OMA; WLYFMFA; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-74217; Purine salvage.
DR UniPathway; UPA00591; UER00663.
DR PRO; PR:P50998; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0003876; F:AMP deaminase activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central.
DR GO; GO:0006188; P:IMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd01319; AMPD; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleotide metabolism; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..831
FT /note="AMP deaminase"
FT /id="PRO_0000194413"
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 609
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 390..395
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 590
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 665..668
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 468..505
FT /note="NVRWLIQVPRLYDVYKKSGIVETFEEVVRNVFEPLFEV -> TFVGLFKYLV
FT CMMCIRSPVLLRLLKRSSEMSLNHCSKF (in Ref. 1; CAA62797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 831 AA; 95887 MW; F027B33C7AD0C63D CRC64;
MNMEQEDDQV PAVAAETVPL KRYVTNPGAN RDEEVAAAPS SQDTPYFDYA YERSLRHQDA
KFLAMNGTQN GRDGLPSKSP RRPSVSASTV RNSDDVNHSK AGPGSGKLLN DTLQSKISSI
HMPHVQQGDN AVVSSVGGPE TDPGNMETTD PLFSDELAEI YLSIHKCMDM RHKYIRVSLQ
GELDNPIDDD SWIIYPDCKE GEDDTGLFNF ADCKIPGIEN EMEYHMDHQG IFQVYENDSA
YIAGTPSFHI PTIRDYYIDL EFLLSASSDG PSKSFSFRRL QYLEGRWNMY MLLNEYQELA
DTKKVPHRDF YNVRKVDTHV HHSALANQKH LLRFIKAKLR KCPNEKVIWR DGKFLTLQEV
FDSLKLTSYD LSIDTLDMHA HTDTFHRFDK FNLKYNPIGE SRLRTIFLKT DNDINGRYLA
ELTKEVFTDL RTQKYQMAEY RISIYGRNRE EWDKLAAWII DNELFSPNVR WLIQVPRLYD
VYKKSGIVET FEEVVRNVFE PLFEVTKDPR THPKLHVFLQ RVIGFDSVDD ESKPERRTFR
KFPYPKHWDI NLNPPYSYWL YYMYANMTSL NSWRKIRGFN TFVLRPHCGE AGDTDHLASA
FLLSHGINHG ILLRKVPFLQ YLWYLDQIPI AMSPLSNNAL FLAYDKNPFL TYFKRGLNVS
LSTDDPLQFA FTREPLIEEY AVAAQIYKLS AVDMCELARN SVLQSGFERQ LKERWLGVDF
QDIDRTNVPI IRLAYRALTL TQEIALVNKH VQPSKHPSNH DLEELIHKYD AMTGTSDPLS
ASPRTNDATI SSRLSLHDGH DHGAFFPGLS VISERRRRKD SMASSSQDLK D
