AMPD_YEAST
ID AMPD_YEAST Reviewed; 810 AA.
AC P15274; D6VZE0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=AMP deaminase;
DE EC=3.5.4.6 {ECO:0000269|PubMed:2690949};
DE AltName: Full=Myoadenylate deaminase;
GN Name=AMD1; Synonyms=AMD; OrderedLocusNames=YML035C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 193-197; 200-208;
RP 348-350; 491-498; 500-508; 581-583; 695-698 AND 783-786, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=2690949; DOI=10.1021/bi00448a009;
RA Meyer S.L., Kvalnes-Krick K.L., Schramm V.L.;
RT "Characterization of AMD, the AMP deaminase gene in yeast. Production of
RT amd strain, cloning, nucleotide sequence, and properties of the protein.";
RL Biochemistry 28:8734-8743(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-61 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58 AND SER-61, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58 AND SER-61, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: AMP deaminase plays a critical role in energy metabolism.
CC {ECO:0000305|PubMed:2690949}.
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:2690949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778;
CC Evidence={ECO:0000269|PubMed:2690949};
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. {ECO:0000305|PubMed:2690949}.
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P15274; P33203: PRP40; NbExp=2; IntAct=EBI-2548, EBI-701;
CC -!- MISCELLANEOUS: Present with 3910 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
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DR EMBL; M30449; AAA34420.1; -; Genomic_DNA.
DR EMBL; Z46659; CAA86620.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09864.1; -; Genomic_DNA.
DR PIR; S49744; S49744.
DR RefSeq; NP_013677.1; NM_001182392.1.
DR AlphaFoldDB; P15274; -.
DR SMR; P15274; -.
DR BioGRID; 35135; 233.
DR DIP; DIP-1949N; -.
DR IntAct; P15274; 11.
DR MINT; P15274; -.
DR STRING; 4932.YML035C; -.
DR iPTMnet; P15274; -.
DR MaxQB; P15274; -.
DR PaxDb; P15274; -.
DR PRIDE; P15274; -.
DR EnsemblFungi; YML035C_mRNA; YML035C; YML035C.
DR GeneID; 854973; -.
DR KEGG; sce:YML035C; -.
DR SGD; S000004498; AMD1.
DR VEuPathDB; FungiDB:YML035C; -.
DR eggNOG; KOG1096; Eukaryota.
DR GeneTree; ENSGT00950000183011; -.
DR HOGENOM; CLU_003782_2_1_1; -.
DR InParanoid; P15274; -.
DR OMA; ESPPYSY; -.
DR BioCyc; YEAST:YML035C-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-74217; Purine salvage.
DR UniPathway; UPA00591; UER00663.
DR PRO; PR:P15274; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P15274; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003876; F:AMP deaminase activity; IDA:SGD.
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:0006178; P:guanine salvage; IMP:SGD.
DR GO; GO:0006188; P:IMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IMP:SGD.
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 Direct protein sequencing; Hydrolase; Metal-binding; Nucleotide metabolism;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..810
FT /note="AMP deaminase"
FT /id="PRO_0000194414"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 652
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 433..438
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 630
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 633
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 707
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 708..711
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950"
FT CONFLICT 568
FT /note="F -> C (in Ref. 1; AAA34420)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 810 AA; 93302 MW; 7A6DCB43B9B45C93 CRC64;
MDNQATQRLN DLSLEPAPSH DEQDGSGLVI DIDQRKIGDE QAGVVVDDET PPLEQQDSHE
SLAADSRNAN FSYHENQQLL ENGTKQLALD EHDSHSAILE QPSHSTNCSS SNIAAMNKGH
DSADHASQNS GGKPRTLSAS AQHILPETLK SFAGAPVVNK QVRTSASYKM GMLADDASQQ
FLDDPSSELI DLYSKVAECR NLRAKYQTIS VQNDDQNPKN KPGWVVYPPP PKPSYNSDTK
TVVPVTNKPD AEVFDFTKCE IPGEDPDWEF TLNDDDSYVV HRSGKTDELI AQIPTLRDYY
LDLEKMISIS SDGPAKSFAY RRLQYLEARW NLYYLLNEYQ ETSVSKRNPH RDFYNVRKVD
THVHHSACMN QKHLLRFIKH KLRHSKDEKV IFRDGKLLTL DEVFRSLHLT GYDLSIDTLD
MHAHKDTFHR FDKFNLKYNP IGESRLREIF LKTNNYIKGT YLADITKQVI FDLENSKYQN
CEYRISVYGR SLDEWDKLAS WVIDNKVISH NVRWLVQIPR LYDIYKKTGI VQSFQDICKN
LFQPLFEVTK NPQSHPKLHV FLQRVIGFDS VDDESKVDRR FHRKYPKPSL WEAPQNPPYS
YYLYYLYSNV ASLNQWRAKR GFNTLVLRPH CGEAGDPEHL VSAYLLAHGI SHGILLRKVP
FVQYLYYLDQ VGIAMSPLSN NALFLTYDKN PFPRYFKRGL NVSLSTDDPL QFSYTREPLI
EEYSVAAQIY KLSNVDMCEL ARNSVLQSGW EAQIKKHWIG KDFDKSGVEG NDVVRTNVPD
IRINYRYDTL STELELVNHF ANFKRTIEEK
