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Database: UniProt
Entry: A0A162YRE6_MUCCL
LinkDB: A0A162YRE6_MUCCL
Original site: A0A162YRE6_MUCCL 
ID   A0A162YRE6_MUCCL        Unreviewed;       799 AA.
AC   A0A162YRE6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE            EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN   ORFNames=MUCCIDRAFT_173785 {ECO:0000313|EMBL:OAD00167.1};
OS   Mucor lusitanicus CBS 277.49.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=747725 {ECO:0000313|EMBL:OAD00167.1, ECO:0000313|Proteomes:UP000077051};
RN   [1] {ECO:0000313|EMBL:OAD00167.1, ECO:0000313|Proteomes:UP000077051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAD00167.1,
RC   ECO:0000313|Proteomes:UP000077051};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004955}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676,
CC       ECO:0000256|PIRNR:PIRNR001251}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAD00167.1}.
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DR   EMBL; AMYB01000007; OAD00167.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162YRE6; -.
DR   STRING; 747725.A0A162YRE6; -.
DR   VEuPathDB; FungiDB:QYA_173785; -.
DR   OrthoDB; 20951at2759; -.
DR   UniPathway; UPA00591; UER00663.
DR   Proteomes; UP000077051; Unassembled WGS sequence.
DR   GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd01319; AMPD; 1.
DR   Gene3D; 4.10.800.20; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR006329; AMPD.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01429; AMP_deaminase; 1.
DR   PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR   PANTHER; PTHR11359:SF0; AMP DEAMINASE; 1.
DR   Pfam; PF19326; AMP_deaminase; 1.
DR   PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077051}.
FT   REGION          140..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   799 AA;  91758 MW;  6F91E001CA832270 CRC64;
     MPNTIYSNKK RQADGIDIPS DEGINNFDDS PYFDYHHLKA IENHDSKYLC QSLSVSPAAN
     HLSDLHIDDD EALPTLPQVP EKSSFLKEPV THTADPNAKF EAKDDAITAE LCVLYGNLQK
     CLDLREKYIT LSSQRLMDDP RNHDDWNIYP APPPKSWPLP SPEELERRKA KEKAREADPV
     AAVGSDFDFD QCEIPGPHVY SFGVGPDGFY QVYKNELDQT AGHPLHPVPS PREFYDDMEF
     ILSVISDGPA KSFAFRRLRY LDSKWQMYIL LNEFQELADS KRTPHRDFYN VRKVDTHVHH
     SSSMNQKHLL RFIKSKMKKS PDDVVIYRDN HHLTLRGVFE SLGLTAYDLS IDTLDMHAHK
     DSFHRFDKFN LKYNPIGESR LREIFMKTDN YIQGKYLAEI TKEVVSDLES SKYQMVEYRV
     SIYGRSIDEW DKLAKWVVNN KLFSANVRWL IQIPRLYNIY KASNAINSFQ DIITNVFEPL
     FEVTKDPSSH PELHVFLQRV IGFDTVDDES KPEKPIFKDF PLPKDWTSGV NPPYSYYLYY
     MYANTAALNK WRQARGFTTL VLRPHCGEAG DTDHLTAAFL TSYGISHGIL LRKVPALQYL
     YYLAQVGIAM SPLSNNALFL TYERNPLPQF FQRGLNISLS TDDPLQFHFT KEPLIEEYSV
     AAQIWKLSST DMCELARNSV IQSGWENQIK THWIGKDWHK PGVEGNDMQK TNVPDIRVGF
     RYETLHEELE ALRRYAPKGE SSEHEEPLSK KDYVGVAGLA ESSSIQQHLM SKSPVDKSHI
     GSFPGAGLVA ERAKLRSGH
//
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