ID A0A2H3CEG1_9AGAR Unreviewed; 795 AA.
AC A0A2H3CEG1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN ORFNames=ARMSODRAFT_951242 {ECO:0000313|EMBL:PBK75157.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK75157.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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}.
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DR EMBL; KZ293418; PBK75157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3CEG1; -.
DR STRING; 1076256.A0A2H3CEG1; -.
DR OrthoDB; 20951at2759; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000218334; 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; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000218334}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 91576 MW; CB044DF7BD68B5EE CRC64;
MAALLQAEVD DIPPQAKPTT TPPPQIPESR DAFYGYPEER TFQHIEEKMW AHRRGSDARS
DGAASFAGSM LGHGVAADAR VPSPFAEELE EEAEEAAKSA MDGHPPETVL SSELVHLFQS
FQRCLELRDK YTRKSCQRLG DNPKDYDGYF QGLEDESADV NGVKPDASLP ARSSASDTKQ
AKRWKVYPSP PPPHWHWTDD KEAVSVDGGY SGSGKEFKFE ECDIPGNHDW DFKIDDKGVY
QVYEPDQATP AFDIPNIREY FVDLDYILGV ISDGPTKSYA FRRLKYLASK FTMYSLLNEF
QELADMKRVP HRDFYNLRKV DTHVHHSSSM NQKHLLRFIK SKMKRSPQDV VIFRDSAELT
LEQVFQSLKL TAYDLSIDTL DMHAHQDTFH RFDKFNLKYN PIGESRLREI FLKTDNFIKG
RYLAEITKEV MTDLEQSKYQ NCEWRLSIYG RSPDEWDKLA KWIVNNKLYS HNVRWLIQVP
RLYDVYKANG SIKTFEDIVI NVFRPLFEVT KDPTTHPELH VFLQRVVGFD TVDDESKAER
RIYKKFPYPR VWDTNQSPPY SYWIYYMFAN MASLNNWRRL RGFNTFVFRP HCGEAGDTDH
LTSAFLTSHS ISHGILLRKV PALQYLFYLK QIGIAMSPLS NNALFLTYER NPLPDFFKTG
LNVSLSTDDP LQFHFTKEPL LEEYSVAAHI YKLPQSSLAE LARNSVIQSG FEMELKRHWI
GHEWYLPGAA GNDINKTNVP NIRLSYRHQT LLEELDMICA KNHGHGSAGR RDSHGHGHGM
LPTADNVAAR AMARH
//