ID A0A439D3B8_9PEZI Unreviewed; 1119 AA.
AC A0A439D3B8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN ORFNames=EKO27_g6176 {ECO:0000313|EMBL:RWA08945.1};
OS Xylaria grammica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA08945.1, ECO:0000313|Proteomes:UP000286045};
RN [1] {ECO:0000313|EMBL:RWA08945.1, ECO:0000313|Proteomes:UP000286045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHI A82 {ECO:0000313|EMBL:RWA08945.1,
RC ECO:0000313|Proteomes:UP000286045};
RA Buettner E., Kellner H.;
RT "Draft genome sequence of Xylaria grammica IHI A82.";
RL Submitted (DEC-2018) 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 -!- 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:RWA08945.1}.
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DR EMBL; RYZI01000177; RWA08945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A439D3B8; -.
DR STRING; 363999.A0A439D3B8; -.
DR UniPathway; UPA00591; UER00663.
DR Proteomes; UP000286045; 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 SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000286045}.
FT REGION 1..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 125761 MW; 721F052C37CBEB94 CRC64;
MSEPEPEPEP EPEPPSRLEK LDFDHRPQFA SSEMLPTFHS TSPQRPSTRR QTFDFDSDES
DTSGRALEHH DSADEHDKDH DENDENDSGH SLRHTESTSV GLRVQDSSPA LENGMLPRDV
PRKTTFYDPV AERQMSQTDA KLFYQRSQRD FHKNDASSRA QSHPTPHGSP PAVPNDGGAS
AGGTGSASGA GGVGGAVAAA AVQGKSPIRP SLMSLPSAAQ SYSLPRIAGS PNPVPRGSYI
APRTATRPSL GGHTGSRVVN RQPTHLFVRE EPDLDPQVSM ELPGVAPIGV ADASGDEDAH
ITAELSTIFQ NVQKVLDIRH KYIRLSLQRD GDNPHDDPSW QIYPPPPEPA WTDPPPDHHT
QGQNTGHNSL SSSVVLPPQT SQSQANDPIT SENTSPQAER KKPAKKRKAG QDIGEDFDME
DLLPLPPASE FTFRLDENGV YQVFENTAAD AANTPVVGVP TIKDFYMDLE KILLVSSDGP
SKSFAFRRLQ YLEGKFKLYA LLNEYQETAD TKKVPHRDFY NVRKVDTHVH HSACMNQKHL
LRFIKSKMKK CPDEYVLSRD GKNLTLKEVF ESINLTAYDL SIDTLDMHAH TDSFHRFDKF
NLKYNPIGES RLRTIFLKTD NHIQGRYLAE ITKEVISDLE SSKYQMVEWR ISIYGRSLDE
WDKLAAWVVD NKLFSHNVRW LIQIPRLYDV YKGSGLMESF EQVVRNIFQP LFEVTKDPEK
HPQLHIFLQR VIGFDSVDDE SKVERRLFKK FPVPKEWDSP QNPPYSYWIY YLFSNMTSLN
FWRRQRGFNT FLLRPHCGEA GDVEHLAVAL LCSHSISHGL LLRKVPLLQY IFYLEQIGIA
MSPLSNNALF LAYERNPFIQ YFRRGLNVSL STDDPLQFAF TREPLMEEYA VAAQIWKLSP
VDMCELAKNS VKQSGYEHSI KQLWLGENFN LPGADGNKMI KTNIPDRREE YRYQTWVEEH
RMISRYTSNN EVDQGLEYHP STGLNATTPL SANTAADTGG SEHKNAGSSS LSVVEGGRPA
APSTRADTSN SHLDTRNGAG QGPIAGPPTP TVQLEREPAW PTDGLQNLHL SSHEPRYIPG
MMARASRRDG ARRSSAHESD EAVSSRNHLR KNGEREEPT
//
