ID   A0A1Y2VVB9_9PEZI        Unreviewed;      1048 AA.
AC   A0A1Y2VVB9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE            EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN   ORFNames=M426DRAFT_323385 {ECO:0000313|EMBL:OTB01494.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB01494.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB01494.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB01494.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(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}.
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DR   EMBL; KZ111581; OTB01494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2VVB9; -.
DR   STRING; 1001833.A0A1Y2VVB9; -.
DR   InParanoid; A0A1Y2VVB9; -.
DR   OrthoDB; 20951at2759; -.
DR   UniPathway; UPA00591; UER00663.
DR   Proteomes; UP000242955; 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:UP000242955}.
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          948..983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1012..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        953..980
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1048 AA;  118170 MW;  4E13B0F4A3BBFE9A CRC64;
     MSSYHPTSPK VPVAHQTLNY DSDGSDAAAH AIESDSEPES QEEHGPRAHD EKENVGPDTP
     NYKEDISSPS LEDGMLPRDL PRKTTFHDAV AERQLTHAEA KLFYQRSQLD QLKTEGSNWS
     LAQNTPYDSP VASVSAAPIK LGNESSAARP QLNSGPKSTE SYNFPHIAGS SPTPGGLNAT
     PRTATRPFLG GYFGSQPTSH PRGATPQEQP KMNLQPNMGL PDGASSSIAS GVGSDDPHIV
     AELSTIFQNI QKILDIRHKY IRLSLQRDGD NPKDDPSWDI YPPPPEPAWA EAHANYDTHG
     VNTGNNSMSN SMVLPPQGTA ADAEPKRPIR KRKPGHDIGE DFVMSDLSPL PQASEFVFRL
     DENGVYQVFE NDAADKANTP VVGVPTIKDF YMDLEDILST SSDGPGKSFA FRRLQYLEGK
     FNLYTLLNEY QETADTKKVP HRDFYNVRKV DTHVHHSACM NQKHLLRFIK SKMKKCPDEY
     VLFRDGKNLT LKEVFESINL TAYDLSIDTL DMHAHTDSFH RFDKFNLKYN PIGESRLRTI
     FLKTDNFIQG RYLAEITKEV ISDLESSKYQ MVEWRISIYG RSLDEWDNLA AWVVDNKLFS
     HNVRWLIQIP RLFDVFKATG LMESFEQVVK NVFQPLFEVT KDPESHPKLH IFLQRVIGFD
     SVDDESKVER RLYRKFPVPK EWNSKQNPPY SYWIYYLFSN MTSLNFWRHQ RGFNTFLLRP
     HCGEAGDSEH LAVAVLCSHS ISHGLLLRKV PLLQYIFYLE QIGIAMSPLS NNALFLAYER
     NPFYQYFRRG LNVSLSTDDP LQFAYTKEPL MEEYAVAAQI YKLSPVDMCE LAKNSVRQSG
     YEYSVKQQWL GEKFNLPGKD GNSMVKTNVP DRREEFRYHT WVEEHRMISS YTSTTELHEV
     LEHHPGAAPT QNPASPTLSA NTNLVSGMAT GDLKSHANLN AANLEGRLPR AGSQAEASSS
     HLDAPTGGSN PRSVSPFSRP HRESWSVEGI RESLRETHLS GHEPRYIPGM MARASRHGSM
     HRSSAYDGED AGSTRSTSKR PNGREEPS
//