ID A0A1Y1UYB8_9FUNG Unreviewed; 513 AA.
AC A0A1Y1UYB8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE SubName: Full=Metallo-dependent hydrolase {ECO:0000313|EMBL:ORX43427.1};
GN ORFNames=BCR36DRAFT_336114 {ECO:0000313|EMBL:ORX43427.1};
OS Piromyces finnis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX43427.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX43427.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT biomass hydrolysis.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX43427.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001466};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. ADGF subfamily.
CC {ECO:0000256|ARBA:ARBA00006083}.
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:ORX43427.1}.
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DR EMBL; MCFH01000053; ORX43427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1UYB8; -.
DR STRING; 1754191.A0A1Y1UYB8; -.
DR EnsemblFungi; ORX43427; ORX43427; BCR36DRAFT_336114.
DR OrthoDB; 4403at2759; -.
DR Proteomes; UP000193719; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:InterPro.
DR GO; GO:0006154; P:adenosine catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006331; ADGF.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01431; adm_rel; 1.
DR PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR PANTHER; PTHR11409:SF39; ADENOSINE DEAMINASE 2; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000313|EMBL:ORX43427.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193719};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 186..481
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 513 AA; 60855 MW; 2ED6CF1BCC2247FE CRC64;
MSKQDFIEKK KILLENDRNE SFDWEVYNKR SLEEEFANAI LQENKEKDLQ MFKELSEAPF
SAIHFSEIKK FLDRKQSYLL DTLKYLPKGI IHHCHIDALV DAKWIIEKII KSDSLYLKFI
GDSNIDNLNI VDFQFFINGI NEEQKNEGWQ NFKEIRHQYK KGIEAFDQWL YECFTIVPTN
KEDIVYTENE IWKRFSRTFI SLRGIFSYVP FTKLYVKEII ERYSKKDLQQ IEIRIPYYEP
YNDTGIVKFT EMFGELVNTI EESKKELSLI NENYFEIKFI ISPVRNTPEE EMLKIMAITT
ELYQKYPRYV VGFDMVGHEH LMTLEAHIDS LLYFKDQQKQ LGIDIPFYFH AGETTDSGSP
TDNNLFDAVL LNTKRIGHGY SLSRHLTSLG PTIKKKNMCL EISPISNQYL GLVKDLANHP
IIIFLKNNIP VSISPDDPSL FGYEGSTYDF YMIFMTYRNF DIWTLKQLCI NSIKYGSFTK
EYNMEDMLKV WECKWQFWIR NIINNNKDVI MAN
//
