ID A0A2N5SEG4_9BASI Unreviewed; 332 AA.
AC A0A2N5SEG4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE RecName: Full=Adenosine deaminase domain-containing protein {ECO:0000259|Pfam:PF00962};
GN ORFNames=PCANC_21464 {ECO:0000313|EMBL:PLW11585.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW11585.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW11585.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW11585.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + N(6)-methyl-AMP = IMP + methylamine;
CC Xref=Rhea:RHEA:16001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:59338, ChEBI:CHEBI:144842;
CC Evidence={ECO:0000256|ARBA:ARBA00036622};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16002;
CC Evidence={ECO:0000256|ARBA:ARBA00036622};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:PLW11585.1}.
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DR EMBL; PGCJ01001014; PLW11585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5SEG4; -.
DR STRING; 200324.A0A2N5SEG4; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR PANTHER; PTHR11409:SF42; ADENOSINE DEAMINASE-LIKE PROTEIN; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000235388}.
FT DOMAIN 11..327
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 332 AA; 37716 MW; 2D513F909C90E3FF CRC64;
MDSKQFCQKL PKVECHAHLS GSIPLEVLHE LHKDTKERHP HLAPCPSPLD YADLQSEHIY
HILDTPEAIT RATTAVLESF REDGYVYLEL RTTPCILPGH LDSFQEYLDA VYEAVDRNDE
SRMMVCLILT INWDFAPDKV KQIVQLATVA RNAGRSIVAV DVAGDPQKSL LRNEEFTREL
VKAKTNGLKL TIHFAEIAKQ RPFLEKQLSK LAPDQLGHAV FLTPEVQANI IQSKRPIEIC
PTSNLKVGSV RLLEEHHFKW AVENKVPVLI STDDTLVFGT TLSEEYGWAF SLLDNDRQKL
MSILKESIPY TFCSSEDQNI LTQKIDQFIT DQ
//