ID K5VCJ2_PHACS Unreviewed; 360 AA.
AC K5VCJ2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Adenosine deaminase domain-containing protein {ECO:0000259|Pfam:PF00962};
GN ORFNames=PHACADRAFT_133307 {ECO:0000313|EMBL:EKM60656.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM60656.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM60656.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM60656.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
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}.
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DR EMBL; JH930468; EKM60656.1; -; Genomic_DNA.
DR RefSeq; XP_007390104.1; XM_007390042.1.
DR AlphaFoldDB; K5VCJ2; -.
DR STRING; 650164.K5VCJ2; -.
DR GeneID; 18908258; -.
DR KEGG; pco:PHACADRAFT_133307; -.
DR HOGENOM; CLU_039228_3_0_1; -.
DR InParanoid; K5VCJ2; -.
DR OrthoDB; 20281at2759; -.
DR Proteomes; UP000008370; 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:UP000008370}.
FT DOMAIN 29..354
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 360 AA; 39619 MW; A2817296011854FD CRC64;
MSAYDIAGYA ADALASLTPE EIEFLRELPK AELHAHLNGS IPIPLLQKIA NEADFSSSAI
SSDAVKAGIE QLKTGVVFNE LHDFFGLFPA IYALTATPET LAEAARAVLA QFLEPDPVSP
KGQPMAAYLE LRSTPRTTPN MSRKQYLEAV LDEVERYPVE RAALIVSLDR RMDAKTAEEI
VSLAIKLRQE GRRVVGVDLC GDPLAGNMDN FEQYFKRVKE AGLGVTLHIA ETSENTHEDT
LKLLSFSPDR LGHATFLDTD ARDVVFSNNA CVEICLSSNL LCKTVSILEE HHIRHYLEAN
HPIAVCTDDT LPFRNNLLGE YALLLAKEPL GLGLTREEVE RIARMSMASR FASPVSKTAQ
//
