ID A0A2H3I4M7_9EURO Unreviewed; 801 AA.
AC A0A2H3I4M7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=Adenine deaminase {ECO:0000256|HAMAP-Rule:MF_03145};
DE Short=ADE {ECO:0000256|HAMAP-Rule:MF_03145};
DE EC=3.5.4.2 {ECO:0000256|HAMAP-Rule:MF_03145};
DE AltName: Full=Adenine aminohydrolase {ECO:0000256|HAMAP-Rule:MF_03145};
DE Short=AAH {ECO:0000256|HAMAP-Rule:MF_03145};
GN Name=AAH1 {ECO:0000256|HAMAP-Rule:MF_03145};
GN ORFNames=PENO1_081300 {ECO:0000313|EMBL:PCG93884.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG93884.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG93884.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG93884.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenine to
CC hypoxanthine. Plays an important role in the purine salvage pathway and
CC in nitrogen catabolism. {ECO:0000256|HAMAP-Rule:MF_03145}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenine + H(+) + H2O = hypoxanthine + NH4(+);
CC Xref=Rhea:RHEA:23688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17368, ChEBI:CHEBI:28938; EC=3.5.4.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03145};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03145};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03145};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03145}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03145}.
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00010643}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. Adenine deaminase type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03145}.
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:PCG93884.1}.
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DR EMBL; NPFK01000299; PCG93884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3I4M7; -.
DR STRING; 290292.A0A2H3I4M7; -.
DR OrthoDB; 177389at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043103; P:hypoxanthine salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR CDD; cd01320; ADA; 1.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 3.30.70.120; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 1.10.10.1590; NADH-quinone oxidoreductase subunit E; 1.
DR HAMAP; MF_01962; Adenine_deaminase; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR028892; ADE.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR036069; DUF34/NIF3_sf.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR01430; aden_deam; 1.
DR NCBIfam; TIGR01958; nuoE_fam; 1.
DR PANTHER; PTHR43114; ADENINE DEAMINASE; 1.
DR PANTHER; PTHR43114:SF2; ADENINE DEAMINASE; 1.
DR Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF102705; NIF3 (NGG1p interacting factor 3)-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
DR PROSITE; PS01099; COMPLEX1_24K; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03145};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03145};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03145}; Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03145};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03145};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_03145}.
FT DOMAIN 14..346
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
FT ACT_SITE 214
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT SITE 235
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
SQ SEQUENCE 801 AA; 89992 MW; 42789B2FEB42A183 CRC64;
MCNTKLHQFL QHLPKCEHHV HLEGCLTPEL MFDLSARNGV CLPDTEKRPE FGSPEALYER
YEHFTSLDDF LSYYFIGMSV LQQQSDFEAL AWEYFQKAYA DGVHHAEVFF DPQEHLNRAV
PFETVVNGFV AGCRRAETEY GMTTKLIMCF VKHLPASDAQ KVFDLAVEGG HFESGALHGI
GASSSEVGPP KDMFKEIYAT AHSKGIRRTA HAGEEGDPTY IEAALESYKS QRIDHGIRLI
DSPQLMEQVA RDEILLTVCP VSNVKLRCFD HISKVPIRTF LKAGVKFSIN SDDPAYFGGF
ILHNYCSVQE AFDLSIEEWR TIAENSIHGS WVEQERKLEL LKKVDEHIHR QLIHLVSRRL
PHSSIRVSID WTLYESLMFS ATTRITVNLL RNHHRLPIHN TLSAKMSSAT PDRYKLIFFV
PHPQLESCKE AVFSTGAGSF PGGKYTKCCF QTSGTGQFLP EDGANPNIGA VGALEHVEEM
KVEILCVGRE TMLDAVKALV KAHPYEEPAF PSDHFEFRAP NFTKPRPFNL TPLNSTTSSP
AMASKLFPAV VRSSRQIIPQ ISRPQWRSFS AVAPKLSDTL HVHRNKPDNN PSIPFKFSTE
NEKIIDEILK RYPPQYKKAA VMPLLDLGQR QHGFTSISVM NEVARLLEMP PMRVYEVATF
YTMYNREPVG KYFVQVCTTT PCQLGGCGSD KIVQAINKHL GITPGHTTED GLFTYIEVEC
LGACVNAPMV QINDDYYEDL TPESITQLLT ALKESATNPA TKVPAPGPLS GRDTCENSAG
LTNLKEVTWN PEQMMRKDGE L
//
