ADD_MYCVP
ID ADD_MYCVP Reviewed; 362 AA.
AC A1T5H1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Adenosine deaminase {ECO:0000255|HAMAP-Rule:MF_00540};
DE EC=3.5.4.4 {ECO:0000255|HAMAP-Rule:MF_00540};
DE AltName: Full=Adenosine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_00540};
GN Name=add {ECO:0000255|HAMAP-Rule:MF_00540}; OrderedLocusNames=Mvan_1592;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-
CC deoxyadenosine. {ECO:0000255|HAMAP-Rule:MF_00540}.
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:0000255|HAMAP-Rule:MF_00540};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+);
CC Xref=Rhea:RHEA:28190, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17256, ChEBI:CHEBI:28938, ChEBI:CHEBI:28997; EC=3.5.4.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00540};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. Adenosine deaminase subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00540}.
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DR EMBL; CP000511; ABM12421.1; -; Genomic_DNA.
DR RefSeq; WP_011778846.1; NC_008726.1.
DR AlphaFoldDB; A1T5H1; -.
DR SMR; A1T5H1; -.
DR STRING; 350058.Mvan_1592; -.
DR EnsemblBacteria; ABM12421; ABM12421; Mvan_1592.
DR KEGG; mva:Mvan_1592; -.
DR eggNOG; COG1816; Bacteria.
DR HOGENOM; CLU_039228_0_0_11; -.
DR OMA; NHFTIHA; -.
DR OrthoDB; 554648at2; -.
DR Proteomes; UP000009159; Chromosome.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:RHEA.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; 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:UniProtKB-UniRule.
DR HAMAP; MF_00540; A_deaminase; 1.
DR InterPro; IPR028893; A_deaminase.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; PTHR11409; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01430; aden_deam; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT CHAIN 1..362
FT /note="Adenosine deaminase"
FT /id="PRO_1000017675"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT SITE 232
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
SQ SEQUENCE 362 AA; 39652 MW; 2DF0562058B4324B CRC64;
MTTPLTFDNI RRAPKALLHD HLDGGLRPST VLELAEQYGY EDLPAHDADG LATFFRTAAH
SGSLVRYLEP FAHTVGVMQN PDALHRVARE CVEDLAADNV VYAEVRFAPE LHIDGGLSLD
AVVDAVLAGF ADGEKAAAAD GRAITVRCLV TAMRHAARSR EIAELAIRFR DKGVVGFDIA
GAEAGYPPSR HLDAFEYMRS NNARFTIHAG EAFGLPSIHE AIAFCGADRL GHGVRIVDDI
EIDADGNAKL GRLASLLRDK RIPFEMCPSS NVQTGAVASI AEHPFDRLAR LRFRVTVNTD
NRLMSDTSMS MEMLRLVEAF GYGWSDLERF TINAMKSAFI AFDERLAIID EVIKPRYAVL
VG
