ID A0A0G3H3L7_9CORY Unreviewed; 324 AA.
AC A0A0G3H3L7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN Name=add {ECO:0000313|EMBL:AKK08001.1};
GN ORFNames=CTEST_02730 {ECO:0000313|EMBL:AKK08001.1};
OS Corynebacterium testudinoris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK08001.1, ECO:0000313|Proteomes:UP000035540};
RN [1] {ECO:0000313|EMBL:AKK08001.1, ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK08001.1,
RC ECO:0000313|Proteomes:UP000035540};
RX PubMed=26227591;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL Genome Announc. 3:e00784-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT recovered from necrotic lesions in the mouth of a tortoise.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
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DR EMBL; CP011545; AKK08001.1; -; Genomic_DNA.
DR RefSeq; WP_047252430.1; NZ_CP011545.1.
DR AlphaFoldDB; A0A0G3H3L7; -.
DR STRING; 136857.CTEST_02730; -.
DR KEGG; cted:CTEST_02730; -.
DR PATRIC; fig|136857.5.peg.537; -.
DR OrthoDB; 9779574at2; -.
DR Proteomes; UP000035540; Chromosome.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
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:SF43; ADENOSINE DEAMINASE; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AKK08001.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035540}.
FT DOMAIN 37..302
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 324 AA; 34195 MW; 4DBED0E577CF0420 CRC64;
MHEEPTSQEP TIHDIVTSLP KVVIHDHLEG GPGIDIAALQ TPTALRDAVA QAVRDLAADN
VVYAELRMSP ELYTAGGLTL SEAVDSAIGG LDAADGIDVR LVLTAQRSGT SLADVAALTV
ARHGGVVVGM DVAGPEDGYP LAGDSESFAL LRANYVPFSV HVGLDAGIES IAEAIQLGAT
RLGHATRIVD DFGVDIEGIV PGKVSSWVRD RHIPLEIAPT LEVQLGAADS LGDHPLTLLQ
QLGFTCTVNP GIRSATGMSD QFLALADTFG YGVEEFFDLT VNAVQASYLT EVERQELLER
IILPAYEALD MQAGLDEFDA TDFA
//
