ADD_VIBCH
ID ADD_VIBCH Reviewed; 334 AA.
AC Q9KNI7;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=VC_2751;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2] {ECO:0007744|PDB:6N91}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH 2'-DEOXYCOFORMYCIN
RP AND ZINC, AND COFACTOR.
RA Maltseva N., Kim Y., Endres M., Welk L., Joachimiak A.;
RT "Crystal structure of adenosine deaminase from Vibrio cholerae complexed
RT with pentostatin (deoxycoformycin) (CASP target).";
RL Submitted (NOV-2018) to the PDB data bank.
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 ECO:0000269|Ref.2};
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; AE003852; AAF95890.1; -; Genomic_DNA.
DR PIR; F82038; F82038.
DR RefSeq; NP_232377.1; NC_002505.1.
DR RefSeq; WP_000633281.1; NZ_LT906614.1.
DR PDB; 6N91; X-ray; 2.05 A; A/B=1-334.
DR PDBsum; 6N91; -.
DR AlphaFoldDB; Q9KNI7; -.
DR SMR; Q9KNI7; -.
DR STRING; 243277.VC_2751; -.
DR DNASU; 2614914; -.
DR EnsemblBacteria; AAF95890; AAF95890; VC_2751.
DR GeneID; 57741342; -.
DR KEGG; vch:VC_2751; -.
DR PATRIC; fig|243277.26.peg.2627; -.
DR eggNOG; COG1816; Bacteria.
DR HOGENOM; CLU_039228_0_2_6; -.
DR OMA; NHFTIHA; -.
DR BioCyc; VCHO:VC2751-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:RHEA.
DR GO; GO:0004000; F:adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006154; P:adenosine catabolic process; IBA:GO_Central.
DR GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central.
DR GO; GO:0046103; P:inosine biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Nucleotide metabolism;
KW Reference proteome; Zinc.
FT CHAIN 1..334
FT /note="Adenosine deaminase"
FT /id="PRO_0000194397"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:6N91"
FT BINDING 14..16
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N91"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:6N91"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 141
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N91"
FT BINDING 170
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N91"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:6N91"
FT BINDING 200
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N91"
FT BINDING 221
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N91"
FT BINDING 278
FT /ligand="2'-deoxycoformycin"
FT /ligand_id="ChEBI:CHEBI:41829"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:6N91"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:6N91"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT SITE 221
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:6N91"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:6N91"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:6N91"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:6N91"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:6N91"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:6N91"
FT STRAND 193..202
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:6N91"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:6N91"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:6N91"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:6N91"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 302..315
FT /evidence="ECO:0007829|PDB:6N91"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6N91"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:6N91"
SQ SEQUENCE 334 AA; 36405 MW; 93195FEFB340781E CRC64;
MITSSLPLTD LHRHLDGNIR TQTILELGQK FGVKLPANTL QTLTPYVQIV EAEPSLVAFL
SKLDWGVAVL GDLDACRRVA YENVEDALNA RIDYAELRFS PYYMAMKHSL PVTGVVEAVV
DGVRAGVRDF GIQANLIGIM SRTFGTDACQ QELDAILSQK NHIVAVDLAG DELGQPGDRF
IQHFKQVRDA GLHVTVHAGE AAGPESMWQA IRDLGATRIG HGVKAIHDPK LMDYLAQHRI
GIESCLTSNL QTSTVDSLAT HPLKRFLEHG ILACINTDDP AVEGIELPYE YEVAAPQAGL
SQEQIRQAQL NGLELAFLSD SEKKALLAKA ALRG
