ID   CADD_LEPIC              Reviewed;         442 AA.
AC   Q72V44;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Cyclic adenylate deaminase {ECO:0000303|PubMed:24074367};
DE            Short=CadD {ECO:0000303|PubMed:24074367};
DE            EC=3.5.4.46 {ECO:0000269|PubMed:24074367};
DE   AltName: Full=cAMP deaminase;
GN   Name=add; OrderedLocusNames=LIC_10459;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
RN   [2]
RP   CATALYTIC ACTIVITY, NOMENCLATURE, AND FUNCTION.
RX   PubMed=24074367; DOI=10.1021/cb4004628;
RA   Goble A.M., Feng Y., Raushel F.M., Cronan J.E.;
RT   "Discovery of a cAMP deaminase that quenches cyclic AMP-dependent
RT   regulation.";
RL   ACS Chem. Biol. 8:2622-2629(2013).
CC   -!- FUNCTION: Deaminates cAMP into cIMP, thereby repressing cAMP dependent
CC       metabolism or genes. {ECO:0000269|PubMed:24074367}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP + H(+) + H2O = 3',5'-cyclic IMP + NH4(+);
CC         Xref=Rhea:RHEA:22908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58165, ChEBI:CHEBI:134197;
CC         EC=3.5.4.46; Evidence={ECO:0000269|PubMed:24074367};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22909;
CC         Evidence={ECO:0000269|PubMed:24074367};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q9I6Y4};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=27 uM for cAMP {ECO:0000269|PubMed:24074367};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000255}.
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DR   EMBL; AE016823; AAS69080.1; -; Genomic_DNA.
DR   RefSeq; WP_001229174.1; NC_005823.1.
DR   AlphaFoldDB; Q72V44; -.
DR   SMR; Q72V44; -.
DR   PaxDb; Q72V44; -.
DR   EnsemblBacteria; AAS69080; AAS69080; LIC_10459.
DR   GeneID; 61143810; -.
DR   KEGG; lic:LIC_10459; -.
DR   HOGENOM; CLU_039228_7_1_12; -.
DR   OMA; NHFTIHA; -.
DR   BRENDA; 3.5.4.46; 15061.
DR   Proteomes; UP000007037; Chromosome I.
DR   GO; GO:0090612; F:cAMP deaminase activity; IDA:CACAO.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd01320; ADA; 1.
DR   InterPro; IPR006650; A/AMP_deam_AS.
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.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..442
FT                   /note="Cyclic adenylate deaminase"
FT                   /id="PRO_0000446370"
SQ   SEQUENCE   442 AA;  51052 MW;  C8E83362A0F498C3 CRC64;
     MALTFQEILD RIRIIDRDVT ELNRLKSRLP ADRPYSSSLQ ISFDKQINEL LNERVGLMEL
     EVLDPPSWIL GVPTTGISQE TPVPLKGLFP SGDLSKEKPD DQDVINFLRE LPKTEIHLHL
     EACVNKDTMK RLMAKNGINV TDEEFEAKFN FKDLNSFIQV FFFIQSLVKE PSDFSFFIES
     LAEYMRANNI LYTEVFFAPS KFIQNGLDFE EMIDFLVNRI REEKENDGIV IRLLVDVSRS
     FGPENAMKNL DRVLKLRHPE VIGIGLGGAE LMGPARDYQG VFQKAREAGL RVVAHSGEDD
     GPWAIWEAVE LLKAERIGHG TSAIQDPELV KYLRENHIPI EICVTSNVFT GKYVRKEQNH
     PVRYYYDQGL PLSINTDDPE IFNVNLTYEY YKLWRFLDFS LDEIVDLIRQ GVFASFHPNK
     ESLWAEMEKN IHLVKTRYGL KR