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Database: UniProt
Entry: ADEC2_RHIME
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ID   ADEC2_RHIME             Reviewed;         593 AA.
AC   Q92VC6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Adenine deaminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade2 {ECO:0000255|HAMAP-Rule:MF_01518}; Synonyms=adeC2;
GN   OrderedLocusNames=RB0782; ORFNames=SMb21278;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymB (megaplasmid 2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481431; DOI=10.1073/pnas.161294698;
RA   Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA   Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT   "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT   endosymbiont Sinorhizobium meliloti.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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:0000255|HAMAP-Rule:MF_01518};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
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DR   EMBL; AL591985; CAC49182.1; -; Genomic_DNA.
DR   PIR; F95939; F95939.
DR   RefSeq; NP_437322.1; NC_003078.1.
DR   RefSeq; WP_010975638.1; NC_003078.1.
DR   AlphaFoldDB; Q92VC6; -.
DR   SMR; Q92VC6; -.
DR   EnsemblBacteria; CAC49182; CAC49182; SM_b21278.
DR   GeneID; 61600758; -.
DR   KEGG; sme:SM_b21278; -.
DR   PATRIC; fig|266834.11.peg.5711; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OrthoDB; 9775607at2; -.
DR   Proteomes; UP000001976; Plasmid pSymB.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR   CDD; cd01295; AdeC; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   HAMAP; MF_01518; Adenine_deamin; 1.
DR   InterPro; IPR006679; Adenine_deam.
DR   InterPro; IPR026912; Adenine_deam_C.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11113:SF2; ADENINE DEAMINASE; 1.
DR   PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR   Pfam; PF13382; Adenine_deam_C; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Plasmid; Reference proteome.
FT   CHAIN           1..593
FT                   /note="Adenine deaminase 2"
FT                   /id="PRO_0000142433"
SQ   SEQUENCE   593 AA;  61858 MW;  6CF4C794779D4E7A CRC64;
     MTVLQQPADL DDACLRARAV AAARGDARFD VLVAGGTVVD VVTGECRAAD VGIVGALIAS
     VHAPGSRSDA DTVIDAAGAY ISPGLIDTHM HVESSMVTPA VYAAAVVPRG VTTVVWDPHE
     FGNVSGLAGV RWAVDAMGGL PLRAVVLAPS CVPSAPGLEV AGADFDADAV AEMLSWPEIG
     GIAEVMNMRG VIDGDPRMTA IVEAGLKAGK PVNGHARGLE GADLQAFVTA GVSSDHELVS
     GDDLIAKLRA GLSIELRGSH DHLLPEFVIA LGTLGHLPQT VTLCTDDVFP DDLHRDGGLD
     DVVRRLVRYG LKAEWALQAA TLNAARRLGR ADLGLIAPGR RADIVLFEDI RDFRALHVLA
     NGRLVASGGG MLQAPVAAGV SPLRHTMKIE PLTEDDFRIA ATGSTARVVT IDRPRFTRWG
     ETRAEVSGGY LVPPKGMTLI AVAHRHGRAD SRPRVGLLEG WGEWRGAFAT TVSHDSHNLT
     VFGSSPRDMR VAANAVIEAG GGMAVVAEGK VEALLPLPLC GLVSDAPLAE VAAGFAAIRE
     AAGRIVEWQP PYLVFKACFG ATLACNAGPH QTDRGIADVA TGKLLESPVL ETF
//
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