ID   YERA_BACSU              Reviewed;         580 AA.
AC   O34909; O30566;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Putative adenine deaminase YerA;
DE            Short=Adenase;
DE            Short=Adenine aminase;
DE            EC=3.5.4.2;
GN   Name=yerA; Synonyms=yecB; OrderedLocusNames=BSU06560;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9701819; DOI=10.1046/j.1365-2958.1998.00927.x;
RA   Petit M.-A., Dervyn E., Rose M., Entian K.-D., McGovern S., Ehrlich S.D.,
RA   Bruand C.;
RT   "PcrA is an essential DNA helicase of Bacillus subtilis fulfilling
RT   functions both in repair and rolling-circle replication.";
RL   Mol. Microbiol. 29:261-273(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969499; DOI=10.1099/13500872-142-11-3027;
RA   Borriss R., Porwollik S., Schroeter R.;
RT   "The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a
RT   region devoted to purine uptake and metabolism, and containing the genes
RT   cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide
RT   sequence.";
RL   Microbiology 142:3027-3031(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
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   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenine deaminase family. {ECO:0000305}.
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DR   EMBL; Y15254; CAA75547.1; -; Genomic_DNA.
DR   EMBL; AF011544; AAB72188.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12476.1; -; Genomic_DNA.
DR   PIR; H69793; H69793.
DR   RefSeq; NP_388538.1; NC_000964.3.
DR   RefSeq; WP_003233929.1; NZ_JNCM01000032.1.
DR   AlphaFoldDB; O34909; -.
DR   SMR; O34909; -.
DR   STRING; 224308.BSU06560; -.
DR   iPTMnet; O34909; -.
DR   jPOST; O34909; -.
DR   PaxDb; O34909; -.
DR   PRIDE; O34909; -.
DR   DNASU; 939337; -.
DR   EnsemblBacteria; CAB12476; CAB12476; BSU_06560.
DR   GeneID; 939337; -.
DR   KEGG; bsu:BSU06560; -.
DR   PATRIC; fig|224308.179.peg.713; -.
DR   eggNOG; COG1001; Bacteria.
DR   InParanoid; O34909; -.
DR   OMA; IEGHFPG; -.
DR   PhylomeDB; O34909; -.
DR   BioCyc; BSUB:BSU06560-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IBA:GO_Central.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR   CDD; cd01295; AdeC; 1.
DR   Gene3D; 2.30.40.10; -; 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   Pfam; PF13382; Adenine_deam_C; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..580
FT                   /note="Putative adenine deaminase YerA"
FT                   /id="PRO_0000142447"
FT   MOD_RES         399
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   CONFLICT        533
FT                   /note="L -> M (in Ref. 2; AAB72188)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        541
FT                   /note="C -> R (in Ref. 2; AAB72188)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        550..551
FT                   /note="LQ -> WE (in Ref. 2; AAB72188)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        554
FT                   /note="H -> D (in Ref. 2; AAB72188)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   580 AA;  66646 MW;  C4C84D1DD1D2B9AA CRC64;
     MSERTFNWKN KDIRAQVDVV DSKLLPTLLL RNALVLNPYV KQWLKKNIWI YQDRIVYVGH
     ELPNRAEEIH TIDCEGKYIV PGYIEPHAHP FQIYNPQTLA EYVSQYGTTT FVNDNLFLLL
     QSGKKKALTI LNELKKQPVQ YFWWSRYDLQ TEVLNEDHVL PFDVRKQWIE HPDVIQGGEM
     TGWPRLVDGD DLMLHCMQAT KKQRKRIEGH FPGASDKTLT KMKLFGADCD HEAMTGDEVM
     RRLELGYYVS LRNSSIRPDV RKILQELHEK GFRYYDHFFY TTDGATPNFY KGGMTNELIR
     IALEEGVPAI DAYNMASFNI AKYYQMDDYL GVVGPGRLAS LNILEDPLNP NPVTVLSKGT
     ILRENGCDLK AFTKTDWHKG GLVPLELSYD MTMDDLQFSM PMGVKMRNAV IMEPYMIEID
     NSMEQLSFDH DESYLTMLDR HGKWRVNTMI KGFASSVQGF VSSFTTTGDI VAIGKNKADM
     LLAFARMKEI GGGIVLAENG NILHEIPLAL CGCASSEAYE DVLEKEQKLR DLLTERGYEF
     CDPIYTLLFL QSTHLPYIRI TPRGIFDVMK KTVLFPSIMR