GUAD_BACSU
ID GUAD_BACSU Reviewed; 156 AA.
AC O34598;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Guanine deaminase;
DE Short=GDEase;
DE Short=Guanase;
DE Short=Guanine aminase;
DE EC=3.5.4.3;
DE AltName: Full=Guanine aminohydrolase;
DE Short=GAH;
GN Name=guaD; Synonyms=gde; OrderedLocusNames=BSU13170;
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;
RA Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=11101664; DOI=10.1099/00221287-146-12-3061;
RA Nygaard P., Bested S.M., Andersen K.A.K., Saxild H.H.;
RT "Bacillus subtilis guanine deaminase is encoded by the yknA gene and is
RT induced during growth with purines as the nitrogen source.";
RL Microbiology 146:3061-3069(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.17 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
RX PubMed=15180998; DOI=10.1074/jbc.m405304200;
RA Liaw S.-H., Chang Y.-J., Lai C.-T., Chang H.-C., Chang G.-G.;
RT "Crystal structure of Bacillus subtilis guanine deaminase: the first
RT domain-swapped structure in the cytidine deaminase superfamily.";
RL J. Biol. Chem. 279:35479-35485(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
RG Northeast structural genomics consortium (NESG);
RT "X-ray structure of guanine deaminase from Bacillus subtilis.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing
CC xanthine and ammonia. {ECO:0000269|PubMed:11101664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanine + H(+) + H2O = NH4(+) + xanthine;
CC Xref=Rhea:RHEA:14665, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16235, ChEBI:CHEBI:17712, ChEBI:CHEBI:28938; EC=3.5.4.3;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC step 1/1.
CC -!- INDUCTION: Expressed only during limited or partially limited nitrogen
CC conditions. Can be induced to high levels in the presence of purines or
CC intermediates of the purine catabolic pathway. Expression seems
CC indirectly controlled by TnrA and GlnR.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AJ002571; CAA05596.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13174.1; -; Genomic_DNA.
DR PIR; F69857; F69857.
DR RefSeq; NP_389200.1; NC_000964.3.
DR RefSeq; WP_003245084.1; NZ_JNCM01000035.1.
DR PDB; 1TIY; X-ray; 2.50 A; A/B=1-156.
DR PDB; 1WKQ; X-ray; 1.17 A; A/B=1-156.
DR PDBsum; 1TIY; -.
DR PDBsum; 1WKQ; -.
DR AlphaFoldDB; O34598; -.
DR SMR; O34598; -.
DR STRING; 224308.BSU13170; -.
DR DrugBank; DB03366; Imidazole.
DR PaxDb; O34598; -.
DR EnsemblBacteria; CAB13174; CAB13174; BSU_13170.
DR GeneID; 936695; -.
DR KEGG; bsu:BSU13170; -.
DR PATRIC; fig|224308.179.peg.1430; -.
DR eggNOG; COG0590; Bacteria.
DR InParanoid; O34598; -.
DR OMA; MCHAAMR; -.
DR PhylomeDB; O34598; -.
DR BioCyc; BSUB:BSU13170-MON; -.
DR BRENDA; 3.5.4.3; 658.
DR UniPathway; UPA00603; UER00660.
DR EvolutionaryTrace; O34598; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008892; F:guanine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0047974; F:guanosine deaminase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006152; P:purine nucleoside catabolic process; IBA:GO_Central.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Purine metabolism;
KW Reference proteome; Zinc.
FT CHAIN 1..156
FT /note="Guanine deaminase"
FT /id="PRO_0000171704"
FT DOMAIN 1..132
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:1WKQ"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1WKQ"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1WKQ"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:1WKQ"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:1WKQ"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:1WKQ"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1WKQ"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1WKQ"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:1WKQ"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1WKQ"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:1WKQ"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:1WKQ"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1WKQ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1WKQ"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1WKQ"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:1WKQ"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:1WKQ"
SQ SEQUENCE 156 AA; 17156 MW; B6498345A98BC214 CRC64;
MNHETFLKRA VTLACEGVNA GIGGPFGAVI VKDGAIIAEG QNNVTTSNDP TAHAEVTAIR
KACKVLGAYQ LDDCILYTSC EPCPMCLGAI YWARPKAVFY AAEHTDAAEA GFDDSFIYKE
IDKPAEERTI PFYQVTLTEH LSPFQAWRNF ANKKEY
