ID GUAD_ECOLI Reviewed; 439 AA. AC P76641; Q2M9V7; Q46816; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 150. DE RecName: Full=Guanine deaminase; DE Short=Guanase; DE Short=Guanine aminase; DE EC=3.5.4.3 {ECO:0000269|PubMed:10913105}; DE AltName: Full=Guanine aminohydrolase; DE Short=GAH; GN Name=guaD; Synonyms=ygfP; OrderedLocusNames=b2883, JW5466; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10913105; DOI=10.1128/jb.182.16.4658-4660.2000; RA Maynes J.T., Yuan R.G., Snyder F.F.; RT "Identification, expression, and characterization of Escherichia coli RT guanine deaminase."; RL J. Bacteriol. 182:4658-4660(2000). CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing CC xanthine and ammonia. {ECO:0000269|PubMed:10913105}. 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 Evidence={ECO:0000269|PubMed:10913105}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14666; CC Evidence={ECO:0000305|PubMed:10913105}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=15 uM for guanine {ECO:0000269|PubMed:10913105}; CC Vmax=3.8 nmol/min/mg enzyme with guanine as substrate CC {ECO:0000269|PubMed:10913105}; CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine: CC step 1/1. {ECO:0000305|PubMed:10913105}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC ATZ/TRZ family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U28375; AAA83064.1; -; Genomic_DNA. DR EMBL; U00096; AAC75921.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76949.1; -; Genomic_DNA. DR PIR; C65072; C65072. DR RefSeq; NP_417359.1; NC_000913.3. DR PDB; 6OHB; X-ray; 2.30 A; A/B/C/D=1-439. DR PDB; 6OHC; X-ray; 2.30 A; A/B/C/D=1-439. DR PDBsum; 6OHB; -. DR PDBsum; 6OHC; -. DR AlphaFoldDB; P76641; -. DR SMR; P76641; -. DR BioGRID; 4259227; 10. DR BioGRID; 851689; 1. DR STRING; 511145.b2883; -. DR jPOST; P76641; -. DR PaxDb; 511145-b2883; -. DR EnsemblBacteria; AAC75921; AAC75921; b2883. DR GeneID; 947366; -. DR KEGG; ecj:JW5466; -. DR KEGG; eco:b2883; -. DR PATRIC; fig|511145.12.peg.2976; -. DR EchoBASE; EB2878; -. DR eggNOG; COG0402; Bacteria. DR HOGENOM; CLU_012358_0_2_6; -. DR InParanoid; P76641; -. DR OMA; CVHMNDS; -. DR PhylomeDB; P76641; -. DR BioCyc; EcoCyc:G7502-MONOMER; -. DR BioCyc; MetaCyc:G7502-MONOMER; -. DR BRENDA; 3.5.4.3; 2026. DR UniPathway; UPA00603; UER00660. DR PRO; PR:P76641; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0018756; F:ammeline aminohydrolase activity; IMP:EcoCyc. DR GO; GO:0008892; F:guanine deaminase activity; IDA:EcoCyc. DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc. DR GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046098; P:guanine metabolic process; IBA:GO_Central. DR CDD; cd01303; GDEase; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR014311; Guanine_deaminase. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR02967; guan_deamin; 1. DR PANTHER; PTHR11271; GUANINE DEAMINASE; 1. DR PANTHER; PTHR11271:SF6; GUANINE DEAMINASE; 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 1: Evidence at protein level; KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..439 FT /note="Guanine deaminase" FT /id="PRO_0000122297" FT BINDING 82 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3" FT BINDING 84..87 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3" FT BINDING 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3" FT BINDING 209..210 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3" FT BINDING 237..240 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3" FT BINDING 237 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3" FT BINDING 327 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3" FT BINDING 327 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3" FT STRAND 8..18 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 25..27 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 29..31 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 32..43 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 46..52 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 53..56 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 67..76 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 78..84 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 98..104 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 106..111 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 116..132 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 135..141 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 146..158 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 182..196 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 203..208 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 216..228 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 232..239 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 242..251 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 258..264 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 272..276 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 282..290 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 294..297 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 299..304 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 312..317 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 321..324 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 336..349 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 356..363 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 365..370 FT /evidence="ECO:0007829|PDB:6OHB" FT TURN 374..376 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 377..379 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 388..391 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 397..404 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 409..419 FT /evidence="ECO:0007829|PDB:6OHB" FT HELIX 422..424 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 425..430 FT /evidence="ECO:0007829|PDB:6OHB" FT STRAND 433..437 FT /evidence="ECO:0007829|PDB:6OHB" SQ SEQUENCE 439 AA; 50244 MW; 43389F3AF9E4AD83 CRC64; MMSGEHTLKA VRGSFIDVTR TIDNPEEIAS ALRFIEDGLL LIKQGKVEWF GEWENGKHQI PDTIRVRDYR GKLIVPGFVD THIHYPQSEM VGAYGEQLLE WLNKHTFPTE RRYEDLEYAR EMSAFFIKQL LRNGTTTALV FGTVHPQSVD ALFEAASHIN MRMIAGKVMM DRNAPDYLLD TAESSYHQSK ELIERWHKNG RLLYAITPRF APTSSPEQMA MAQRLKEEYP DTWVHTHLCE NKDEIAWVKS LYPDHDGYLD VYHQYGLTGK NCVFAHCVHL EEKEWDRLSE TKSSIAFCPT SNLYLGSGLF NLKKAWQKKV KVGMGTDIGA GTTFNMLQTL NEAYKVLQLQ GYRLSAYEAF YLATLGGAKS LGLDDLIGNF LPGKEADFVV MEPTATPLQQ LRYDNSVSLV DKLFVMMTLG DDRSIYRTYV DGRLVYERN //