GUAD_ECOLI
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 03-AUG-2022, entry version 143.
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; Proteobacteria; 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}.
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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; P76641; -.
DR PRIDE; P76641; -.
DR EnsemblBacteria; AAC75921; AAC75921; b2883.
DR EnsemblBacteria; BAE76949; BAE76949; BAE76949.
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; ALIGKVC; -.
DR PhylomeDB; P76641; -.
DR BioCyc; EcoCyc:G7502-MON; -.
DR BioCyc; MetaCyc:G7502-MON; -.
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:0019239; F:deaminase activity; IBA:GO_Central.
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; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR014311; Guanine_deaminase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11271:SF6; PTHR11271:SF6; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02967; guan_deamin; 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
