ID A0A411WTB8_9BURK Unreviewed; 485 AA.
AC A0A411WTB8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Guanine deaminase {ECO:0000256|ARBA:ARBA00012781, ECO:0000256|RuleBase:RU366009};
DE Short=Guanase {ECO:0000256|RuleBase:RU366009};
DE EC=3.5.4.3 {ECO:0000256|ARBA:ARBA00012781, ECO:0000256|RuleBase:RU366009};
DE AltName: Full=Guanine aminohydrolase {ECO:0000256|RuleBase:RU366009};
GN Name=guaD {ECO:0000313|EMBL:QBH99897.1};
GN ORFNames=EYF70_02840 {ECO:0000313|EMBL:QBH99897.1}, GCM10007387_41350
GN {ECO:0000313|EMBL:GGY54689.1};
OS Pseudoduganella albidiflava.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=321983 {ECO:0000313|EMBL:QBH99897.1, ECO:0000313|Proteomes:UP000292307};
RN [1] {ECO:0000313|EMBL:GGY54689.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY54689.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [2] {ECO:0000313|EMBL:QBH99897.1, ECO:0000313|Proteomes:UP000292307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17472 {ECO:0000313|EMBL:QBH99897.1,
RC ECO:0000313|Proteomes:UP000292307};
RA Miess H., Frediansyhah A., Gross H.;
RT "Draft Genome Sequences of Six Type Strains of the Genus Massilia.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GGY54689.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY54689.1};
RA Sun Q., Kim S.;
RL Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing
CC xanthine and ammonia. {ECO:0000256|RuleBase:RU366009}.
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:0000256|RuleBase:RU366009};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU366009};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU366009};
CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC step 1/1. {ECO:0000256|ARBA:ARBA00004984,
CC ECO:0000256|RuleBase:RU366009}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000256|ARBA:ARBA00006745,
CC ECO:0000256|RuleBase:RU366009}.
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; BMWV01000010; GGY54689.1; -; Genomic_DNA.
DR EMBL; CP036401; QBH99897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411WTB8; -.
DR KEGG; mali:EYF70_02840; -.
DR OrthoDB; 3189065at2; -.
DR UniPathway; UPA00603; UER00660.
DR Proteomes; UP000292307; Chromosome.
DR Proteomes; UP000628442; Unassembled WGS sequence.
DR GO; GO:0008892; F:guanine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniRule.
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 InterPro; IPR006311; TAT_signal.
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; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366009, ECO:0000313|EMBL:QBH99897.1};
KW Metal-binding {ECO:0000256|RuleBase:RU366009};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU366009}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..485
FT /note="Guanine deaminase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019245789"
FT DOMAIN 106..474
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 485 AA; 52952 MW; 819E2192611E768F CRC64;
MNKARLSCLT AAIAAALAAT AATAAPSAQA SQQNQQQQQQ QGSVAYRAAV LHFTGDPSAT
QQSYEYYEDG VLLVGADGKV KAIGPASTVL SNHQNVQVVD YRGRLIVPGF IDSHVHYPQT
EMIGSFGEQL LEWLNTYTFP TEKQFGNKDY AKGVAKTFVN ELVKNGTTTA LVMATVHPES
VDALFEEAAK RNMRIIAGKV MMDRNAPDYL LDTAQTSYAD SKTLINRWHK RGRALYAVTP
RFAPTSTPEQ LTMAGKLLQE YPDVYMHTHL SENKGEIAWV QELFPSSTGY LNVYDSFGLS
RKRSVYAHGV HLRDDEFASL AKTGSAIAFC PTSNLFLGSG LFDLQAAEKH GVKVGMGTDV
GAGTSFSALR TMGEAYKVIQ LHKAFTDTPA EKKPLTALKS FYLSTLGAAK ALDLDDRIGS
FKAGNEADFV VLNPNATELL KFRSARATTL EEKLFVLQTL GDDRTVERTY IMGKRQDVAA
SGNKR
//
