ID A0A097R6S1_HAFAL Unreviewed; 438 AA.
AC A0A097R6S1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=AT03_19905 {ECO:0000313|EMBL:AIU74438.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU74438.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU74438.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU74438.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(2014).
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}.
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DR EMBL; CP009706; AIU74438.1; -; Genomic_DNA.
DR RefSeq; WP_025798511.1; NZ_CP009706.1.
DR AlphaFoldDB; A0A097R6S1; -.
DR KEGG; hav:AT03_19905; -.
DR PATRIC; fig|1453496.5.peg.4101; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_012358_0_2_6; -.
DR OrthoDB; 9787621at2; -.
DR UniPathway; UPA00603; UER00660.
DR Proteomes; UP000029986; Chromosome.
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 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366009};
KW Metal-binding {ECO:0000256|RuleBase:RU366009};
KW Reference proteome {ECO:0000313|Proteomes:UP000029986};
KW Zinc {ECO:0000256|RuleBase:RU366009}.
FT DOMAIN 72..434
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 438 AA; 50052 MW; 248C1FE0C259EFF4 CRC64;
MSGQHSLKAI RGNFLDIVKT VEQPEEIESH LRFIEDGLML LRSGKVEWFG TWQEGKHLIP
EGIRVRDYSG KMIVPGFVDT HIHYPQSEMV GAYGEQLLEW LNKHTFPAER RYNDIEYARE
MSAFFIKQLL RNGTTTALVF GTVHPESVDA LFEAAHNINM RMIAGKVMMD RNAPDYLLDT
AESSYSQSKA LIERWHHNGR LLYAITPRFA PTSTPEQLAM AQRLREEYPD TYLHTHLCEN
KDEIEWVKAL YPERKGYLDV YHHYGLTGKN SVFAHCVHLE ESEWDCLRDT GSSIAFCPTS
NLYLGSGLFN LRKAWHKQIK VGMGTDIGAG TTFNMLQTLN EAYKVMQLQG WRMSAYEAFY
LATLGGAKAL GLDGIIGNFN VGKEADFVVL EPTATPLQQL RYDNSVTLMD KLFVMMTLGD
DRSIYRTYVD GQLVYERT
//