GUAD_DROME
ID GUAD_DROME Reviewed; 448 AA.
AC Q9VMY9;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Guanine deaminase {ECO:0000303|PubMed:19567870};
DE EC=3.5.4.3 {ECO:0000269|PubMed:19567870};
DE AltName: Full=Dihydropterin deaminase {ECO:0000303|PubMed:19567870};
DE EC=3.5.4.- {ECO:0000305|PubMed:19567870};
GN Name=DhpD {ECO:0000312|FlyBase:FBgn0261436};
GN ORFNames=CG18143 {ECO:0000312|FlyBase:FBgn0261436};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM49953.1, ECO:0000312|EMBL:AAN71291.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM49953.1, ECO:0000312|EMBL:AAN71291.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM49953.1, ECO:0000312|EMBL:AAN71291.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, DEVELOPMENTAL STAGE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19567870; DOI=10.1074/jbc.m109.016493;
RA Kim J., Park S.I., Ahn C., Kim H., Yim J.;
RT "Guanine deaminase functions as dihydropterin deaminase in the biosynthesis
RT of aurodrosopterin, a minor red eye pigment of Drosophila.";
RL J. Biol. Chem. 284:23426-23435(2009).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing
CC xanthine and ammonia. Also has 7,8-dihydropterin deaminase activity,
CC which plays a role in synthesis of the red eye pigment aurodrosopterin.
CC {ECO:0000269|PubMed:19567870}.
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:19567870};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2T3};
CC -!- ACTIVITY REGULATION: Strongly inhibited by p-chloromercuribenzoate
CC (PCMB). Potassium cyanide (KCN) strongly inhibits activity towards 7,8-
CC dihydropterin but has almost no effect on activity towards guanine.
CC Pterin inhibits activity towards guanine but has little effect on
CC activity towards 7,8-dihydropterin. {ECO:0000269|PubMed:19567870}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=75.7 uM for guanine {ECO:0000269|PubMed:19567870};
CC KM=1621.0 uM for 7,8-dihydropterin {ECO:0000269|PubMed:19567870};
CC Vmax=23.6 nmol/min/ug enzyme with guanine as substrate
CC {ECO:0000269|PubMed:19567870};
CC Vmax=8.9 nmol/min/ug enzyme with 7,8-dihydropterin as substrate
CC {ECO:0000269|PubMed:19567870};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:19567870};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:19567870};
CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC step 1/1. {ECO:0000305|PubMed:19567870}.
CC -!- DEVELOPMENTAL STAGE: Peak dihydropterin deaminase activity is observed
CC in late pupae and newly eclosed adults, which correlates with the time
CC of eye pigment formation. {ECO:0000269|PubMed:19567870}.
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; AE014297; AAF52167.1; -; Genomic_DNA.
DR EMBL; AY118584; AAM49953.1; -; mRNA.
DR EMBL; BT001536; AAN71291.1; -; mRNA.
DR RefSeq; NP_649439.1; NM_141182.3.
DR AlphaFoldDB; Q9VMY9; -.
DR SMR; Q9VMY9; -.
DR IntAct; Q9VMY9; 1.
DR STRING; 7227.FBpp0078625; -.
DR MEROPS; M38.981; -.
DR PaxDb; Q9VMY9; -.
DR PRIDE; Q9VMY9; -.
DR DNASU; 40528; -.
DR EnsemblMetazoa; FBtr0078986; FBpp0078625; FBgn0261436.
DR GeneID; 40528; -.
DR KEGG; dme:Dmel_CG18143; -.
DR UCSC; CG18143-RA; d. melanogaster.
DR CTD; 40528; -.
DR FlyBase; FBgn0261436; DhpD.
DR VEuPathDB; VectorBase:FBgn0261436; -.
DR eggNOG; KOG3968; Eukaryota.
DR GeneTree; ENSGT00390000017130; -.
DR HOGENOM; CLU_012358_0_1_1; -.
DR InParanoid; Q9VMY9; -.
DR OMA; ALIGKVC; -.
DR OrthoDB; 612054at2759; -.
DR PhylomeDB; Q9VMY9; -.
DR BioCyc; MetaCyc:MON-18459; -.
DR Reactome; R-DME-74259; Purine catabolism.
DR SignaLink; Q9VMY9; -.
DR UniPathway; UPA00603; UER00660.
DR BioGRID-ORCS; 40528; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 40528; -.
DR PRO; PR:Q9VMY9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0261436; Expressed in capitellum (Drosophila) and 25 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR GO; GO:0004153; F:dihydropterin deaminase activity; IDA:FlyBase.
DR GO; GO:0008892; F:guanine deaminase activity; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0051067; P:dihydropteridine metabolic process; IDA:FlyBase.
DR GO; GO:0006726; P:eye pigment biosynthetic process; IMP:FlyBase.
DR GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046098; P:guanine metabolic process; IMP:FlyBase.
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; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02967; guan_deamin; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..448
FT /note="Guanine deaminase"
FT /id="PRO_0000439491"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 76..79
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 204..205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 231..234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
SQ SEQUENCE 448 AA; 48885 MW; E21B8EBADF557CD9 CRC64;
MATVFLGTVV HTKSFSEFES FEGGFLAVDD AGKIIGVGQD YHAWASSNPA HAKGLTEVHL
SDYQFLMPGF VDCHIHAPQF AQLGLGLDMP LLDWLNTYTF PLEAKFSNHQ YAQQVYQGVV
EATLRCGTTL ASYFATNHLE STLTLAREAV RQGQRALIGK VCSNCNSPEF YVETAEESVS
ATLAFVEGVR KLGSPMVMPT ITPRFALSCS KELLKSLGDI AKRFDLHIQS HISENLEEIE
MVKGIFKTSY AGAYDEAGLL TNKTVLAHGV HLEDDEVALL KVRGCSVAHC PTSNTMLSSG
LCDVQRLVSG GVSVGLGTDV SGGNSVSIQD VLLRALDVSK HLDFFKKQNI RGTGVSKTQD
FNYHQLKYKQ ALYLATLGGA KALSLDHLTG NFALGKDFDA LLVDVSVVDK PLRRLSVDEL
VEKFIYTGSD RNIVEVFVAG KRIKQGYQ
