ID   RIBD1_BUCAI             Reviewed;         147 AA.
AC   P57533;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-FEB-2002, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Diaminohydroxyphosphoribosylamino-pyrimidine deaminase;
DE            Short=DRAP deaminase;
DE            EC=3.5.4.26;
DE   AltName: Full=Riboflavin-specific deaminase;
GN   Name=ribD1; OrderedLocusNames=BU461;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine +
CC         H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+);
CC         Xref=Rhea:RHEA:21868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58453, ChEBI:CHEBI:58614; EC=3.5.4.26;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC       ribitylamino)uracil from GTP: step 2/4.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB13158.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000003; BAB13158.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_240272.1; NC_002528.1.
DR   RefSeq; WP_029585593.1; NC_002528.1.
DR   AlphaFoldDB; P57533; -.
DR   SMR; P57533; -.
DR   STRING; 107806.10039124; -.
DR   EnsemblBacteria; BAB13158; BAB13158; BAB13158.
DR   KEGG; buc:BU461; -.
DR   PATRIC; fig|107806.10.peg.470; -.
DR   eggNOG; COG0117; Bacteria.
DR   HOGENOM; CLU_036590_10_0_6; -.
DR   OMA; GFVDPDP; -.
DR   UniPathway; UPA00275; UER00401.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR004794; Eubact_RibD.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR00326; eubact_ribD; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Riboflavin biosynthesis;
KW   Zinc.
FT   CHAIN           1..147
FT                   /note="Diaminohydroxyphosphoribosylamino-pyrimidine
FT                   deaminase"
FT                   /id="PRO_0000171725"
FT   DOMAIN          1..123
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        52
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   147 AA;  16049 MW;  7E4753A37EDFE506 CRC64;
     MNDIFYMKRA IELSKLGEFT TAPNPNVGCV IVKNNIIVGE GWHEQAGKNH AEINALIMAG
     EKAQGGTAYV TLEPCNHFGK TPPCCNALIK SGINRVVISN IDPNPKISGN GILYLKKHGI
     CVKTGLLSKE SKQYNKGFFK RMKTGFP