ID A0A3N6ZKN5_9ACTN Unreviewed; 341 AA.
AC A0A3N6ZKN5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|PIRNR:PIRNR006769};
DE Includes:
DE RecName: Full=Diaminohydroxyphosphoribosylaminopyrimidine deaminase {ECO:0000256|PIRNR:PIRNR006769};
DE Short=DRAP deaminase {ECO:0000256|PIRNR:PIRNR006769};
DE EC=3.5.4.26 {ECO:0000256|PIRNR:PIRNR006769};
DE AltName: Full=Riboflavin-specific deaminase {ECO:0000256|PIRNR:PIRNR006769};
DE Includes:
DE RecName: Full=5-amino-6-(5-phosphoribosylamino)uracil reductase {ECO:0000256|PIRNR:PIRNR006769};
DE EC=1.1.1.193 {ECO:0000256|PIRNR:PIRNR006769};
DE AltName: Full=HTP reductase {ECO:0000256|PIRNR:PIRNR006769};
GN Name=ribD {ECO:0000313|EMBL:RQN07587.1};
GN ORFNames=EHW97_09995 {ECO:0000313|EMBL:RQN07587.1};
OS Aeromicrobium camelliae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1538144 {ECO:0000313|EMBL:RQN07587.1, ECO:0000313|Proteomes:UP000275225};
RN [1] {ECO:0000313|EMBL:RQN07587.1, ECO:0000313|Proteomes:UP000275225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YS17T {ECO:0000313|EMBL:RQN07587.1,
RC ECO:0000313|Proteomes:UP000275225};
RA Li F.;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-
CC phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-
CC phosphate. {ECO:0000256|ARBA:ARBA00002151,
CC ECO:0000256|PIRNR:PIRNR006769}.
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 Evidence={ECO:0000256|PIRNR:PIRNR006769};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-
CC amino-6-(5-phospho-D-ribosylamino)uracil + H(+) + NADPH;
CC Xref=Rhea:RHEA:17845, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58421, ChEBI:CHEBI:58453;
CC EC=1.1.1.193; Evidence={ECO:0000256|PIRNR:PIRNR006769};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR006769,
CC ECO:0000256|PIRSR:PIRSR006769-3};
CC Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR006769,
CC ECO:0000256|PIRSR:PIRSR006769-3};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 2/4. {ECO:0000256|ARBA:ARBA00004882,
CC ECO:0000256|PIRNR:PIRNR006769}.
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 3/4. {ECO:0000256|ARBA:ARBA00004910,
CC ECO:0000256|PIRNR:PIRNR006769}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HTP reductase
CC family. {ECO:0000256|ARBA:ARBA00007417, ECO:0000256|PIRNR:PIRNR006769}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and
CC deoxycytidylate deaminase family. {ECO:0000256|ARBA:ARBA00005259,
CC ECO:0000256|PIRNR:PIRNR006769}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RQN07587.1}.
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DR EMBL; RQJX01000012; RQN07587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6ZKN5; -.
DR OrthoDB; 9800865at2; -.
DR UniPathway; UPA00275; UER00401.
DR Proteomes; UP000275225; Unassembled WGS sequence.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:UniProtKB-EC.
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 CDD; cd01284; Riboflavin_deaminase-reductase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR004794; Eubact_RibD.
DR InterPro; IPR002734; RibDG_C.
DR NCBIfam; TIGR00326; eubact_ribD; 1.
DR PANTHER; PTHR38011:SF7; 2,5-DIAMINO-6-RIBOSYLAMINO-4(3H)-PYRIMIDINONE 5'-PHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR38011; DIHYDROFOLATE REDUCTASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_8G06820); 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF01872; RibD_C; 1.
DR PIRSF; PIRSF006769; RibD; 2.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006769, ECO:0000313|EMBL:RQN07587.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006769};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR006769};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR006769};
KW Reference proteome {ECO:0000313|Proteomes:UP000275225};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW ECO:0000256|PIRNR:PIRNR006769};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006769}.
FT DOMAIN 1..108
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 46
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-1"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3"
FT BINDING 147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 264..270
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
SQ SEQUENCE 341 AA; 36227 MW; 07CA87D47A498B57 CRC64;
MRRALDAARA VPRTLPNPPV GCVLLDPDGR ELAVGVHRGA GTPHAEVDAL SQAGEAARGA
TAVVTLEPCD HTGRTGPCTQ ALIAAGVAEV VYAVDDPHPI GAGGAQTLLS AGVKVTTGVL
TEEAKELLAP WATRYWLGRP FVTWKYAATL DGLSAAPDGT SKWITGPEAR RDVQQFRAEC
DAIMAGTGAV LADDPRLTVR DADDMPLPYE QQPMRIVVGE TPIPNYYRVF DRVAPTLLIQ
TREPHDVLAK LMENDIHHVW LEGGPRLAGA FWNAGLIDRV IGYIAPAMLG SGRAALEGEA
TTLADLRPIT ITDLRQIGPD IRIVGTPGPP PREAMGKGEG Y
//
