ID A0A0M3R9I1_9BACI Unreviewed; 366 AA.
AC A0A0M3R9I1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ORFNames=AM592_07540 {ECO:0000313|EMBL:ALC81466.1};
OS Bacillus gobiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1441095 {ECO:0000313|EMBL:ALC81466.1, ECO:0000313|Proteomes:UP000067625};
RN [1] {ECO:0000313|Proteomes:UP000067625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-4402 {ECO:0000313|Proteomes:UP000067625};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALC81466.1, ECO:0000313|Proteomes:UP000067625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-4402 {ECO:0000313|EMBL:ALC81466.1,
RC ECO:0000313|Proteomes:UP000067625};
RX PubMed=26530456; DOI=10.1099/ijsem.0.000729;
RA Liu B., Liu G.H., Cetin S., Schumann P., Pan Z.Z., Chen Q.Q.;
RT "Bacillus gobiensis sp. nov., isolated from a soil sample.";
RL Int. J. Syst. Evol. Microbiol. 66:379-384(2016).
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}.
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DR EMBL; CP012600; ALC81466.1; -; Genomic_DNA.
DR RefSeq; WP_053603224.1; NZ_CP012600.1.
DR AlphaFoldDB; A0A0M3R9I1; -.
DR STRING; 1441095.AM592_07540; -.
DR PATRIC; fig|1441095.3.peg.1661; -.
DR OrthoDB; 9800865at2; -.
DR UniPathway; UPA00275; UER00401.
DR Proteomes; UP000067625; Chromosome.
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:0050661; F:NADP binding; IEA:InterPro.
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; IPR011549; RibD_C.
DR InterPro; IPR002734; RibDG_C.
DR NCBIfam; TIGR00326; eubact_ribD; 1.
DR NCBIfam; TIGR00227; ribD_Cterm; 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; 1.
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};
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:UP000067625};
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..122
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 51
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-1"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3"
FT BINDING 153
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 199
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT BINDING 292..298
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
SQ SEQUENCE 366 AA; 39713 MW; F3873C55218DBBA7 CRC64;
MDKQFMQTAI DLAKTAEGQT GKNPLVGAVV VKNNQVVGLG AHLMYGEPHA EVNALTMAGS
AAEGSTLYVT LEPCNHHGKT PPCTELIISS RVKQVVIGSK DPNPIVNGKG IKRLQDAGIA
VTEGILKEEC DKLNTMLFHS LRTGLPFVTL KSAVSLDGKT AVESGESKWI TGEEARKDVH
LYRSSHQSIL VGVNTVIQDD PSLTARLPNV QKQPVRVVLD SSLKIPIHSK VLNDREAETW
IFTTNQANAE KVNFLKSEGI RVFQSSSQQP SVREVLRTLA SEGIYSVFVE GGSKVHSSFL
KDQLYQQLII YYAPKLIGGK SSPGLFSDVG FQSMKDVPLL TIHSISKIGR DFKLIAAPSV
ENFPNG
//
