ID   A0A7L5UF69_9LACO        Unreviewed;       351 AA.
AC   A0A7L5UF69;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   02-JUN-2021, entry version 2.
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:QLL69106.1};
GN   ORFNames=GTO83_00200 {ECO:0000313|EMBL:QLL69106.1};
OS   Lactobacillus sp. 3B(2020).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus; unclassified Lactobacillus.
OX   NCBI_TaxID=2695882 {ECO:0000313|EMBL:QLL69106.1, ECO:0000313|Proteomes:UP000510624};
RN   [1] {ECO:0000313|EMBL:QLL69106.1, ECO:0000313|Proteomes:UP000510624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3B(2020) {ECO:0000313|Proteomes:UP000510624};
RA   Hassan H.M.;
RT   "Complete and circular genome sequences of six lactobacillus isolates from
RT   horses.";
RL   Submitted (JAN-2020) 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|ARBA:ARBA00000334,
CC         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|ARBA:ARBA00000659,
CC         ECO:0000256|PIRNR:PIRNR006769};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006769};
CC       Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR006769};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005104}.
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; CP047410; QLL69106.1; -; Genomic_DNA.
DR   UniPathway; UPA00275; -.
DR   Proteomes; UP000510624; 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   Gene3D; 3.40.430.10; -; 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   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   Pfam; PF01872; RibD_C; 1.
DR   PIRSF; PIRSF006769; RibD; 1.
DR   SUPFAM; SSF53597; SSF53597; 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 {ECO:0000256|PIRNR:PIRNR006769, ECO:0000313|EMBL:QLL69106.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR006769};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|PIRNR:PIRNR006769};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006769,
KW   ECO:0000313|EMBL:QLL69106.1};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW   ECO:0000256|PIRNR:PIRNR006769};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006769}.
FT   DOMAIN          2..125
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
SQ   SEQUENCE   351 AA;  38579 MW;  C70C3C32C8DFEA65 CRC64;
     MNHDQAMMQL AINAAKEGRF LTWQNPMVGA AVVKDGHVLA LGHHVKYGAV HAERNAIEKL
     TPEQLFNATL YVTLEPCNHQ GKQPPCSELI IHSKIKRVVI GQTDPHALVT GKGIARLKTA
     GIEVITGVLA DQATALNPFY TYFFQHHQPW ITLKQAISLD HKLSLPGQRI TLSSSAALKQ
     VHFERANYQG ILIGSETAII DDPSLLTTVK SPFPPIRMII DRRGRLLNHP NLKLLTDGAA
     PTWIFTQNNQ LGNHQWPAHV KVISLADGQL SSVIDYLTDQ GIQSLYVEGG RRLHQAFCDA
     GLGNELITYL APVTLGKNGV PAYQPKAGQL IKPSYQFFGN TIRIQGGIQN V
//