ID A0A1J4NYC7_9ACTN Unreviewed; 376 AA.
AC A0A1J4NYC7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|ARBA:ARBA00019930};
DE EC=3.5.4.26 {ECO:0000256|ARBA:ARBA00012766};
GN ORFNames=WN71_015185 {ECO:0000313|EMBL:OIJ67058.1};
OS Streptomyces mangrovisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428628 {ECO:0000313|EMBL:OIJ67058.1, ECO:0000313|Proteomes:UP000034196};
RN [1] {ECO:0000313|EMBL:OIJ67058.1, ECO:0000313|Proteomes:UP000034196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC149T {ECO:0000313|Proteomes:UP000034196};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces mangrovisoli MUSC 149.";
RL Submitted (OCT-2016) 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 -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004882}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HTP reductase
CC family. {ECO:0000256|ARBA:ARBA00007417}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and
CC deoxycytidylate deaminase family. {ECO:0000256|ARBA:ARBA00005259}.
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:OIJ67058.1}.
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DR EMBL; LAVA02000033; OIJ67058.1; -; Genomic_DNA.
DR RefSeq; WP_071369845.1; NZ_LAVA02000033.1.
DR AlphaFoldDB; A0A1J4NYC7; -.
DR STRING; 1428628.WN71_015185; -.
DR OrthoDB; 9800865at2; -.
DR UniPathway; UPA00275; UER00401.
DR Proteomes; UP000034196; Unassembled WGS sequence.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro.
DR GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR002734; RibDG_C.
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 SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000034196}.
FT DOMAIN 229..356
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 376 AA; 39801 MW; 06B00B0D147E4222 CRC64;
MPYPYVLLSA AVSLDGFLDD TGPERLLLSS RADFDRVDEV RASVDAILVG AGTIRADNPR
LLVNSPERRA VRIAEGRSAY PLKVTVSGSG ELDPAAHFWH TGGDKAVYTT DKGAARARGL
GLAADVVALG PDLDWRALLE HLHDVRGVRR LMVEGGGTVH TQLLRQGLAD ELQLVLAPLF
VGDPDAPRLF GPGGYQGGRL RLLETRAVGD VVLMRYEPTA PGTGRLPSAA DRHWLWLACQ
LAALCPPSRT AFSVGAVVVA ADGTELARGH SREGGDPVVH AEEAALAKLD PADPRLPGAT
VYSSLEPCAR RASRPAPCAR LILDAGVRRV VTAWREPDTF VTGADGTGLL AANGVDVVVL
AEHEKAAQAP NRHLLG
//
