ID A0A1D2I9N6_9ACTN Unreviewed; 377 AA.
AC A0A1D2I9N6;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, 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 Name=ribD2_2 {ECO:0000313|EMBL:ODA71206.1};
GN ORFNames=APS67_004551 {ECO:0000313|EMBL:ODA71206.1};
OS Streptomyces sp. AVP053U2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1737066 {ECO:0000313|EMBL:ODA71206.1, ECO:0000313|Proteomes:UP000054731};
RN [1] {ECO:0000313|EMBL:ODA71206.1, ECO:0000313|Proteomes:UP000054731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AVP053U2 {ECO:0000313|EMBL:ODA71206.1,
RC ECO:0000313|Proteomes:UP000054731};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-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:ODA71206.1}.
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DR EMBL; LMTQ02000028; ODA71206.1; -; Genomic_DNA.
DR RefSeq; WP_042175253.1; NZ_LMTQ02000028.1.
DR AlphaFoldDB; A0A1D2I9N6; -.
DR OrthoDB; 9800865at2; -.
DR UniPathway; UPA00275; UER00401.
DR Proteomes; UP000054731; 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 ECO:0000313|EMBL:ODA71206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054731}.
FT DOMAIN 229..359
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 377 AA; 39816 MW; 5602D3A0E801D967 CRC64;
MPHPYVLLSA AVSLDGYLDD TGPERLLLSG PEDFDRVDEV RASVDAILVG AGTIRADNPR
LLVNAPERRA ARVAEGRPAY PLKVTVSGSG DLDPAARFWH TGGAKVLYTT GKGAERARAH
GLAADIVPLG AELDWRRLLT HLYDAYGVRR LMVEGGGLIH TQLLTQGLAD ELQLVLAPLF
VGDPDAARLF GPGTYQGGRL RLLETRQVGD VVLMRYEPTA PGTGPLPVAA DHHWLALACE
LAKRCPPSET AFSVGAVVVA ADGTELARGH SREGGDPVVH AEEAALARTD PADPRLATAT
VYSSLEPCAR RASRPAPCAR LILDAGVRRV VTAWREPDTF VAGADGSGAL AAEGALVVVL
PEHEESAEAP NGHLIGR
//