ID A0A1H7S1C5_STRJI Unreviewed; 389 AA.
AC A0A1H7S1C5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|ARBA:ARBA00019930};
DE EC=3.5.4.26 {ECO:0000256|ARBA:ARBA00012766};
GN ORFNames=SAMN05414137_111100 {ECO:0000313|EMBL:SEL66401.1};
OS Streptacidiphilus jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptacidiphilus.
OX NCBI_TaxID=235985 {ECO:0000313|EMBL:SEL66401.1, ECO:0000313|Proteomes:UP000183015};
RN [1] {ECO:0000313|Proteomes:UP000183015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45096 / BCRC 16803 / CGMCC 4.1857 / CIP 109030 / JCM 12277
RC / KCTC 19219 / NBRC 100920 / 33214
RC {ECO:0000313|Proteomes:UP000183015};
RA Varghese N.;
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}.
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DR EMBL; FOAZ01000011; SEL66401.1; -; Genomic_DNA.
DR RefSeq; WP_042449099.1; NZ_FOAZ01000011.1.
DR AlphaFoldDB; A0A1H7S1C5; -.
DR STRING; 235985.SAMN05414137_111100; -.
DR eggNOG; COG0117; Bacteria.
DR eggNOG; COG1985; Bacteria.
DR OrthoDB; 9800865at2; -.
DR UniPathway; UPA00275; UER00401.
DR Proteomes; UP000183015; 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:UP000183015}.
FT DOMAIN 240..354
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 389 AA; 40694 MW; D08827F79F6DC3E0 CRC64;
MSLEPHPARP SVLISAAMSV DGHIDDAAPE RLLLSSPEDF DRVDALRAAY DAILVGAGTL
RADDPRLEVR DEARRAARVA RGLPEHPLKV ALVGHGGLAA DLRLWQSGGA KLVLAPDAAV
AGLRAELGER AEVVGTGAGL DPARVLDALA ARGVRRLMVE GGGAIQSLFL TAGLVDEIQL
ALAPFFVGDA AAPRFAPPVA GAVFPQDAAH RMTLLGAQSL GDLVVLRYAA RRADASRVTT
ADVDRMRLAI ELSRECPASE TAYSVGAVIV AADGTEIACG FSREGGDDKV HAEESALGKI
DLTDPRLRTA TIYSTLEPCS VRASRPHPCA ELIRAAGIGR VVLAWREPAL FVADCQGVEL
LEQAGATVVE IPALAEEARA VNAHLVSRS
//
