ID A6DMG4_9BACT Unreviewed; 415 AA.
AC A6DMG4;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Riboflavin synthase {ECO:0000256|ARBA:ARBA00013950};
DE EC=2.5.1.9 {ECO:0000256|ARBA:ARBA00012827};
DE EC=4.1.99.12 {ECO:0000256|ARBA:ARBA00012153};
GN ORFNames=LNTAR_15832 {ECO:0000313|EMBL:EDM27154.1};
OS Lentisphaera araneosa HTCC2155.
OC Bacteria; Lentisphaerota; Lentisphaeria; Lentisphaerales; Lentisphaeraceae;
OC Lentisphaera.
OX NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM27154.1, ECO:0000313|Proteomes:UP000004947};
RN [1] {ECO:0000313|EMBL:EDM27154.1, ECO:0000313|Proteomes:UP000004947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM27154.1,
RC ECO:0000313|Proteomes:UP000004947};
RX PubMed=20363947; DOI=10.1128/JB.00208-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.;
RT "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species of
RT the order Lentisphaerales in the phylum Lentisphaerae.";
RL J. Bacteriol. 192:2938-2939(2010).
CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC and 3,4-dihydroxy-2-butanone 4-phosphate.
CC {ECO:0000256|ARBA:ARBA00002284}.
CC -!- FUNCTION: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-
CC ribityllumazine, resulting in the formation of riboflavin and 5-amino-
CC 6-(D-ribitylamino)uracil. {ECO:0000256|ARBA:ARBA00002803}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-
CC ribitylamino)uracil + riboflavin; Xref=Rhea:RHEA:20772,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:57986,
CC ChEBI:CHEBI:58201; EC=2.5.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000968};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-
CC oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004904}.
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC ribitylamino)uracil: step 2/2. {ECO:0000256|ARBA:ARBA00004887}.
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:EDM27154.1}.
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DR EMBL; ABCK01000011; EDM27154.1; -; Genomic_DNA.
DR RefSeq; WP_007279062.1; NZ_ABCK01000011.1.
DR AlphaFoldDB; A6DMG4; -.
DR STRING; 313628.LNTAR_15832; -.
DR eggNOG; COG0307; Bacteria.
DR OrthoDB; 9788537at2; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000004947; Unassembled WGS sequence.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00402; Riboflavin_synthase_like; 1.
DR Gene3D; 2.40.30.20; -; 2.
DR Gene3D; 3.90.870.10; DHBP synthase; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR000422; DHBP_synthase_RibB.
DR InterPro; IPR001783; Lumazine-bd.
DR InterPro; IPR026017; Lumazine-bd_dom.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; TIGR00187; ribE; 1.
DR PANTHER; PTHR21098:SF0; RIBOFLAVIN SYNTHASE; 1.
DR PANTHER; PTHR21098; RIBOFLAVIN SYNTHASE ALPHA CHAIN; 1.
DR Pfam; PF00926; DHBP_synthase; 1.
DR Pfam; PF00677; Lum_binding; 2.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 2.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
DR PROSITE; PS51177; LUMAZINE_BIND; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000004947};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDM27154.1}.
FT REPEAT 1..97
FT /note="Lumazine-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00524"
FT DOMAIN 1..97
FT /note="Lumazine-binding"
FT /evidence="ECO:0000259|PROSITE:PS51177"
FT DOMAIN 98..196
FT /note="Lumazine-binding"
FT /evidence="ECO:0000259|PROSITE:PS51177"
FT REPEAT 98..196
FT /note="Lumazine-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00524"
SQ SEQUENCE 415 AA; 44994 MW; 8B053F8722D2130D CRC64;
MFGGIIKYKG SVQSISGNEV DGMVLELNTS LVEQVQIGDS VGVDGVCLTV TEIVSDTVLK
FDIWPESLQR TTLVDLKIDQ EVHVDLPLKA NDFIGGHPVL GHVDYVGSIL SMSQVDEASQ
LKIWISLPQE FSSLIPARGS IAVDGVSLTI TGRESDRFAI SLIPETLRLT HLDALTEGSQ
VNIEVDFSSR ALQDESGMIH LANESSTISN KVDKLEAAID TYKNGGLILI QDGADFALCS
SAETITDKNL TFALSLSRTP CTVAVTEGLA EKLFIPAPVI NTKAEERRFL LPVNHKENSL
HDYSTKAMKR SIGLFCSSEL SIDDWMTPGN INPLQIFGAN SSSQPGLPEA AVALCFKSKL
PHAAICQSLI DAEGKAMNSK QAEVISTRYQ IPLYQVSDLI AENAELFEDD YFGDL
//
