RISA_PHOPO
ID RISA_PHOPO Reviewed; 218 AA.
AC P51961;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Riboflavin synthase {ECO:0000303|PubMed:8144477};
DE Short=RS {ECO:0000305};
DE EC=2.5.1.9 {ECO:0000269|PubMed:8144477};
GN Name=ribE {ECO:0000303|PubMed:8144477};
GN Synonyms=ribI {ECO:0000303|PubMed:8144477};
OS Photobacterium phosphoreum.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=659;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=DSM 2167 / CIP 104260 / LMG 4231 / NCIMB 844;
RX PubMed=8144477; DOI=10.1128/jb.176.7.2100-2104.1994;
RA Lee C.Y., O'Kane D.J., Meighen E.A.;
RT "Riboflavin synthesis genes are linked with the lux operon of
RT Photobacterium phosphoreum.";
RL J. Bacteriol. 176:2100-2104(1994).
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:0000269|PubMed:8144477}.
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; Evidence={ECO:0000269|PubMed:8144477};
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:0000269|PubMed:8144477}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q2YN92}.
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DR EMBL; L11391; AAA25628.1; -; Genomic_DNA.
DR AlphaFoldDB; P51961; -.
DR SMR; P51961; -.
DR UniPathway; UPA00275; UER00405.
DR GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-EC.
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 InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR001783; Lumazine-bd.
DR InterPro; IPR026017; Lumazine-bd_dom.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR21098; PTHR21098; 1.
DR Pfam; PF00677; Lum_binding; 2.
DR PIRSF; PIRSF000498; Riboflavin_syn_A; 1.
DR SUPFAM; SSF63380; SSF63380; 2.
DR TIGRFAMs; TIGR00187; ribE; 1.
DR PROSITE; PS51177; LUMAZINE_BIND; 2.
PE 1: Evidence at protein level;
KW Repeat; Riboflavin biosynthesis; Transferase.
FT CHAIN 1..218
FT /note="Riboflavin synthase"
FT /id="PRO_0000068171"
FT REPEAT 1..97
FT /note="Lumazine-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00524"
FT REPEAT 98..194
FT /note="Lumazine-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00524"
FT BINDING 4..6
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 48..50
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 62..67
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P0AFU8"
FT BINDING 101..103
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 136
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 145..147
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 159..164
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
SQ SEQUENCE 218 AA; 23639 MW; 309B197A71430975 CRC64;
MFTGIIEAVG NISAITSKGS DFEVSVNCDT LDLADVKIGD SIATNGICLT VVKLTANSYV
ADLSIETLSR TAFNYYKVGQ AVNLEKAMLP TTRFGGHIVS GHVDAVAEVI ECRTSGRAID
IWIRVPSQIE KYLSEKGSVT VDGVSLTVNA VTGNEFKLTI VPHTVVETTI ADFKVGNKVN
IEVDVLARYI ERLLLVDKPE DKQSKISMDL LERNGFLL
