LUXP_PHOLE
ID LUXP_PHOLE Reviewed; 186 AA.
AC Q06877; Q51877;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Lumazine protein;
DE Short=LUMP;
GN Name=lumP;
OS Photobacterium leiognathi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=553611;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=741;
RX PubMed=8472956; DOI=10.1016/0378-1119(93)90605-3;
RA Lin J.-W., Chao Y.-F., Weng S.-F.;
RT "The lumazine protein-encoding gene in Photobacterium leiognathi is linked
RT to the lux operon.";
RL Gene 126:153-154(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=554;
RA Illarionov B.A.;
RL Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Antenna protein that modulates the color of the
CC bioluminescence emission of the luciferase. In the presence of LumP,
CC luciferase emission is shifted to higher energy values (shorter
CC wavelength).
CC -!- COFACTOR:
CC Name=6,7-dimethyl-8-(1-D-ribityl)lumazine; Xref=ChEBI:CHEBI:58201;
CC Note=Binds 1 6,7-dimethyl-8-(1'-D-ribityl)lumazine non-covalently.;
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DR EMBL; X65611; CAA46562.1; -; Genomic_DNA.
DR EMBL; X56534; CAA39879.1; -; Genomic_DNA.
DR PIR; JN0517; JN0517.
DR PDB; 3DDY; X-ray; 2.50 A; A=1-186.
DR PDBsum; 3DDY; -.
DR AlphaFoldDB; Q06877; -.
DR SMR; Q06877; -.
DR STRING; 553611.GCA_001557755_01584; -.
DR EvolutionaryTrace; Q06877; -.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
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 PROSITE; PS51177; LUMAZINE_BIND; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Luminescence; Repeat.
FT CHAIN 1..186
FT /note="Lumazine protein"
FT /id="PRO_0000068153"
FT REPEAT 1..96
FT /note="Lumazine-binding 1"
FT REPEAT 97..186
FT /note="Lumazine-binding 2"
FT CONFLICT 94
FT /note="G -> C (in Ref. 2; CAA39879)"
FT /evidence="ECO:0000305"
FT STRAND 8..17
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:3DDY"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:3DDY"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3DDY"
FT TURN 65..69
FT /evidence="ECO:0007829|PDB:3DDY"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:3DDY"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:3DDY"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:3DDY"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3DDY"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3DDY"
SQ SEQUENCE 186 AA; 19997 MW; F52BB662F59F6218 CRC64;
MFRGIVQGRG VIRSISKSED SQRHGIAFPE GMFQLVDVDT VMLVNGCSLT VVRILGDMVY
FDIDQALGTT TFDGLKEGDQ VNLEIHPKFG EVVGRGGLTG NIKGTALVAA IEENDAGFSV
LIDIPKGLAE NLTVKDDIGI DGISLPITDM SDSIITLNYS RDLLASTNIA SLAKDVKVNV
EILNEW
