LUXB1_PHOLE
ID LUXB1_PHOLE Reviewed; 325 AA.
AC P09141;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Alkanal monooxygenase beta chain;
DE EC=1.14.14.3 {ECO:0000250|UniProtKB:P12744};
DE AltName: Full=Bacterial luciferase beta chain;
GN Name=luxB;
OS Photobacterium leiognathi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=553611;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=554;
RX PubMed=3186447; DOI=10.1093/nar/16.20.9855;
RA Illiarinov B.A., Protopopova M.V., Karginov V.A., Mertvetsov N.P.,
RA Gitelson J.I.;
RT "Nucleotide sequence of part of Photobacterium leiognathi lux region.";
RL Nucleic Acids Res. 16:9855-9855(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=554;
RX PubMed=3382442;
RA Illarionov B.A., Protopopova M.V., Karginov V.A., Mertvetsov N.P.,
RA Gitelson J.I.;
RT "Nucleotide sequence of genes for alpha- and beta-subunits of luciferase
RT from Photobacterium leiognathi.";
RL Bioorg. Khim. 14:412-415(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=554;
RX PubMed=2311938; DOI=10.1016/0378-1119(90)90117-a;
RA Illarionov B.A., Blinov V.M., Donchenko A.P., Protopopova M.V.,
RA Karginov V.A., Mertvetsov N.P., Gitelson J.I.;
RT "Isolation of bioluminescent functions from Photobacterium leiognathi:
RT analysis of luxA, luxB, luxG and neighboring genes.";
RL Gene 86:89-94(1990).
CC -!- FUNCTION: Light-emitting reaction in luminous bacteria. The specific
CC role of the beta subunit is unknown, but it is absolutely required for
CC bioluminescence activity. {ECO:0000250|UniProtKB:P12744}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty aldehyde + FMNH2 + O2 = a long-chain fatty
CC acid + FMN + 2 H(+) + H2O + hnu; Xref=Rhea:RHEA:17181,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17176, ChEBI:CHEBI:30212, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.3;
CC Evidence={ECO:0000250|UniProtKB:P12744};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000250|UniProtKB:P07740}.
CC -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; X08036; CAA30832.1; -; Genomic_DNA.
DR PIR; S01698; S01698.
DR RefSeq; WP_053987809.1; NZ_LNRC01000002.1.
DR PDB; 6FRI; X-ray; 2.30 A; A/B/C/D=1-325.
DR PDBsum; 6FRI; -.
DR AlphaFoldDB; P09141; -.
DR SMR; P09141; -.
DR STRING; 553611.GCA_001557755_01580; -.
DR PRIDE; P09141; -.
DR GO; GO:0047646; F:alkanal monooxygenase (FMN-linked) activity; IEA:UniProtKB-EC.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR CDD; cd01096; Alkanal_monooxygenase; 1.
DR Gene3D; 3.20.20.30; -; 2.
DR InterPro; IPR033924; Alkanal_monooxygenase.
DR InterPro; IPR018235; Bacterial_luciferase_CS.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR002103; Luciferase_bac/NFP.
DR Pfam; PF00296; Bac_luciferase; 1.
DR PRINTS; PR00089; LUCIFERASE.
DR SUPFAM; SSF51679; SSF51679; 1.
DR PROSITE; PS00494; BACTERIAL_LUCIFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; Luminescence; Monooxygenase;
KW Oxidoreductase; Photoprotein.
FT CHAIN 1..325
FT /note="Alkanal monooxygenase beta chain"
FT /id="PRO_0000220174"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 17..31
FT /evidence="ECO:0007829|PDB:6FRI"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:6FRI"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:6FRI"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:6FRI"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 126..143
FT /evidence="ECO:0007829|PDB:6FRI"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:6FRI"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:6FRI"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:6FRI"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 200..216
FT /evidence="ECO:0007829|PDB:6FRI"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 238..256
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:6FRI"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:6FRI"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:6FRI"
FT HELIX 307..321
FT /evidence="ECO:0007829|PDB:6FRI"
SQ SEQUENCE 325 AA; 37353 MW; 73A7AFA4F92CF2A9 CRC64;
MNFGLFFLNF QLKGMTSEAV LDNMIDTIAL VDKDEYHFKT AFVNEHHFSK NGIVGAPMTA
ASFLLGLTER LHIGSLNQVI TTHHPVRIAE EASLLDQMSD GRFILGLSDC VSDFEMDFFK
RQRDSQQQQF EACYEILNDG ITTNYCYANN DFYNFPKISI NPHCISKENL KQYILATSMG
VVEWAAKKGL PLTYRWSDTL AEKENYYQRY LTVAAENNVD ITHVDHQFPL LVNINPDRDI
AKQEMRDYIR GYIAEAYPNT DQEEKIEELI KQHAVGTEDE YYESSKYALE KTGSKNVLLS
FESMKNKAAV IDLINMVNEK IKKNL
