ID LUXA_VIBHA Reviewed; 355 AA.
AC P07740; Q56698; Q6LBZ4; Q6LBZ5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Alkanal monooxygenase alpha chain;
DE EC=1.14.14.3 {ECO:0000250|UniProtKB:P19839};
DE AltName: Full=Bacterial luciferase alpha chain;
GN Name=luxA;
OS Vibrio harveyi (Beneckea harveyi).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=669;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3997817; DOI=10.1016/s0021-9258(18)88948-7;
RA Cohn D.H., Mileham A.J., Simon M.I., Nealson K.H., Rausch S.K., Bonam D.,
RA Baldwin T.O.;
RT "Nucleotide sequence of the luxA gene of Vibrio harveyi and the complete
RT amino acid sequence of the alpha subunit of bacterial luciferase.";
RL J. Biol. Chem. 260:6139-6146(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CTP5;
RX PubMed=1685011; DOI=10.1007/bf00280295;
RA Escher A., O'Kane D.J., Szalay A.A.;
RT "The beta subunit polypeptide of Vibrio harveyi luciferase determines light
RT emission at 42 degrees C.";
RL Mol. Gen. Genet. 230:385-393(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 AND 74-133.
RC STRAIN=ATCC 33843 / NCIMB 1871 / 392 / MAV;
RX PubMed=6571986; DOI=10.1073/pnas.80.1.120;
RA Cohn D.H., Ogden R.C., Abelson J.N., Baldwin T.O., Nealson K.H.,
RA Simon M.I., Mileham A.J.;
RT "Cloning of the Vibrio harveyi luciferase genes: use of a synthetic
RT oligonucleotide probe.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:120-123(1983).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND SUBUNIT.
RX PubMed=7756289; DOI=10.1021/bi00020a002;
RA Fisher A.J., Raushel F.M., Baldwin T.O., Rayment I.;
RT "Three-dimensional structure of bacterial luciferase from Vibrio harveyi at
RT 2.4-A resolution.";
RL Biochemistry 34:6581-6586(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), AND SUBUNIT.
RX PubMed=8703001; DOI=10.1074/jbc.271.36.21956;
RA Fisher A.J., Thompson T.B., Thoden J.B., Baldwin T.O., Rayment I.;
RT "The 1.5-A resolution crystal structure of bacterial luciferase in low salt
RT conditions.";
RL J. Biol. Chem. 271:21956-21968(1996).
CC -!- FUNCTION: Light-emitting reaction in luminous bacteria.
CC {ECO:0000250|UniProtKB:P19839}.
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:P19839};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000269|PubMed:7756289, ECO:0000269|PubMed:8703001}.
CC -!- MISCELLANEOUS: The synthesis of this protein is regulated by a complex
CC control mechanism that has been termed autoinduction. In fully induced
CC cells luciferase comprises up to 5% of the soluble protein.
CC -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; M10961; AAA88685.1; -; Genomic_DNA.
DR EMBL; X58791; CAA41597.1; -; Genomic_DNA.
DR EMBL; V01422; CAA24692.1; -; Genomic_DNA.
DR EMBL; V01423; CAA24693.1; -; Genomic_DNA.
DR PIR; A22613; A22613.
DR RefSeq; WP_010991819.1; NZ_UAVF01000022.1.
DR PDB; 1BRL; X-ray; 2.40 A; A/C=1-355.
DR PDB; 1LUC; X-ray; 1.50 A; A=1-355.
DR PDB; 3FGC; X-ray; 2.30 A; A/C=1-355.
DR PDBsum; 1BRL; -.
DR PDBsum; 1LUC; -.
DR PDBsum; 3FGC; -.
DR AlphaFoldDB; P07740; -.
DR SMR; P07740; -.
DR MINT; P07740; -.
DR BindingDB; P07740; -.
DR BRENDA; 1.14.14.3; 4778.
DR EvolutionaryTrace; P07740; -.
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; Luciferase-like domain; 1.
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 PANTHER; PTHR30137; LUCIFERASE-LIKE MONOOXYGENASE; 1.
DR PANTHER; PTHR30137:SF8; OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR PRINTS; PR00089; LUCIFERASE.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
DR PROSITE; PS00494; BACTERIAL_LUCIFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Flavoprotein; FMN; Luminescence;
KW Monooxygenase; Oxidoreductase; Photoprotein.
FT CHAIN 1..355
FT /note="Alkanal monooxygenase alpha chain"
FT /id="PRO_0000220172"
FT CONFLICT 17
FT /note="Q -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="T -> K (in Ref. 2; CAA41597)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="P -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="A -> P (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..205
FT /note="QL -> HV (in Ref. 2; CAA41597)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="R -> K (in Ref. 2; CAA41597)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="D -> N (in Ref. 2; CAA41597)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1LUC"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:1LUC"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 83..97
FT /evidence="ECO:0007829|PDB:1LUC"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:1LUC"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:1LUC"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:1LUC"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:1LUC"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1LUC"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 198..214
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1LUC"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 236..259
FT /evidence="ECO:0007829|PDB:1LUC"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:3FGC"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:3FGC"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:1LUC"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 304..318
FT /evidence="ECO:0007829|PDB:1LUC"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 333..346
FT /evidence="ECO:0007829|PDB:1LUC"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1LUC"
SQ SEQUENCE 355 AA; 40153 MW; F915E6BBE41ACEEE CRC64;
MKFGNFLLTY QPPELSQTEV MKRLVNLGKA SEGCGFDTVW LLEHHFTEFG LLGNPYVAAA
HLLGATETLN VGTAAIVLPT AHPVRQAEDV NLLDQMSKGR FRFGICRGLY DKDFRVFGTD
MDNSRALMDC WYDLMKEGFN EGYIAADNEH IKFPKIQLNP SAYTQGGAPV YVVAESASTT
EWAAERGLPM ILSWIINTHE KKAQLDLYNE VATEHGYDVT KIDHCLSYIT SVDHDSNRAK
DICRNFLGHW YDSYVNATKI FDDSDQTKGY DFNKGQWRDF VLKGHKDTNR RIDYSYEINP
VGTPEECIAI IQQDIDATGI DNICCGFEAN GSEEEIIASM KLFQSDVMPY LKEKQ
//
