ID Q1W5V9_VIBHA Unreviewed; 355 AA.
AC Q1W5V9;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Alkanal monooxygenase {ECO:0000256|RuleBase:RU367112};
DE EC=1.14.14.3 {ECO:0000256|RuleBase:RU367112};
DE AltName: Full=Bacterial luciferase {ECO:0000256|RuleBase:RU367112};
GN Name=luxA {ECO:0000313|EMBL:ABD97811.1};
OS Vibrio harveyi (Beneckea harveyi).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=669 {ECO:0000313|EMBL:ABD97811.1};
RN [1] {ECO:0000313|EMBL:ABD97811.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 15634 {ECO:0000313|EMBL:ABD97811.1};
RA Ranoa D.R.E., Hedreyda C.T.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Light-emitting reaction in luminous bacteria.
CC {ECO:0000256|RuleBase:RU367112}.
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:0000256|ARBA:ARBA00001552,
CC ECO:0000256|RuleBase:RU367112};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870, ECO:0000256|RuleBase:RU367112}.
CC -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010426, ECO:0000256|RuleBase:RU367112}.
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DR EMBL; DQ436496; ABD97811.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1W5V9; -.
DR SMR; Q1W5V9; -.
DR GO; GO:0047646; F:alkanal monooxygenase (FMN-linked) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|RuleBase:RU367112};
KW FMN {ECO:0000256|RuleBase:RU367112};
KW Luminescence {ECO:0000256|ARBA:ARBA00023223,
KW ECO:0000256|RuleBase:RU367112};
KW Monooxygenase {ECO:0000256|RuleBase:RU367112};
KW Oxidoreductase {ECO:0000256|RuleBase:RU367112};
KW Photoprotein {ECO:0000256|ARBA:ARBA00023262,
KW ECO:0000256|RuleBase:RU367112}.
FT DOMAIN 1..321
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
SQ SEQUENCE 355 AA; 40124 MW; F7E4AFE2F5627D80 CRC64;
MKFGNFLLTY QPPELSQTEV MKRLVNLGKA SEGCGFDTVW LLEHHFTEFG LLGNPYVAAA
HLLGATETLN VGTAAIVLPT AHPVRQAEDV NLLDQMSKGR FRFGICRGLY DKDFRVFGTD
MDNSRALMDC WYDLMKEGFN EGYIAADNEH IKFPKIQLNP SAYTQGGAPV YVVAESASTT
EWAAERGLPM ILSWIINTHE KKAQLDLYTK VATEHGYDVT KNDHCLAYIT SVDHDSNRAK
DICRNFLGHW YDSYVNATKI FDDSDQTKGY DFNKGQWRDF VLKGHKDTNR RIDYSYEINP
VGTPEECIAI IQQDIDATGI DNICCGFEAN GSEEEIIASM KLFQSDVMPY LKEKQ
//
