ID   LUCI_VARHI              Reviewed;         555 AA.
AC   P17554;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Luciferin 2-monooxygenase;
DE            EC=1.13.12.6;
DE   AltName: Full=Cypridina-type luciferase;
DE   Flags: Precursor;
OS   Vargula hilgendorfii (Sea firefly) (Cypridina hilgendorfii).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Oligostraca;
OC   Ostracoda; Myodocopa; Myodocopida; Cypridinoidea; Cypridinidae; Vargula.
OX   NCBI_TaxID=6674;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2771943; DOI=10.1073/pnas.86.17.6567;
RA   Thompson E.M., Nagata S., Tsuji F.I.;
RT   "Cloning and expression of cDNA for the luciferase from the marine ostracod
RT   Vargula hilgendorfii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:6567-6571(1989).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cypridina luciferin + O2 = CO2 + hnu + oxidized Cypridina
CC         luciferin; Xref=Rhea:RHEA:22760, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:30212, ChEBI:CHEBI:58006,
CC         ChEBI:CHEBI:58059; EC=1.13.12.6;
CC   -!- PTM: The cysteine residues presumably exist in intramolecular disulfide
CC       bridges.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: 60 kcal/mol are required for the blue emission of light
CC       (460 nm) due to the oxidation of luciferin via a dioxetanone
CC       intermediate, in which the excited state oxyluciferin bound to
CC       luciferase is the emitter.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M25666; AAA30332.1; -; mRNA.
DR   PIR; A33723; A33723.
DR   AlphaFoldDB; P17554; -.
DR   BRENDA; 1.13.12.6; 1799.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0047712; F:Cypridina-luciferin 2-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR   InterPro; IPR001846; VWF_type-D.
DR   Pfam; PF00094; VWD; 2.
DR   SMART; SM00216; VWD; 2.
DR   PROSITE; PS51233; VWFD; 2.
PE   1: Evidence at protein level;
KW   Decarboxylase; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Luminescence; Lyase; Monooxygenase; Oxidoreductase; Photoprotein; Repeat;
KW   Signal.
FT   SIGNAL          1..11
FT                   /evidence="ECO:0000255"
FT   CHAIN           12..555
FT                   /note="Luciferin 2-monooxygenase"
FT                   /id="PRO_0000021626"
FT   DOMAIN          80..266
FT                   /note="VWFD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          319..494
FT                   /note="VWFD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        82..222
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        321..454
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        343..493
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        352..451
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ   SEQUENCE   555 AA;  61627 MW;  2FB150371A80A0DF CRC64;
     MKIIILSVIL AYCVTDNCQD ACPVEAEPPS STPTVPTSCE AKEGECIDTR CATCKRDILS
     DGLCENKPGK TCCRMCQYVI ECRVEAAGYF RTFYGKRFNF QEPGKYVLAR GTKGGDWSVT
     LTMENLDGQK GAVLTKTTLE VAGDVIDITQ ATADPITVNG GADPVIANPF TIGEVTIAVV
     EIPGFNITVI EFFKLIVIDI LGGRSVRIAP DTANKGLISG ICGNLEMNDA DDFTTDADQL
     AIQPNINKEF DGCPFYGNPS DIEYCKGLME PYRAVCRNNI NFYYYTLSCA FAYCMGGEER
     AKHVLFDYVE TCAAPETRGT CVLSGHTFYD TFDKARYQFQ GPCKEILMAA DCYWNTWDVK
     VSHRDVESYT EVEKVTIRKQ STVVDLIVDG KQVKVGGVDV SIPYSSENTS IYWQDGDILT
     TAILPEALVV KFNFKQLLVV HIRDPFDGKT CGICGNYNQD STDDFFDAEG ACALTPNPPG
     CTEEQKPEAE RLCNNLFDSS IDEKCNVCYK PDRIARCMYE YCLRGQQGFC DHAWEFKKEC
     YIKHGDTLEV PPECQ