LUCIF_LINPO
ID LUCIF_LINPO Reviewed; 1241 AA.
AC O77206; Q39912;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Dinoflagellate luciferase;
DE EC=1.13.12.18;
OS Lingulodinium polyedra (Dinoflagellate) (Gonyaulax polyedra).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Gonyaulacales; Lingulodiniaceae;
OC Lingulodinium.
OX NCBI_TaxID=160621;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 115-140 AND 373-383.
RC STRAIN=GP70;
RX PubMed=9256416; DOI=10.1073/pnas.94.17.8954;
RA Li L., Hong R., Hastings J.W.;
RT "Three functional luciferase domains in a single polypeptide chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8954-8958(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 600-1241, AND FUNCTION.
RC STRAIN=GP70;
RX PubMed=7918642; DOI=10.1016/0167-4781(94)90071-x;
RA Bae Y.M., Hastings J.W.;
RT "Cloning, sequencing and expression of dinoflagellate luciferase DNA from a
RT marine alga, Gonyaulax polyedra.";
RL Biochim. Biophys. Acta 1219:449-456(1994).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7197271; DOI=10.1016/s0021-9258(19)68651-5;
RA Dunlap J.C., Hastings J.W.;
RT "The biological clock in Gonyaulax controls luciferase activity by
RT regulating turnover.";
RL J. Biol. Chem. 256:10509-10518(1981).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 866-1239, FUNCTION, SUBCELLULAR
RP LOCATION, ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=15665092; DOI=10.1073/pnas.0409335102;
RA Schultz L.W., Liu L., Cegielski M., Hastings J.W.;
RT "Crystal structure of a pH-regulated luciferase catalyzing the
RT bioluminescent oxidation of an open tetrapyrrole.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1378-1383(2005).
CC -!- FUNCTION: Emits blue light flashes with a wavelength of 475 nm during
CC the night phase. {ECO:0000269|PubMed:15665092,
CC ECO:0000269|PubMed:7197271, ECO:0000269|PubMed:7918642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dinoflagellate luciferin + O2 = H(+) + H2O + hnu + oxidized
CC dinoflagellate luciferin; Xref=Rhea:RHEA:28775, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30212,
CC ChEBI:CHEBI:61708, ChEBI:CHEBI:61796; EC=1.13.12.18;
CC Evidence={ECO:0000269|PubMed:7197271};
CC -!- ACTIVITY REGULATION: Regulated by pH: upon acidification, at a pH of
CC 6.3, dinoflagellate luciferin is released from luciferin-binding
CC protein LBP, allowing the interaction between Dinoflagellate luciferase
CC and its substrate luciferin. {ECO:0000269|PubMed:15665092}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:15665092}. Note=Localizes in scintillons,
CC specialized organelles formed as outpocketings from the cytoplasm into
CC the acidic vacuole.
CC -!- DOMAIN: Composed of 3 homologous Luciferase domains: each of the
CC individual domains are most active at pH 6.3, and there is very little
CC activity at pH 8.0. {ECO:0000269|PubMed:15665092}.
CC -!- MISCELLANEOUS: Dinoflagellate luciferase mediates much of the
CC bioluminescence in ocean surface waters. {ECO:0000305|PubMed:15665092}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Luciferase family.
CC {ECO:0000305}.
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DR EMBL; AF085332; AAC36472.1; -; mRNA.
DR EMBL; L04648; AAA68491.1; -; mRNA.
DR PIR; S50144; S50144.
DR PDB; 1VPR; X-ray; 1.80 A; A=866-1239.
DR PDBsum; 1VPR; -.
DR AlphaFoldDB; O77206; -.
DR SMR; O77206; -.
DR PRIDE; O77206; -.
DR KEGG; ag:AAC36472; -.
DR BioCyc; MetaCyc:MON-20284; -.
DR BRENDA; 1.13.12.18; 2492.
DR EvolutionaryTrace; O77206; -.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0045289; F:luciferin monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0016703; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases); IDA:UniProtKB.
DR GO; GO:0008218; P:bioluminescence; IDA:UniProtKB.
DR Gene3D; 2.40.128.20; -; 3.
DR Gene3D; 4.10.1300.10; -; 3.
DR Gene3D; 4.10.1310.10; -; 3.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR007959; Dino_Luciferase_N.
DR InterPro; IPR044902; Dino_Luciferase_rpt_sf.
DR InterPro; IPR018804; Luciferase_cat.
DR InterPro; IPR044903; Luciferase_hlx-bundle_dom_sf.
DR InterPro; IPR018475; Luciferase_hlx-bundle_domain.
DR Pfam; PF10284; Luciferase_3H; 3.
DR Pfam; PF10285; Luciferase_cat; 3.
DR Pfam; PF05295; Luciferase_N; 1.
DR SUPFAM; SSF50814; SSF50814; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Direct protein sequencing; Luminescence;
KW Oxidoreductase.
FT CHAIN 1..1241
FT /note="Dinoflagellate luciferase"
FT /id="PRO_0000418501"
FT REGION 114..465
FT /note="Luciferase 1"
FT REGION 491..842
FT /note="Luciferase 2"
FT REGION 868..1218
FT /note="Luciferase 3"
FT CONFLICT 737..738
FT /note="LL -> QH (in Ref. 2; AAA68491)"
FT /evidence="ECO:0000305"
FT CONFLICT 756..760
FT /note="MESGH -> ILRPA (in Ref. 2; AAA68491)"
FT /evidence="ECO:0000305"
FT CONFLICT 766..768
FT /note="RRA -> PAR (in Ref. 2; AAA68491)"
FT /evidence="ECO:0000305"
FT CONFLICT 1228
FT /note="M -> I (in Ref. 2; AAA68491)"
FT /evidence="ECO:0000305"
FT STRAND 871..873
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 877..881
FT /evidence="ECO:0007829|PDB:1VPR"
FT TURN 884..887
FT /evidence="ECO:0007829|PDB:1VPR"
FT HELIX 888..893
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 912..914
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 917..920
FT /evidence="ECO:0007829|PDB:1VPR"
FT HELIX 922..930
FT /evidence="ECO:0007829|PDB:1VPR"
FT HELIX 952..965
FT /evidence="ECO:0007829|PDB:1VPR"
FT HELIX 972..976
FT /evidence="ECO:0007829|PDB:1VPR"
FT HELIX 985..991
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 1028..1036
FT /evidence="ECO:0007829|PDB:1VPR"
FT HELIX 1037..1046
FT /evidence="ECO:0007829|PDB:1VPR"
FT HELIX 1052..1062
FT /evidence="ECO:0007829|PDB:1VPR"
FT HELIX 1064..1066
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 1070..1077
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 1080..1084
FT /evidence="ECO:0007829|PDB:1VPR"
FT TURN 1087..1089
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 1090..1098
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 1102..1107
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 1112..1118
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 1121..1131
FT /evidence="ECO:0007829|PDB:1VPR"
FT TURN 1132..1134
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 1136..1147
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 1150..1159
FT /evidence="ECO:0007829|PDB:1VPR"
FT STRAND 1162..1173
FT /evidence="ECO:0007829|PDB:1VPR"
FT HELIX 1186..1189
FT /evidence="ECO:0007829|PDB:1VPR"
FT TURN 1190..1192
FT /evidence="ECO:0007829|PDB:1VPR"
FT TURN 1211..1214
FT /evidence="ECO:0007829|PDB:1VPR"
SQ SEQUENCE 1241 AA; 136889 MW; 4235C5EF63B63D5F CRC64;
MAAQLEQFLV NEGQVDQRAV TYMLKGLQLE SLSDFASFWT SKDYENGVRD DIISKVAPFN
SDLSLPAAKL QVARLRAAWR KAQGKPSAAV PLQSAKPVAG SVVTATKDTG FCEKTGLESG
GVAHGGALNA AQVAHLDEDA FKGGLHRPKF DSEGLHKPHT SGGKTYETGF HYLLEAHELG
GKNADGGFGG PLCADPFSPE IEQLCQALVR EAQDDKTLCF ENFTKPCPQL TKKQVELCKG
FDYGDKTLKL PCGPLPWPAG LPEPGYVPKT NPLHGRWITV SGGQAAFIKE AIKAGMLGAA
ESHKIMADTD HHQTGGMYLR INQNGDVCTV DASVAKFARA KRTWKSGHYF YEPLVSGGNL
LGVWVLPEEY RKIGFFWEME SGRCFRIERR AFERNGLMIM RQATEVAGKI SFVFYVKVSN
DPESKPIPLQ SRDYTALAGL DNVPDSLGNP YTCEAKDLDY PIKRDTWLDK NQEEMLKQRS
IVGTAFAKCC DQGFEAHDNP KGGALTAAHV ESLGKENFKN GLHAPNFHDD GLHKPMEAGG
KVYSTGFHYL LEAHDLGGKN EDGGYGGPLC KDPYGKEVQS MVENLLVQAN VDTTNAFDNF
KQPCPQLTKE QVAMCKGFDY GDKTLKLPCG PLPWPAGLPE PGYVPKTNPL HGRWITVSGG
QVAFIKEAIK SGMLGAAEAK KIIADTDHHQ TGGMYLRINQ YGEVCTVDAS VAKFARAKRT
WKSGHYFYEP LVSGGNLLGV WVLPEEYRKI GFFWEMESGH CFRIERRAFP CGPYMFLRQA
TEVGGKISYV FYVKVSNDPG SKPIPLQSRD YTALAGQDNA PDNLGKPYKC TARDLDAPTK
RDGWLDTNKG AMLDQREKVS KAFAKVCEKG FEAGDNKLGG ALNAKHVEKY GDNFKNGMHK
PEFHEDGLHK PMEVGGKKFE SGFHYLLECH ELGGKNASGG YGGPLCEDPY GSEVQAMTEK
LLKEADSDRT LCFNNFQDPC PQLTKEQVAM CKGFDYGDKT LKLPCGPLPW PAGLPEPGYV
PKTNPLHGRW ITVSGGQAAF IKEAIKSGML GAAEANKIVA DTDHHQTGGM YLRINQFGDV
CTVDASVAKF ARAKRTWKSG HYFYEPLVSG GNLLGVWVLP EEYRKIGFFW EMESGRCFRI
ERRAFPVGPY TFMRQATEVG GKISFVFYVK VSNDPESDPI PLQSRDYTAL AGRDNAPTNL
GKPYPTLAKD LDYPKKRDGW LEKNEKEMLR QRNIVSSTFR S
