位置:首页 > 蛋白库 > LUXB_VIBHA
LUXB_VIBHA
ID   LUXB_VIBHA              Reviewed;         324 AA.
AC   P07739;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Alkanal monooxygenase beta chain;
DE            EC=1.14.14.3 {ECO:0000250|UniProtKB:P19840};
DE   AltName: Full=Bacterial luciferase beta chain;
GN   Name=luxB;
OS   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 33843 / NCIMB 1871 / 392 / MAV;
RX   PubMed=3514602; DOI=10.1016/s0021-9258(19)89176-7;
RA   Johnston T.C., Thompson R.B., Baldwin T.O.;
RT   "Nucleotide sequence of the luxB gene of Vibrio harveyi and the complete
RT   amino acid sequence of the beta subunit of bacterial luciferase.";
RL   J. Biol. Chem. 261:4805-4811(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
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   [3]
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   [4]
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).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=9020763; DOI=10.1021/bi962511x;
RA   Tanner J.J., Miller M.D., Wilson K.S., Tu S.C., Krause K.L.;
RT   "Structure of bacterial luciferase beta 2 homodimer: implications for
RT   flavin binding.";
RL   Biochemistry 36:665-672(1997).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX   PubMed=9007973; DOI=10.1002/pro.5560060103;
RA   Thoden J.B., Holden H.M., Fisher A.J., Sinclair J.F., Wesenberg G.,
RA   Baldwin T.O., Rayment I.;
RT   "Structure of the beta 2 homodimer of bacterial luciferase from Vibrio
RT   harveyi: X-ray analysis of a kinetic protein folding trap.";
RL   Protein Sci. 6:13-23(1997).
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:P19840}.
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:P19840};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000269|PubMed:7756289, ECO:0000269|PubMed:8703001}.
CC   -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC       {ECO:0000305}.
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; M10961; AAA88686.1; -; Genomic_DNA.
DR   PIR; A23866; A23866.
DR   RefSeq; WP_010991820.1; NZ_UAVF01000022.1.
DR   PDB; 1BRL; X-ray; 2.40 A; B/D=1-324.
DR   PDB; 1BSL; X-ray; 1.95 A; A/B=1-324.
DR   PDB; 1LUC; X-ray; 1.50 A; B=1-324.
DR   PDB; 1XKJ; X-ray; 2.50 A; A/B=1-324.
DR   PDB; 3FGC; X-ray; 2.30 A; B/D=1-324.
DR   PDBsum; 1BRL; -.
DR   PDBsum; 1BSL; -.
DR   PDBsum; 1LUC; -.
DR   PDBsum; 1XKJ; -.
DR   PDBsum; 3FGC; -.
DR   AlphaFoldDB; P07739; -.
DR   SMR; P07739; -.
DR   MINT; P07739; -.
DR   GeneID; 57823102; -.
DR   BRENDA; 1.14.14.3; 4778.
DR   EvolutionaryTrace; P07739; -.
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; Direct protein sequencing; Flavoprotein; FMN; Luminescence;
KW   Monooxygenase; Oxidoreductase; Photoprotein.
FT   CHAIN           1..324
FT                   /note="Alkanal monooxygenase beta chain"
FT                   /id="PRO_0000220181"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   HELIX           17..32
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   TURN            33..35
FT                   /evidence="ECO:0007829|PDB:1BRL"
FT   STRAND          38..41
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   HELIX           55..65
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   STRAND          67..77
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:1XKJ"
FT   HELIX           83..96
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   STRAND          101..106
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   HELIX           111..116
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..144
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   STRAND          147..150
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:1BSL"
FT   STRAND          170..173
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   HELIX           177..186
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   STRAND          190..192
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:1BSL"
FT   STRAND          225..232
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   HELIX           236..254
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   TURN            255..257
FT                   /evidence="ECO:0007829|PDB:1BSL"
FT   HELIX           260..270
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   STRAND          271..275
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   HELIX           276..290
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   STRAND          293..298
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   HELIX           305..317
FT                   /evidence="ECO:0007829|PDB:1LUC"
FT   HELIX           319..324
FT                   /evidence="ECO:0007829|PDB:3FGC"
SQ   SEQUENCE   324 AA;  36345 MW;  974FF37653C052D3 CRC64;
     MKFGLFFLNF MNSKRSSDQV IEEMLDTAHY VDQLKFDTLA VYENHFSNNG VVGAPLTVAG
     FLLGMTKNAK VASLNHVITT HHPVRVAEEA CLLDQMSEGR FAFGFSDCEK SADMRFFNRP
     TDSQFQLFSE CHKIINDAFT TGYCHPNNDF YSFPKISVNP HAFTEGGPAQ FVNATSKEVV
     EWAAKLGLPL VFRWDDSNAQ RKEYAGLYHE VAQAHGVDVS QVRHKLTLLV NQNVDGEAAR
     AEARVYLEEF VRESYSNTDF EQKMGELLSE NAIGTYEEST QAARVAIECC GAADLLMSFE
     SMEDKAQQRA VIDVVNANIV KYHS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024