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UniProtKB/Swiss-Prot entry P29236


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LUXC2_PHOLE
Primary accession number P29236
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 38)
Name and origin of the protein
Protein name Acyl-CoA reductase
Synonym EC 1.2.1.50
Gene name
Name: luxC
From
Photobacterium leiognathi [TaxID: 658] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Photobacterium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25521 / L1 / CIP 665;
PubMed=1915359 [NCBI, ExPASy, EBI, Israel, Japan]
Lee C.Y., Szittner R.B., Meighen E.A.;
"The lux genes of the luminous bacterial symbiont, Photobacterium leiognathi, of the ponyfish. Nucleotide sequence, difference in gene organization, and high expression in mutant Escherichia coli.";
Eur. J. Biochem. 201:161-167(1991).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M63594; AAA25616.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S17836; S17836.
3D structure databases
ModBase P29236.
Ontologies
GO
GO:0019109; Molecular function: acyl-CoA reductase activity (inferred from electronic annotation from InterPro).
GO:0050062; Molecular function: long-chain-fatty-acyl-CoA reductase activity (inferred from electronic annotation from EC).
GO:0008218; Biological process: bioluminescence (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR008670; LuxC.
Graphical view of domain structure.
Pfam PF05893; LuxC; 1.
Pfam graphical view of domain structure.
BLOCKS P29236.
ProtoNet P29236.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Luminescence; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   478  478     Acyl-CoA reductase. PRO_0000220197
Sequence information
Length: 478 AA [This is the length of the unprocessed precursor] Molecular weight: 53713 Da [This is the MW of the unprocessed precursor] CRC64: 4716EF699BF7FE4A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIKKIPMIIG GVVQNTSGYG MRELTLNNNK VNIPIITQSD VEAIQSLNIE NKLTINQIVN 

        70         80         90        100        110        120 
FLYTVGQKWK SETYSRRLTY IRDLIKFLGY SQEMAKLEAN WISMILCSKS ALYDIVENDL 

       130        140        150        160        170        180 
SSRHIIDEWI PQGECYVKAL PKGKSVHLLA GNVPLSGVTS ILRAILTKNE CIIKTSSADP 

       190        200        210        220        230        240 
FTATALVNSF IDVDAEHPIT RSISVMYWSH SEDLAIPKQI MSCADVVIAW GGDDAIKWAT 

       250        260        270        280        290        300 
EHAPSHADIL KFGPKKSISI VDNPTDIKAA AIGVAHDICF YDQQACFSTQ DIYYIGDSID 

       310        320        330        340        350        360 
IFFDELAQQL NKYKDILPKG ERNFDEKAAF SLTERECLFA KYKVQKGESQ SWLLTQSPAG 

       370        380        390        400        410        420 
SFGNQPLSRS AYIHQVNDIS EVIPFVHKAV TQTVAIAPWE SSFKYRDILA EHGAERIIEA 

       430        440        450        460        470 
GMNNIFRVGG AHDGMRPLQR LVNYISHERP STYTTKDVSV KIEQTRYLEE DKFLVFVP 

P29236 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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