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UniProtKB/Swiss-Prot entry P09186


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

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Entry information
Entry name LOX3_SOYBN
Primary accession number P09186
Secondary accession number Q39838
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 86)
Name and origin of the protein
Protein name Seed lipoxygenase-3
Synonyms L-3
EC 1.13.11.12
Gene name
Name: LOX1.3
Synonyms: LOX3
From
Glycine max (Soybean) [TaxID: 3847] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE.
Yenofsky R.L., Fine M., Liu C.;
"Isolation and characterization of a soybean (Glycine max) lipoxygenase-3 gene.";
Mol. Gen. Genet. 211:215-222(1988).
[2]
SEQUENCE REVISION.
Yenofsky R.L.;
Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE, AND MUTAGENESIS OF ASN-713.
STRAIN=cv. Provar;
DOI=10.1021/bi00254a010; PubMed=7999759 [NCBI, ExPASy, EBI, Israel, Japan]
Kramer J.A., Johnson K.R., Dunham W.R., Sands R.H., Funk M.O. Jr.;
"Position 713 is critical for catalysis but not iron binding in soybean lipoxygenase 3.";
Biochemistry 33:15017-15022(1994).
[4]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
STRAIN=cv. Provar;
DOI=10.1002/(SICI)1097-0134(199709)29:1<15::AID-PROT2>3.3.CO;2-F; PubMed=9294864 [NCBI, ExPASy, EBI, Israel, Japan]
Skrzypczak-Jankun E., Amzel L.M., Kroa B.A., Funk M.O. Jr.;
"Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme.";
Proteins 29:15-31(1997).
[5]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
STRAIN=cv. Provar;
DOI=10.1021/bi981989t; PubMed=9922163 [NCBI, ExPASy, EBI, Israel, Japan]
Pham C., Jankun J., Skrzypczak-Jankun E., Flowers R.A., Funk M.O. Jr.;
"Structural and thermochemical characterization of lipoxygenase-catechol complexes.";
Biochemistry 37:17952-17957(1998).
[6]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON IONS AND SUBSTRATE.
STRAIN=cv. Provar;
DOI=10.1021/ja011759t; PubMed=11686682 [NCBI, ExPASy, EBI, Israel, Japan]
Skrzypczak-Jankun E., Bross R.A., Carroll R.T., Dunham W.R., Funk M.O. Jr.;
"Three-dimensional structure of a purple lipoxygenase.";
J. Am. Chem. Soc. 123:10814-10820(2001).
[7]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH IRON IONS AND CURCUMIN.
PubMed=12792803 [NCBI, ExPASy, EBI, Israel, Japan]
Skrzypczak-Jankun E., Zhou K., McCabe N.P., Selman S.H., Jankun J.;
"Structure of curcumin in complex with lipoxygenase and its significance in cancer.";
Int. J. Mol. Med. 12:17-24(2003).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH IRON IONS AND THE INHIBITOR EPIGALLO-CATECHIN.
PubMed=12964012 [NCBI, ExPASy, EBI, Israel, Japan]
Skrzypczak-Jankun E., Zhou K., Jankun J.;
"Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead.";
Int. J. Mol. Med. 12:415-420(2003).
[9]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH IRON IONS AND 4-NITROCATECHOL.
DOI=10.1107/S0907444904000861; PubMed=14993710 [NCBI, ExPASy, EBI, Israel, Japan]
Skrzypczak-Jankun E., Borbulevych O.Y., Jankun J.;
"Soybean lipoxygenase-3 in complex with 4-nitrocatechol.";
Acta Crystallogr. D 60:613-615(2004).
[10]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH IRON IONS AND PROTOCATECHUIC ACID.
DOI=10.1002/prot.10579; PubMed=14705020 [NCBI, ExPASy, EBI, Israel, Japan]
Borbulevych O.Y., Jankun J., Selman S.H., Skrzypczak-Jankun E.;
"Lipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 A resolution.";
Proteins 54:13-19(2004).
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
X06928; CAA30016.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13302; CAA31664.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50081; AAB41272.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S01864; S01864.
UniGene Gma.30739
3D structure databases
PDB
1HU9; X-ray; 2.20 A; A=1-857.[ExPASy / RCSB / EBI]
1IK3; X-ray; 2.00 A; A=1-857.[ExPASy / RCSB / EBI]
1JNQ; X-ray; 2.10 A; A=1-857.[ExPASy / RCSB / EBI]
1LNH; X-ray; 2.60 A; A=1-857.[ExPASy / RCSB / EBI]
1N8Q; X-ray; 2.10 A; A=1-857.[ExPASy / RCSB / EBI]
1NO3; X-ray; 2.15 A; A=1-857.[ExPASy / RCSB / EBI]
1ROV; X-ray; 2.00 A; A=1-857.[ExPASy / RCSB / EBI]
1RRH; X-ray; 2.00 A; A=1-857.[ExPASy / RCSB / EBI]
1RRL; X-ray; 2.09 A; A/B=1-857.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1HU9; -.
1IK3; -.
1JNQ; -.
1LNH; -.
1N8Q; -.
1NO3; -.
1ROV; -.
1RRH; -.
1RRL; -.
ModBase P09186.
Family and domain databases
InterPro IPR000907; LipOase.
IPR013819; LipOase_C.
IPR001024; LipOase_LH2.
IPR001246; LipOase_pln.
Graphical view of domain structure.
Gene3D G3DSA:2.60.60.20; Lipase_LipOase; 1.
PANTHER PTHR11771; LipOase; 1.
Pfam PF00305; Lipoxygenase; 1.
PF01477; PLAT; 1.
Pfam graphical view of domain structure.
PRINTS PR00087; LIPOXYGENASE.
PR00468; PLTLPOXGNASE.
SMART SM00308; LH2; 1.
SMART graphical view of domain structure.
PROSITE PS00711; LIPOXYGENASE_1; 1.
PS00081; LIPOXYGENASE_2; 1.
PS51393; LIPOXYGENASE_3; 1.
PS50095; PLAT; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P09186.
Other
LinkHub P09186; -.
ProtoNet P09186.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Iron; Lipid synthesis; Metal-binding; Oxidoreductase; Oxylipin biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   857  857     Seed lipoxygenase-3. PRO_0000220719
DOMAIN   38   163  126     PLAT. 
DOMAIN   166   857  692     Lipoxygenase. 
METAL   518   518        Iron; catalytic. 
METAL   523   523        Iron; catalytic. 
METAL   709   709        Iron; catalytic. 
METAL   713   713        Iron; catalytic. 
METAL   857   857        Iron; via carboxylate; catalytic. 
VARIANT   25    25  1     H -> D (in strain: cv. Provar). 
VARIANT   57    57  1     P -> S (in strain: cv. Provar). 
VARIANT   112   112  1     L -> P (in strain: cv. Provar). 
VARIANT   201   201  1     V -> I (in strain: cv. Provar). 
VARIANT   382   382  1     E -> D (in strain: cv. Provar). 
VARIANT   428   428  1     G -> D (in strain: cv. Provar). 
VARIANT   630   630  1     A -> T (in strain: cv. Provar). 
MUTAGEN   713   713        N->A,S: No loss of iron-binding; loss of catalytic activity. 
MUTAGEN   713   713        N->H: No loss of iron-binding; no change in catalytic activity. 
STRAND   10    20  11      
HELIX   21    24  4      
TURN   26    28  3      
HELIX   40    42  3      
STRAND   44    47  4      
HELIX   50    53  4      
TURN   54    57  4      
STRAND   58    68  11      
STRAND   70    72  3      
STRAND   74    81  8      
STRAND   96   105  10      
HELIX   107   109  3      
STRAND   112   119  8      
STRAND   121   123  3      
STRAND   125   133  9      
STRAND   135   137  3      
STRAND   141   149  9      
HELIX   152   154  3      
STRAND   160   162  3      
TURN   169   171  3      
HELIX   174   188  15      
HELIX   213   215  3      
STRAND   224   230  7      
HELIX   269   271  3      
HELIX   273   282  10      
HELIX   284   290  7      
TURN   291   295  5      
HELIX   304   308  5      
HELIX   309   311  3      
HELIX   319   322  4      
STRAND   325   328  4      
HELIX   331   334  4      
STRAND   339   341  3      
TURN   349   351  3      
HELIX   357   359  3      
HELIX   361   370  10      
STRAND   382   384  3      
STRAND   391   397  7      
STRAND   408   410  3      
HELIX   415   420  6      
STRAND   424   429  6      
HELIX   430   433  4      
HELIX   434   436  3      
HELIX   437   440  4      
TURN   441   444  4      
STRAND   449   456  8      
STRAND   462   472  11      
STRAND   476   479  4      
STRAND   482   486  5      
STRAND   490   492  3      
HELIX   493   515  23      
HELIX   516   522  7      
HELIX   523   536  14      
HELIX   542   547  6      
HELIX   548   551  4      
HELIX   554   564  11      
HELIX   571   575  5      
HELIX   579   581  3      
HELIX   582   590  9      
HELIX   595   598  4      
HELIX   600   606  7      
STRAND   609   612  4      
STRAND   619   625  7      
HELIX   628   648  21      
TURN   649   651  3      
HELIX   655   659  5      
HELIX   662   673  12      
TURN   674   676  3      
HELIX   677   679  3      
HELIX   691   705  15      
HELIX   707   713  7      
HELIX   716   720  5      
TURN   723   725  3      
HELIX   740   747  8      
HELIX   749   754  6      
HELIX   760   773  14      
TURN   783   785  3      
HELIX   795   818  24      
HELIX   825   827  3      
TURN   828   832  5      
STRAND   844   846  3      
STRAND   852   854  3      
Sequence information
Length: 857 AA [This is the length of the unprocessed precursor] Molecular weight: 96758 Da [This is the MW of the unprocessed precursor] CRC64: 5DFC33D0F6FD32F0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLGGLLHRGH KIKGTVVLMR KNVLHVNSVT SVGGIIGQGL DLVGSTLDTL TAFLGRPVSL 

        70         80         90        100        110        120 
QLISATKADA NGKGKLGKAT FLEGIITSLP TLGAGQSAFK INFEWDDGSG ILGAFYIKNF 

       130        140        150        160        170        180 
MQTEFFLVSL TLEDIPNHGS IHFVCNSWIY NAKLFKSDRI FFANQTYLPS ETPAPLVKYR 

       190        200        210        220        230        240 
EEELHNLRGD GTGERKEWER VYDYDVYNDL GDPDKGENHA RPVLGGNDTF PYPRRGRTGR 

       250        260        270        280        290        300 
KPTRKDPNSE SRSNDVYLPR DEAFGHLKSS DFLTYGLKSV SQNVLPLLQS AFDLNFTPRE 

       310        320        330        340        350        360 
FDSFDEVHGL YSGGIKLPTD IISKISPLPV LKEIFRTDGE QALKFPPPKV IQVSKSAWMT 

       370        380        390        400        410        420 
DEEFAREMLA GVNPNLIRCL KEFPPRSKLD SQVYGDHTSQ ITKEHLEPNL EGLTVDEAIQ 

       430        440        450        460        470        480 
NKRLFLLGHH DPIMPYLRRI NATSTKAYAT RTILFLKNDG TLRPLAIELS LPHPQGDQSG 

       490        500        510        520        530        540 
AFSQVFLPAD EGVESSIWLL AKAYVVVNDS CYHQLVSHWL NTHAVVEPFI IATNRHLSVV 

       550        560        570        580        590        600 
HPIYKLLHPH YRDTMNINGL ARLSLVNDGG VIEQTFLWGR YSVEMSAVVY KDWVFTDQAL 

       610        620        630        640        650        660 
PADLIKRGMA IEDPSCPHGI RLVIEDYPYA VDGLEIWDAI KTWVHEYVFL YYKSDDTLRE 

       670        680        690        700        710        720 
DPELQACWKE LVEVGHGDKK NEPWWPKMQT REELVEACAI IIWTASALHA AVNFGQYPYG 

       730        740        750        760        770        780 
GLILNRPTLS RRFMPEKGSA EYEELRKNPQ KAYLKTITPK FQTLIDLSVI EILSRHASDE 

       790        800        810        820        830        840 
VYLGERDNPN WTSDTRALEA FKRFGNKLAQ IENKLSERNN DEKLRNRCGP VQMPYTLLLP 

       850 
SSKEGLTFRG IPNSISI 

P09186 in FASTA format

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