LILIP_NOSS1
ID LILIP_NOSS1 Reviewed; 773 AA.
AC Q8YK97;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Linolenate 9R-lipoxygenase;
DE EC=1.13.11.61;
DE AltName: Full=NspLOX;
GN OrderedLocusNames=all8020;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OG Plasmid pCC7120gamma.
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=18031288; DOI=10.1042/bj20071277;
RA Lang I., Gobel C., Porzel A., Heilmann I., Feussner I.;
RT "A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC
RT 7120.";
RL Biochem. J. 410:347-357(2008).
CC -!- FUNCTION: Catalyzes the conversion of alpha-linoleate to
CC (9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate in oxylipin
CC biosynthesis. Also converts alpha-linoleate to (9R,10E,12Z)-9-
CC hydroperoxyoctadeca-10,12-dienoate. {ECO:0000269|PubMed:18031288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (9R,10E,12Z,15Z)-9-
CC hydroperoxyoctadeca-10,12,15-trienoate; Xref=Rhea:RHEA:31687,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:63241;
CC EC=1.13.11.61; Evidence={ECO:0000269|PubMed:18031288};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-10. {ECO:0000269|PubMed:18031288};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726, ECO:0000269|PubMed:18031288}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; AP003603; BAB77350.1; -; Genomic_DNA.
DR PIR; AE2553; AE2553.
DR RefSeq; WP_010994078.1; NC_003267.1.
DR AlphaFoldDB; Q8YK97; -.
DR SMR; Q8YK97; -.
DR PeroxiBase; 5629; NOspKatLox01.
DR EnsemblBacteria; BAB77350; BAB77350; BAB77350.
DR KEGG; ana:all8020; -.
DR OMA; WTHELTH; -.
DR OrthoDB; 788329at2; -.
DR BioCyc; MetaCyc:MON-16943; -.
DR BRENDA; 1.13.11.B1; 4371.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000002483; Plasmid pCC7120gamma.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0102300; F:linoleate 9R-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0102299; F:linolenate 9R-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR Pfam; PF00305; Lipoxygenase; 1.
DR SUPFAM; SSF48484; SSF48484; 1.
DR SUPFAM; SSF56634; SSF56634; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis;
KW Lipid metabolism; Metal-binding; Oxidoreductase; Oxylipin biosynthesis;
KW Plasmid; Reference proteome.
FT CHAIN 1..773
FT /note="Linolenate 9R-lipoxygenase"
FT /id="PRO_0000418759"
FT DOMAIN 176..773
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 515
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 520
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 773
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 773 AA; 87860 MW; 13538EBE3024DAB9 CRC64;
MDLNTYLKLL NLLDSESQKI MLELQAMFSA AGLALRGRGT HTDGIIVKGN LTVLHSSDVP
SHSLFTPGKK YDVIFRHANI VGGAKDDALI NGRGSAIRIG NIGDDLSKPR LLDLVLNTGE
VFGLPTARLY HQFFGSDFHQ KSDMLASGSL RRYAVEAALR NPDSFTELYY HTQLCYEWVD
SKKKSRYARF RLLNPNQSTE GGLLDDSVEI GPRLVLPRKR GDTREKNYLR NEFRQRLTDG
NIVEYVLQAQ FRSIEDVAVD CSNIWDPNTY PWLDIAAIVL NQDESENDYY QEIAYNPGNT
HYDLKLPNSY SVDDFASLGV SGALVHYFGS IVRAERTQYL YGSKDDLPGK PVYFPLPVTE
IPSKRFLFLL EKYNFLTDNS YPSDGEHDKI EALVSAMPTT ALDLAVGTTD PTDIPDSYFL
ERRLNGYNPG AIRESSGQEG WTHELTHNLA KYDIKPGLHF PDFVQCRLFV DKQNGVKLHS
IKIDDHEITP CQEQWQYAKR TYLQAEFLSQ ELKLHLARCH FNIEQYVMAI KRRLAPTHPV
RAFINPHLEG LIFINSSAVP KIIGSTGFIP IASMLTQGSI VDVMKNELSK LSYMWNPIAD
LPRDIPGDLF TPAATAYWEL LNNYVEQGLL QPFEDELRTE VNAIQVDELF AELKERSLYS
GDQPPKYDSS ELKSLLMYII YHSSFLHSWA NFKQYDDAGN PNHVSMGDYS QYDQQTQDKI
RFSQRSLTWV LSSIRYNSVA VYGSDLLKQL IREKSSILEP GLPLEDLMMS INI
