ID S7MEN5_MYOBR Unreviewed; 739 AA.
AC S7MEN5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 03-MAY-2023, entry version 35.
DE SubName: Full=Arachidonate 5-lipoxygenase {ECO:0000313|EMBL:EPQ01640.1};
GN ORFNames=D623_10006732 {ECO:0000313|EMBL:EPQ01640.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ01640.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR601885-1};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000256|PIRSR:PIRSR601885-1};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family.
CC {ECO:0000256|RuleBase:RU003974}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR EMBL; KE161080; EPQ01640.1; -; Genomic_DNA.
DR AlphaFoldDB; S7MEN5; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR GO; GO:0034440; P:lipid oxidation; IEA:InterPro.
DR Gene3D; 3.10.450.60; -; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001885; LipOase_mml.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF5; POLYUNSATURATED FATTY ACID 5-LIPOXYGENASE; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00467; MAMLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF48484; Lipoxigenase; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR601885-2};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601885-1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601885-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003974};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT DOMAIN 1..93
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 93..739
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT BINDING 433
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT BINDING 438
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT BINDING 616
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT BINDING 739
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT SITE 78
FT /note="Essential for stabilizing binding to COTL1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-3"
SQ SEQUENCE 739 AA; 85469 MW; F1253D61CA2D0B7C CRC64;
MNSVPSTGPT GMLRALGSAA EGKLRVDSYD VTVDEELGEI QLIKIEKRKY WLHDDWYLKY
VTLKTPSGDY IEFPCYRWLT GDGEVVLRDG RAKLSRDDQI HILKQHRRQE LDTRQKQYRW
MEWNPGFPLS IDAKCHRDLP RDIQFDSEKG VDFVLNYSKA MENLFVNRFM HMFQSSWSDF
ADFEKIFVKI SNTISGEMEN LFVNRFMHMF QSSWSDFADF EKIFVKISNT ISGAPRMAQS
SLGIAYSLHL MENLFVNRFM HMFQSSWSDF ADFEKIFVKI SNTISERVMN HWQEDLMFGY
QFLNGCNPVL IQRCTKLPEK LPVTTEMVEC SLERQLTLEQ EIEQGNVFIV DFELLDGIDA
NKTDPCTMQF LAAPICLLYK NLVNKMVPIA IQLNQVPGEE NPIFLPSDAK YDWLLAKIWV
RSSDFHIHQT VTHLLRTHLV SEVFGIAMYR QLPAVHPIFK LLVAHVRFTI AINTKAREQL
ICEYGLFDKA NATGGGGHVQ MVQKAMQNLT YTSLCFPEAI KARGMDSTED IPYYFYRDDG
LLVWEAIRAF TADVVGIYYE NDQVVEEDQE LQDFVKDVYV YGMRGRKASG FPKSIKTREK
LSEYLTVVIF TASAQHAAVN FGQYDWCSWI PNAPPTMRAP PPTAKGVVTI EQIVDTLPDR
GRSCWHLGAV WALSQFQENE LFLGMYPEEH FTEKPVKEAM TRFRKNLDTI VSVIAERNKN
KKLPYYYLSP DRIPNSVAI
//
