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Database: UniProt
Entry: A0A2Y9Q147_DELLE
LinkDB: A0A2Y9Q147_DELLE
Original site: A0A2Y9Q147_DELLE 
ID   A0A2Y9Q147_DELLE        Unreviewed;       710 AA.
AC   A0A2Y9Q147;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=LOW QUALITY PROTEIN: hydroperoxide isomerase ALOXE3 {ECO:0000313|RefSeq:XP_022451420.1};
GN   Name=ALOXE3 {ECO:0000313|RefSeq:XP_022451420.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022451420.1};
RN   [1] {ECO:0000313|RefSeq:XP_022451420.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022451420.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962,
CC         ECO:0000256|RuleBase:RU003974};
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   RefSeq; XP_022451420.1; XM_022595712.2.
DR   STRING; 9749.A0A2Y9Q147; -.
DR   KEGG; dle:111185793; -.
DR   InParanoid; A0A2Y9Q147; -.
DR   OrthoDB; 999249at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; 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; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   PANTHER; PTHR11771:SF184; HYDROPEROXIDE ISOMERASE ALOXE3; 1.
DR   PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR   Pfam; PF00305; Lipoxygenase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PRINTS; PR00087; LIPOXYGENASE.
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   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003974};
KW   Isomerase {ECO:0000313|RefSeq:XP_022451420.1};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003974};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT   DOMAIN          2..118
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          118..710
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
SQ   SEQUENCE   710 AA;  79978 MW;  AF786B15BC0FBDAB CRC64;
     MAVYRVCVGT APYLMAGTLD IFVTLVGTCG ESPKRRLDRV GRGFAPGQVQ KYKVRCSEEL
     GELLLLRLHK ERYAFFPKDS WYCSRICITT PGGTLCHFPC YQWIEGYCTI ELRQGTGGTI
     CQDSLPLLLD HRKWELQAXQ ECYRWQVYAA PGFPGIVGVS SFEEVESDKK FALIKRVPCA
     DQGDSNENRY RPGFPMKTDI PSLLSMEPNI CYSATKTTSL LFNAIPASLG MKLLGLLDRK
     GSWKKLDDIR NIMCCHKTFT SEYVTEHXCE DHFFGYQYLN GVNPVMLHCL SSLPSKLPVT
     NDIVAPSLGP GTCPQTELER GHIFLADYWI PAEVPIHCIN GRPQYAASPL CRLWLNPQGA
     LVPLAIQLSQ TSGPDSPIFL PTDSDWDWLL AKTWVRNSEF LVHENNTHFL CTHLLCEAFA
     VAMLRQLPRC HPIYKLLLPH TRYTLQVNTV ARATLLKPEG LVDKVTSIGR KVLLYLMSTD
     LAHLTYTNFC LPDSLRARGI LDTPNYHYRD NGLKVWVAIE SFVSEIVAYY YPSDASVQQD
     SELQAWVGEI FAQEFLGQES SGFPCRLCTP GELVKLLTAV IFNCSAQHAA VNSGQHDFGA
     WMPNAPXSMR QPPPQTKGTT TLKSYLDTLP EVNTTCNNIL LFWLVSQEPK DQRPLDTYPD
     EHFTEERPLR STAIFQSRLA QISRDIRSER GPGVALYYLD PPLIENSVSI
//
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