ID A0A1U7R7P2_ALLSI Unreviewed; 645 AA.
AC A0A1U7R7P2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Arachidonate 5-lipoxygenase {ECO:0000313|RefSeq:XP_006014893.1};
GN Name=ALOX5 {ECO:0000313|RefSeq:XP_006014893.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006014893.1};
RN [1] {ECO:0000313|RefSeq:XP_006014893.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_006014893.1; XM_006014831.2.
DR AlphaFoldDB; A0A1U7R7P2; -.
DR STRING; 38654.A0A1U7R7P2; -.
DR GeneID; 102371605; -.
DR KEGG; asn:102371605; -.
DR CTD; 240; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR InParanoid; A0A1U7R7P2; -.
DR OrthoDB; 999249at2759; -.
DR Proteomes; UP000189705; Unplaced.
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; 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; 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:UP000189705}.
FT DOMAIN 1..89
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 89..645
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT BINDING 339
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT BINDING 344
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT BINDING 522
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT SITE 74
FT /note="Essential for stabilizing binding to COTL1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-3"
SQ SEQUENCE 645 AA; 75561 MW; 8E579D67C211F420 CRC64;
MLDMDKGTDY CQYSRRRDLL EVDSYDVTVA EHLGEIQLIK IEKRKYWYLD DWYLRYITVK
TPIGDYLEFP CYRWITDEKE IVLRNGTAKL PRDDKIQILK QHRRKELEDR QKMYRWKEWH
PGFPLSIDAH SHSDLPRDIQ FDNEKGVDFI LNYSKAMENL YVNRFMHMFQ SSWSDFADFE
KIFVRISNTI SEYVMQHWKE DFMFGYQFLN GCNPVMIKRC TEIPKKFPVT TEMVECSLER
NLTLEEEIKQ GNVFIVDYEV LSGIDANKTD PCTIQYLTAP ICLLYKNLEN KIVPIAIQLS
QASGPDNPIF FPSDSTYDWL MAKIWVRSSD FHVHQTVTHL LRTHLVCEVF SIAMFRQLPS
VHPFFKLLVP HMRFTIAINT KAREQLICEC GLFDKANATG GGGHVQMVQR AMKDLTYNSL
CFPEAIKARG MDSKEDIPYY FYRDDGIKVW EAIRSFVEEV IGIYYESDEV VCEDVELQGF
VKDVYVYGMK GNKTSGFPKT IKTREKLSEY LTVVIFTASG QHAAVNFGQY DWCSWIPNSP
PTMRCPPPTE KGTVTIEKIV ETLPDRGRSC WHLGAVWALS QFQENELFLG TYPDEHFVEK
PVKLAMENFR KKLDEIVSFI SERNKNKKLP YYYFSPDRIP NSVAV
//
