ID T2MH56_HYDVU Unreviewed; 663 AA.
AC T2MH56;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 03-MAY-2023, entry version 36.
DE SubName: Full=Arachidonate 5-lipoxygenase {ECO:0000313|EMBL:CDG71439.1};
GN Name=ALOX5 {ECO:0000313|EMBL:CDG71439.1};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG71439.1};
RN [1] {ECO:0000313|EMBL:CDG71439.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG71439.1};
RX PubMed=24065732; DOI=10.1093/gbe/evt142;
RA Wenger Y., Galliot B.;
RT "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT bilaterian, euteleostome, and hominidae ancestors.";
RL Genome Biol. Evol. 5:1949-1968(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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR EMBL; HAAD01005207; CDG71439.1; -; mRNA.
DR AlphaFoldDB; T2MH56; -.
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; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
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:SF180; LIPOXYGENASE DOMAIN-CONTAINING PROTEIN; 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; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|PIRSR:PIRSR601885-2};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {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}.
FT DOMAIN 10..126
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 120..663
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-2"
FT BINDING 357
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT BINDING 362
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT BINDING 542
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT BINDING 663
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-1"
FT SITE 111
FT /note="Essential for stabilizing binding to COTL1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601885-3"
SQ SEQUENCE 663 AA; 75339 MW; CD720190F038D214 CRC64;
MGAIESLLKA DLKVVVKTGD VKGAGTDSNV YCCLIDDKGF KSRNILLDVK WRNDFEKGNL
DEFDIRNVSN LSNVVSIELW RDQKGVNDSW FVEYIIVKHS NYTSPFPCNR WIEANKKYVF
YIFNSSLPQY DPCLSQRKQE LEANKVKYIF TNNSEVPKQV ANLPIEENFS FSYKWDVVSR
KIKLITQAKL TGLLTSEKWT TIGDYLKLYK GIFPVPYGFN NWQSDEKFGE QRLRGCNPVL
IQLCKKVPDN FPVTNEMVSQ FLDGFTLEET IEKKQLFIVN LAILENLILE NGRTVCAPMA
LFYANKNGTL LPVAIQLFQK PSEENPIFLP SDPQYTWLLA KMYFNNADCS LHQSCTHLGL
THLLCESICV AAHQNLSLNH PVFQLLAPHF LYIMAINSLA LKNLVSPGGW IDKTMTIGVS
GLMEILKRSW QTFKFDRDCW LPNDISARGV GDTEILKNYF YRDDALLIHE AIVNYVTEIL
SRVYDTPDKL KTDYEVQNWA ICLSDETNGA GIKGVFGNGN FDDLNDLIKF VASVIFICSV
GHAAANFCQY DEYAFPPSYP AMLTGKIPSS KAPLTMQDII NQLPNKETTL DTMAVTKMLS
ERGTNELGTF EIQYLFRPED VAAVERFKSA LAEISNKIKK RNEELSTPYP YLDPKEVPNA
ISI
//
