ID A0A3Q4GUY8_NEOBR Unreviewed; 524 AA.
AC A0A3Q4GUY8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=hypoxia-inducible factor-proline dioxygenase {ECO:0000256|ARBA:ARBA00039004};
DE EC=1.14.11.29 {ECO:0000256|ARBA:ARBA00039004};
GN Name=EGLN2 {ECO:0000313|Ensembl:ENSNBRP00000007492.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000007492.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000007492.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[hypoxia-inducible factor alpha
CC subunit] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[hypoxia-
CC inducible factor alpha subunit]; Xref=Rhea:RHEA:48400, Rhea:RHEA-
CC COMP:12093, Rhea:RHEA-COMP:12094, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.29;
CC Evidence={ECO:0000256|ARBA:ARBA00035981};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR AlphaFoldDB; A0A3Q4GUY8; -.
DR Ensembl; ENSNBRT00000007702.1; ENSNBRP00000007492.1; ENSNBRG00000005857.1.
DR GeneTree; ENSGT00940000160655; -.
DR OMA; KGQEREC; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000005857; Expressed in muscle tissue and 9 other cell types or tissues.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR12907; EGL NINE HOMOLOG-RELATED; 1.
DR PANTHER; PTHR12907:SF6; PROLYL HYDROXYLASE EGLN2; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580}.
FT DOMAIN 407..505
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 56385 MW; 7D34007D5D2E6E63 CRC64;
MESLEQTDLV NPARGSVAVS HSQDRGANSR QFVSGPTEIH HTHRTDMGLN GLCAAPVGSP
TAAELLADLA SQTDSPGITT PTKQCKTGVP LYNGGVVSPS ATVEGNHSGI LAQTPNGYPA
QVTGVEGQTE GPGYPLTSRA CLMENGDWTA HEKHPSIMRR LNGDLKTRQA QQQKKRCGEN
REIGPETVNS QSMGSAGPGG SMDPVFASGD SDWKRRRLVD GGVASKSTET SRVARAVAPL
SVAVNCGNSS HSNQLASLTH AAPHNNQHSG HSKVASSGLS AAPGVHAARK PPLPAGTGWS
AEHIAKQYIV PCMRYYGICV KDNFLGCQLG DRVLEEVETL NQNGKFRGGQ LVSQKNIPSL
NIRGDQIAWV EGKEPGCENI GVLMAHIDEA VMYSSANGQL GNCVINGRTK AMVACYPGNG
AGYVRHIDNP NGDGRCITCI YYLNKNWDAK KQGGLLQIYP EGKNVVAKVE PLFDRLLIFW
SDRRNPHEVR PAYSTRYAIT VWYFDAKERA EAKEKYRLGE FLFS
//