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Database: UniProt
Entry: A0A3Q4GUY8_NEOBR
LinkDB: A0A3Q4GUY8_NEOBR
Original site: A0A3Q4GUY8_NEOBR 
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
//
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