ID A0A091ENT2_CORBR Unreviewed; 703 AA.
AC A0A091ENT2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 {ECO:0000256|ARBA:ARBA00040791};
DE EC=1.14.11.4 {ECO:0000256|ARBA:ARBA00012264};
DE AltName: Full=Lysyl hydroxylase 1 {ECO:0000256|ARBA:ARBA00042560};
DE Flags: Fragment;
GN ORFNames=N302_09959 {ECO:0000313|EMBL:KFO59568.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO59568.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO59568.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO59568.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-
CC lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA-
CC COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4;
CC Evidence={ECO:0000256|ARBA:ARBA00024166};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004367}; Lumenal side
CC {ECO:0000256|ARBA:ARBA00004367}. Rough endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00037819}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00037819}; Lumenal side
CC {ECO:0000256|ARBA:ARBA00037819}.
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DR EMBL; KK718900; KFO59568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091ENT2; -.
DR STRING; 85066.A0A091ENT2; -.
DR Proteomes; UP000052976; Unassembled WGS sequence.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IEA:UniProtKB-EC.
DR CDD; cd23004; GT_LH1; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR001006; Procol_lys_dOase.
DR PANTHER; PTHR10730:SF5; PROCOLLAGEN-LYSINE,2-OXOGLUTARATE 5-DIOXYGENASE 1; 1.
DR PANTHER; PTHR10730; PROCOLLAGEN-LYSINE,2-OXOGLUTARATE 5-DIOXYGENASE/GLYCOSYLTRANSFERASE 25 FAMILY MEMBER; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS01325; LYS_HYDROXYLASE; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:KFO59568.1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 612..703
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO59568.1"
FT NON_TER 703
FT /evidence="ECO:0000313|EMBL:KFO59568.1"
SQ SEQUENCE 703 AA; 81754 MW; 7B4B87BF1D64FD28 CRC64;
ENLLVLTVAT KQTEGFQRFR RSAQFFNYKV QVLGLDEEWQ GGDDQQPAGG GQKVRLLKSA
LKQYVDKEDL IILFVESYDV LFASGPTELL KKFKQAKSKV VFSAENYIYP DRKLEAKYPR
VRDGKRFLGS GGFIGYAPNL KKLVEEWKGQ DNDSDQLFYT SIFLDPEKRE SINISLDHRS
RIFQNLNGAL DEIVLKFENS RVRARNLLYD TLPVVIHGNG PTKLQLNYLG NYIPQIWTFE
TGCTVCDEGL RSLTGFKDEA LPMILIGIFI EQPTPFLSQF FLRLRNLHYP KQRIQLFIHN
HEEHHLMEVD SFVEEHGKEY LTVKVIGPED EMENAEARNL GMDLCRKDPD CDYYFSLDAE
VVLKNTETLR ILIEQNKLVI APLVSRHEKL WSNFWGALSP DGYYARSEDY VDIVQRRRIG
LWNVPYISSV YMVKAKALHL ELDQGDLFHS GKLDADMAFC HNVRNQGVFM YLTNRHQFGH
ILSLENYQTS HFHNDLWQIF SNPEDWREKY IHENYTAALK GKLIEMPCPD VYWFPIFTDT
ACDELVEEME HYGQWSTGDN TDSRIQGGYE NVPTIDIHMN QIGFEREWYK FLLDYIAPIT
EKLYPGYYTK TQFELAFVVR YKPDEQPSLM PHHDASTFTI NIALNRVGID YEGGGCRFLR
YNCSIRAPRK GWTLMHPGRL THYHEGLPTT KGTRYIAVSF LDP
//