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Database: UniProt
Entry: A0A091ENT2_CORBR
LinkDB: A0A091ENT2_CORBR
Original site: A0A091ENT2_CORBR 
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
//
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