ID A0A3Q4BE91_MOLML Unreviewed; 702 AA.
AC A0A3Q4BE91;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
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};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000017305.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000017305.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q4BE91; -.
DR STRING; 94237.ENSMMOP00000017305; -.
DR Ensembl; ENSMMOT00000017593.1; ENSMMOP00000017305.1; ENSMMOG00000013171.1.
DR OMA; CTYYFSM; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0005789; C: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 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};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
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:UP000261620};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 611..702
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 702 AA; 81433 MW; A0FA9AA2578A7C05 CRC64;
MLCLLEKLIV VTVATKETDG FKRFLRSAKH FNYTVLGRGQ KWKGGDYMGA PGGGQKVRLL
KEALEEKEIQ DKIILFIDSY DVVFASGPKE LFKKFQQARH KVVFSSESLI WPDRHLEDKH
PHVREGNRFL GSGGFIGYAA NVKEMVAEWT GEDNESDQLF FTKIYIDPAK RKSINITLDS
KCRLFQNLHG SLDEVVLKFE DGRSRARNLL YNTLPSIIHG NGPTKLQINY LGNYIPNTWA
FETGCMVCHK ELRPLTTLKS EYPLVVIGIF IQQPTPFVTV FFERLLKLQY PKNRLKLFIY
NQEVHHERHV SSFLRDHGRL YQDVKFIGPE EEMDAAASRN MGFDMCRKDK DCEYFFSVDI
EVVLKNENTL KILLEQNLPV VAPMITRAGR LWSNFWGALS EDGYYARSED YVDIVQGRRV
GVWNVPYVSS VYLMKASLLR SELTDYELFN SHSLDPDMAY CHNVRSKGIF MYVTNMHTFG
RILSTENYQT SHLHNDLWQI FVNPLDWQER YIHENYTRIT KDKLIETPCP DVYWFPIFSE
VACNHIVEEM EHFGRWSGGN DTRIQGGYEN VPTIDIHMNQ VNFEKEWHKF LLEYVAPITE
KMYPGYYTKA QFDLAFVVRY KPDEQPSLRP HHDASTFTIN IALNQVGPDY QGGGCRFLRY
DCSIQAPRKG WALMHPGRLT HYHEGLPTTA GVRYIAVSFV DP
//