ID A0A2Y9LPM4_DELLE Unreviewed; 551 AA.
AC A0A2Y9LPM4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Prolyl 3-hydroxylase OGFOD1 {ECO:0000256|ARBA:ARBA00016364};
DE AltName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00031489};
DE AltName: Full=uS12 prolyl 3-hydroxylase {ECO:0000256|ARBA:ARBA00029938};
GN Name=OGFOD1 {ECO:0000313|RefSeq:XP_022411679.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022411679.1};
RN [1] {ECO:0000313|RefSeq:XP_022411679.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022411679.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC Evidence={ECO:0000256|ARBA:ARBA00001792};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the TPA1 family.
CC {ECO:0000256|ARBA:ARBA00007443}.
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DR RefSeq; XP_022411679.1; XM_022555971.2.
DR AlphaFoldDB; A0A2Y9LPM4; -.
DR Proteomes; UP000248483; Unplaced.
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:0031543; F:peptidyl-proline dioxygenase activity; IEA:UniProt.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR PANTHER; PTHR12117; HISTONE ACETYLTRANSFERASE COMPLEX; 1.
DR PANTHER; PTHR12117:SF0; PROLYL 3-HYDROXYLASE OGFOD1; 1.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
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:UP000248483};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 134..239
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 372..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 63292 MW; 1DAD3D6DA21582B8 CRC64;
MSGKRPAEPV PGRAGKKGKK EVMAKFSDAV TEETLKKQVA EAWSRRTPFR HEAIVMDMDP
FLHCVIPNFI QSENFLEGLQ KELLNLDFHE KYNDLYKFQQ SDDLKKRREP HICALRKILF
EHFRAWLSDI SKIDLESTID MSCAKYEFSD ALLCHDDELE GRRIAFILYL VPPWDRSLGG
TLDLYNVDEH FQPKQIVKSL IPSWNTLVFF EVSPVSFHQV SEVLSEEKSR LSISGWFHGP
LLTRPPTYFE PLIPRSPHVP QDHEILYDWI NPTYLDMEYQ VQIQEEFEES SEILLKEFLK
PEKFAEVCEA LEKGDVEWSN RGPPNKRFYE KAEESKLPDI LKDCMALFRS EAMFLLLSNF
TGLKLHFLAP SEEGELEDKK EGEAASAAEN TEEGPSRSSE PESRQVAISN SSQQSGEQVD
PEPEENDAKK ESSVPTCQGE LRHWKTGHYT LIHDNSKTEF ALDLLFYCGC EGWEPEYGGF
TSYIAKGEDE EVPEQHHSAP FRRPHVQNQE AATPASRSPS HASFSTTQNL FLLHRQASET
EFGSRTTLHL L
//
