ID H3B0A4_LATCH Unreviewed; 555 AA.
AC H3B0A4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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|Ensembl:ENSLACP00000015325.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000015325.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000015325.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFYH01114326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01114327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01114328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01114329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01114330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01114331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01114332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01114333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01114334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01114335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3B0A4; -.
DR Ensembl; ENSLACT00000015431.1; ENSLACP00000015325.1; ENSLACG00000013491.2.
DR GeneTree; ENSGT00390000002349; -.
DR HOGENOM; CLU_027679_0_0_1; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000013491; Expressed in muscle tissue and 2 other cell types or tissues.
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:UP000008672};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 141..245
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 63703 MW; 7B036D0F9AE8855B CRC64;
CGGKNPEEDD PHQAPGRKKA REKQAVTAQI SGSVREEAGN GLLREAWRSE TIFSQGGLEL
DSKPFPHCVI PNFLEDNGFL EELRDELLKL NFHQKSNDLY KFKQSDDLKR RKEPHISALR
KVLFEDFRKW LFDVTQIELE STVDISCAKY EHTVPDVLLC HDDELEGRRI AFILYLVPSW
ESSDGGMLDL YSSDVHYQPV QIMKSLLPSW NTLAFFEVSS VSHHQVSEVL SESKSRLSVS
GWFHGSSLER PPRYVEPSLP RTPHLPRDHE VLYEWLNPVY LQTDAQAQIQ EEFEERSEIL
LKNFLQAEKF QQVCEALTNV DMKWILRGPP NKRCYEQVEE GSLPEILRQC MELLHSEPMF
LLLSNFTGLK LHFLASSNEE DEDEEAESSS DSSQHAEASS SRREVAGAPP GANIEVKERD
TELDGQQAVS QLGKRGTEAK ESVPVCRGEL RHWRHGHYTL LHDTDVENAE FALDLLLFCG
CEGWEAEFGG FTSYIAKGED EELLTIYPEN NSLALIYRDK ETLKFVKHVN QRSSQRWIKV
PTSNGFWDFS FAYYE
//