ID A0A2P6TZZ8_CHLSO Unreviewed; 1040 AA.
AC A0A2P6TZZ8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=PKHD-type hydroxylase ofd1 {ECO:0000313|EMBL:PRW59644.1};
GN ORFNames=C2E21_1575 {ECO:0000313|EMBL:PRW59644.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW59644.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW59644.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRW59644.1}.
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DR EMBL; LHPG02000003; PRW59644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6TZZ8; -.
DR STRING; 3076.A0A2P6TZZ8; -.
DR OrthoDB; 313087at2759; -.
DR Proteomes; UP000239899; Unassembled WGS sequence.
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; 3.60.130.20; Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR043044; TPA1/Ofd1_C.
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:UP000239899};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 117..226
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 980..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1040
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 112951 MW; 9D62A46F71BA33FB CRC64;
MAADDGTVFR AGLLSTGEEL KARYDASKPY PHCVIREFCN PDLLRKVRDE IIENVEATYK
ETDLFKMLQT GDLANMDALP AEQAAKLPTV RKLRDAIYSP EFRAFISHVT GCGELSDQTD
CACNIHPFGG HLLCHDDVIG NRRVSYIVYL TDPDQGWTAE DGGALELYPQ GKDTPHEPDV
IPTATALPLW NSMAFFKVQP GFSFHSIQEV FSQDKPRMSI QGWFHTDQAP DNVELATRSQ
LQLRAGQDTA HDFQPFTGGA PSDELSADDL AALGKYVNPS YLQEENWLKL QAAFEQEGSV
QLQNFLSPAW AEQVSAAIAA ADVAAKAGRG QVPAYDAGIC GGWQAVGPCH KQRYLRYAPV
AANGGDAEGA AAASAVGGLL AQIRDELFST AAFARLLTKF TTIGLEGQQS EVRRFRPGLD
YTVAHYGVLT KDPQLDAVLC FVTSSDSDDK AAWDSGEVGG YEAYLLADDD NEAAEVYKAA
QDDETGVLNV SPAANTLNLV LRDEGLMKFV KYLSAAAPSS RFDIAAVYKP EPDSDEEEEA
AAAADELAAA APRALRRSPM AVYRLLGALG GLLLLLAAGA AAKPAKRSPQ GPNWTEVYNK
LTGRTGRDPN PEFCVIVRTY WGHGQTAGDG GLRRLLRSLQ LQSVQSWEAV LLVLDARPFE
DLHHIVQDFH DDRIWVFAEW IDKAFKPKVG VEWAPGYHGT LYNLTDDAIQ VCPPSTRWLV
VTNGDNEYAD NFMQLVKDGG KGADLVAVDF YSRYQRPTAP SCERFAAIEG APPCKTNRLR
WCHTDLGANA ISYQRFQKEG RRFGTLGAVS GGLEAEHFDG VMMQALMAAN WSVQHLEGVC
PFNHAPSFQS CGWSGGVWDD RDIVSWETAG GRCLTPAEAA AVLVEDKEAE EVLIQASSDG
NATAYEGVQP ESLRVRCLRK RHYMRDDVLG AAVEWFNALC VDDYDLPAFR QWQAAQADLA
AAGGDGEGAA AGDVAARAAE AAKQQQAAAA GQGAGEDGEE VEDFYALQDE FYKEPAGKAA
AEGQQPQDGE EEDAPTATER
//
