ID D2VBE8_NAEGR Unreviewed; 529 AA.
AC D2VBE8;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Proline hydroxylase {ECO:0000313|EMBL:EFC45784.1};
GN ORFNames=NAEGRDRAFT_79305 {ECO:0000313|EMBL:EFC45784.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC45784.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC45784.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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 EMBL; GG738861; EFC45784.1; -; Genomic_DNA.
DR RefSeq; XP_002678528.1; XM_002678482.1.
DR AlphaFoldDB; D2VBE8; -.
DR STRING; 5762.D2VBE8; -.
DR EnsemblProtists; EFC45784; EFC45784; NAEGRDRAFT_79305.
DR GeneID; 8850506; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_79305; -.
DR eggNOG; KOG3844; Eukaryota.
DR InParanoid; D2VBE8; -.
DR OrthoDB; 5480441at2759; -.
DR Proteomes; UP000006671; 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; 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:UP000006671};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 155..263
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..529
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 529 AA; 61876 MW; 6F2AC371ED2AC02F CRC64;
MKRKIEKNQA MKRKQQKKAK AVPKRTAEEE KAYQEYLQNL NLMDHLNAEY SSEEGVQKAK
KTFGENKPFP YLHLKNFFKD LEFVKDVKQE TLALKYWEKN NDLYHFLQTK DLQKNAIVEE
NEHLRKLRDV LYSPSFRGWL EEVCSLKERG IKLNPSIDMF VSCYRDTHHL LCHDDELEKR
RIAYIIYLVP EDWSEADGGH LDLYNCDPKQ MDQPVSIGGS VLPSFNSISF FEVSTISYHR
VREVLRAIDM EEDRIAITGW LYSDTLVERP DYTIEDIAPL TYEEVSTVET PAAHLDVAYW
LGESYVKEDI RKAVNEQFCN ESSIELRSFL SAQKFDTLYE EFKSLKEDQF DFTIPANRRH
FLRLNSEKLE KSSELSKFYE FAKSQVFVDY LKEITSLPIK KINLQGRRFR PGDYALVQNT
PVDEVRLDVL FRLCPKDWDF DFGAGVTYMD EEEELLSILP EPNTISIVLR DTGVQTFVKY
VTHHAPGDVY DFLLTCETEI PEGSEGDWDD DEEGEEGEEE GAEEAEEEE
//
