ID   P4H_MIMIV               Reviewed;         242 AA.
AC   Q5UP57;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   23-FEB-2022, entry version 69.
DE   RecName: Full=Putative prolyl 4-hydroxylase;
DE            Short=4-PH;
DE            EC=1.14.11.2;
DE   AltName: Full=Procollagen-proline,2-oxoglutarate-4-dioxygenase;
GN   OrderedLocusNames=MIMI_L593;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA   Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA   Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT   "Mimivirus giant particles incorporate a large fraction of anonymous and
RT   unique gene products.";
RL   J. Virol. 80:11678-11685(2006).
CC   -!- FUNCTION: May catalyze the post-translational formation of 4-
CC       hydroxyproline in -Xaa-Pro-Gly- sequences in the 6 collagen-like
CC       proteins of Mimivirus. {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC         trans-4-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:18945, Rhea:RHEA-
CC         COMP:11676, Rhea:RHEA-COMP:11680, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.2;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16971431}.
CC   -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50856.1; -; Genomic_DNA.
DR   RefSeq; YP_003987108.1; NC_014649.1.
DR   SMR; Q5UP57; -.
DR   GeneID; 9925229; -.
DR   KEGG; vg:9925229; -.
DR   Proteomes; UP000001134; Genome.
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:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR045054; P4HA-like.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   PANTHER; PTHR10869; PTHR10869; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW   Virion; Vitamin C.
FT   CHAIN           1..242
FT                   /note="Putative prolyl 4-hydroxylase"
FT                   /id="PRO_0000206660"
FT   DOMAIN          128..238
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   242 AA;  27901 MW;  EF3D0F965EC41C2A CRC64;
     MKTVTIITII VVIIVVILII MVLSKSCVSH FRNVGSLNSR DVNLKDDFSY ANIDDPYNKP
     FVLNNLINPT KCQEIMQFAN GKLFDSQVLS GTDKNIRNSQ QMWISKNNPM VKPIFENICR
     QFNVPFDNAE DLQVVRYLPN QYYNEHHDSC CDSSKQCSEF IERGGQRILT VLIYLNNEFS
     DGHTYFPNLN QKFKPKTGDA LVFYPLANNS NKCHPYSLHA GMPVTSGEKW IANLWFRERK
     FS