PLOD_MIMIV
ID PLOD_MIMIV Reviewed; 895 AA.
AC Q5UQC3; E3VZ93;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Procollagen lysyl hydroxylase and glycosyltransferase;
DE Short=LHGT;
DE EC=1.14.11.4;
DE EC=2.4.1.-;
DE AltName: Full=Lysyl hydroxylase;
DE AltName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase;
GN OrderedLocusNames=MIMI_L230;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4;
RX PubMed=21646533; DOI=10.1073/pnas.1101118108;
RA Boyer M., Azza S., Barrassi L., Klose T., Campocasso A., Pagnier I.,
RA Fournous G., Borg A., Robert C., Zhang X., Desnues C., Henrissat B.,
RA Rossmann M.G., La Scola B., Raoult D.;
RT "Mimivirus shows dramatic genome reduction after intraamoebal culture.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10296-10301(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA / MRNA].
RX PubMed=21375749; DOI=10.1186/1743-422x-8-99;
RA Legendre M., Santini S., Rico A., Abergel C., Claverie J.M.;
RT "Breaking the 1000-gene barrier for Mimivirus using ultra-deep genome and
RT transcriptome sequencing.";
RL Virol. J. 8:99-99(2011).
RN [4]
RP FUNCTION, CHARACTERIZATION, AND MUTAGENESIS OF ASP-250 AND
RP 825-HIS--ASP-827.
RC STRAIN=M4;
RX PubMed=22045808; DOI=10.1074/jbc.m111.309096;
RA Luther K.B., Hulsmeier A.J., Schegg B., Deuber S.A., Raoult D., Hennet T.;
RT "Mimivirus collagen is modified by bifunctional lysyl hydroxylase and
RT glycosyltransferase enzyme.";
RL J. Biol. Chem. 286:43701-43709(2011).
CC -!- FUNCTION: Displays two enzymatic activities involved in procollagen
CC processing. Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in
CC collagens. These hydroxylysines are subsequentially glucosylated by a
CC glucosyltransferase activity. Collagen post-translationally modified is
CC detected in mimivirus virion. {ECO:0000269|PubMed:22045808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-
CC lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA-
CC COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
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DR EMBL; AY653733; AAV50503.1; -; Genomic_DNA.
DR EMBL; HQ336222; ADO18068.1; -; Genomic_DNA.
DR EMBL; JN036606; AEJ34465.1; -; Genomic_DNA.
DR RefSeq; YP_003986726.1; NC_014649.1.
DR PDB; 6AX6; X-ray; 2.24 A; A/B=680-895.
DR PDB; 6AX7; X-ray; 2.00 A; A/B=680-895.
DR PDBsum; 6AX6; -.
DR PDBsum; 6AX7; -.
DR SMR; Q5UQC3; -.
DR CAZy; GT25; Glycosyltransferase Family 25.
DR PRIDE; Q5UQC3; -.
DR GeneID; 9924837; -.
DR KEGG; vg:9924837; -.
DR Proteomes; UP000001134; Genome.
DR Proteomes; UP000201519; Genome.
DR Proteomes; UP000240552; 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:0008475; F:procollagen-lysine 5-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd06532; Glyco_transf_25; 1.
DR InterPro; IPR002654; Glyco_trans_25.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR Pfam; PF01755; Glyco_transf_25; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Transferase; Vitamin C.
FT CHAIN 1..895
FT /note="Procollagen lysyl hydroxylase and
FT glycosyltransferase"
FT /id="PRO_0000164452"
FT DOMAIN 805..895
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..194
FT /note="Lysyl hydroxylase region"
FT REGION 537..895
FT /note="Glucosyl transferase region"
FT ACT_SITE 887
FT /evidence="ECO:0000255"
FT BINDING 825
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 827
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 877
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MUTAGEN 250
FT /note="D->A: Partial loss of glucosyl transferase
FT activity."
FT /evidence="ECO:0000269|PubMed:22045808"
FT MUTAGEN 825..827
FT /note="HHD->SHA: Complete loss of lysyl hydroxylase
FT activity."
FT /evidence="ECO:0000269|PubMed:22045808"
FT TURN 689..692
FT /evidence="ECO:0007829|PDB:6AX7"
FT HELIX 693..700
FT /evidence="ECO:0007829|PDB:6AX7"
FT HELIX 703..706
FT /evidence="ECO:0007829|PDB:6AX7"
FT TURN 707..710
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 724..728
FT /evidence="ECO:0007829|PDB:6AX7"
FT HELIX 732..745
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 770..772
FT /evidence="ECO:0007829|PDB:6AX7"
FT HELIX 773..776
FT /evidence="ECO:0007829|PDB:6AX7"
FT HELIX 779..788
FT /evidence="ECO:0007829|PDB:6AX7"
FT HELIX 790..797
FT /evidence="ECO:0007829|PDB:6AX7"
FT TURN 798..800
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 806..815
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 828..836
FT /evidence="ECO:0007829|PDB:6AX7"
FT TURN 841..843
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 844..846
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 849..851
FT /evidence="ECO:0007829|PDB:6AX7"
FT TURN 852..855
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 865..874
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 877..879
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 882..885
FT /evidence="ECO:0007829|PDB:6AX7"
FT STRAND 887..894
FT /evidence="ECO:0007829|PDB:6AX7"
SQ SEQUENCE 895 AA; 103501 MW; CF68849A39BC5FBF CRC64;
MISRTYVINL ARRPDKKDRI LAEFLKLKEK GVELNCVIFE AVDGNNPEHL SRFNFKIPNW
TDLNSGKPMT NGEVGCALSH WSVWKDVVDC VENGTLDKDC RILVLEDDVV FLDNFMERYQ
TYTSEITYNC DLLYLHRKPL NPYTETKIST HIVKPNKSYW ACAYVITYQC AKKFMNANYL
ENLIPSDEFI PIMHGCNVYG FEKLFSNCEK IDCYAVQPSL VKLTSNAFND SETFHSGSYV
PSNKFNFDTD KQFRIVYIGP TKGNSFHRFT EYCKLYLLPY KVIDEKETND FVSLRSELQS
LSEQDLNTTL MLVVSVNHND FCNTIPCAPT NEFIDKYKQL TTDTNSIVSA VQNGTNKTMF
IGWANKISEF INHYHQKLTE SNAETDINLA NLLLISSISS DFNCVVEDVE GNLFQLINEE
SDIVFSTTTS RVNNKLGKTP SVLYANSDSS VIVLNKVENY TGYGWNEYYG YHVYPVKFDV
LPKIYLSIRI VKNANVTKIA ETLDYPKELI TVSISRSEHD SFYQADIQKF LLSGADYYFY
ISGDCIITRP TILKELLELN KDFVGPLMRK GTESWTNYWG DIDPSNGYYK RSFDYFDIIG
RDRVGCWNVP YLASVYLIKK SVIEQVPNLF TENSHMWNGS NIDMRLCHNL RKNNVFMYLS
NLRPYGHIDD SINLEVLSGV PTEVTLYDLP TRKEEWEKKY LHPEFLSHLQ NFKDFDYTEI
CNDVYSFPLF TPAFCKEVIE VMDKANLWSK GGDSYFDPRI GGVESYPTQD TQLYEVGLDK
QWHYVVFNYV APFVRHLYNN YKTKDINLAF VVKYDMERQS ELAPHHDSST YTLNIALNEY
GKEYTAGGCE FIRHKFIWQG QKVGYATIHA GKLLAYHRAL PITSGKRYIL VSFVN
