ID A0A2P6VE73_9CHLO Unreviewed; 605 AA.
AC A0A2P6VE73;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=procollagen-lysine 5-dioxygenase {ECO:0000256|ARBA:ARBA00012264};
DE EC=1.14.11.4 {ECO:0000256|ARBA:ARBA00012264};
GN ORFNames=C2E20_4317 {ECO:0000313|EMBL:PSC72393.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC72393.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC72393.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC72393.1,
RC ECO:0000313|Proteomes:UP000239649};
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 + 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 Evidence={ECO:0000256|ARBA:ARBA00024166};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000256|ARBA:ARBA00009789}.
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:PSC72393.1}.
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DR EMBL; LHPF02000010; PSC72393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6VE73; -.
DR STRING; 554055.A0A2P6VE73; -.
DR Proteomes; UP000239649; Unassembled WGS sequence.
DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR CDD; cd02516; CDP-ME_synthetase; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR HAMAP; MF_00108; IspD; 1.
DR InterPro; IPR001228; IspD.
DR InterPro; IPR034683; IspD/TarI.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR003582; ShKT_dom.
DR NCBIfam; TIGR00453; ispD; 1.
DR PANTHER; PTHR32125; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR32125:SF4; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF01128; IspD; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS51670; SHKT; 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000239649};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 372..518
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 544..584
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
SQ SEQUENCE 605 AA; 65573 MW; 3B50DE8F61626760 CRC64;
MLLAGGVGKR MGASIPKQYL ELRGQPIAIF SMQTFAGMPE VGEIVVVCEP EWRDVFEACY
ARLPRKLPLK FAKPGAERQD SVLSGLQAIQ SSAQLVAIHD SARPLVTAAD TLLCLRDAWE
VGAAVLGVPV KPTIKEVDGD GMVVKTLKRA ALWEVQTPQV IRPALLREGF ELVAREGLEV
TDDVSIIEAL GKPVRITSGS YTNIKVTTPD DMSVAERFLE EAAAAARRAI MPDPLEQARL
EYCEGDPSAK ECKVFDDQLP AAAAVVAAAA RRVPLQGSAA SPRTLLADPT ATGGIAVAAG
NETASCLLAP ECDPARSPRI ETLQEEGRIF LYHNFLTDEE CDHIVRLAEP HLERPGVVET
ETGKEDISNV RTSKGMFLER GQDPIIAGIE ARIAKWTLMP AGNGEGLQVL EYEGHYDYFF
HKEGTENGGN RYLTVLMYLN DVEEGGETCF PNIPAPNGDN GPEFSDCARK VLAAKPKKGN
AVLFHSIKPN GELERLSLHT ACPVTKGIKW STPKWVHVGH YATGDEQPER IEQVTETDLA
YPDCKDKDSA CDSWAGSGEC EGNVAFMIGT PSRPGHCIKA CGKCALFYEY KGEEEALEEA
AADEL
//
