ID A0A1D6GFB9_MAIZE Unreviewed; 358 AA.
AC A0A1D6GFB9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN ORFNames=ZEAMMB73_Zm00001d013053 {ECO:0000313|EMBL:AQK62266.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK62266.1};
RN [1] {ECO:0000313|EMBL:AQK62266.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK62266.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00024151};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the P4HA family.
CC {ECO:0000256|ARBA:ARBA00006511}.
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DR EMBL; CM000781; AQK62266.1; -; Genomic_DNA.
DR EMBL; CM000781; AQK62268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6GFB9; -.
DR SMR; A0A1D6GFB9; -.
DR STRING; 4577.A0A1D6GFB9; -.
DR InParanoid; A0A1D6GFB9; -.
DR ExpressionAtlas; A0A1D6GFB9; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IBA:GO_Central.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
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 InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR10869:SF222; PROCOLLAGEN-PROLINE 4-DIOXYGENASE; 1.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF01549; ShK; 1.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00254; ShKT; 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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..358
FT /note="procollagen-proline 4-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010804419"
FT DOMAIN 179..301
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 316..356
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
SQ SEQUENCE 358 AA; 38926 MW; 098ADE70EA41FAE2 CRC64;
MAPPLALLLL AAIVLSRAVS HAHGGGGGFY DPASVTQLSS RPRAFLYSGF LSDTECDHLV
SLVGWVGVGF ANRPFCSAAA RVVAMIRGAL TYGAVSILLS VGFQAKGSME KSMVADNDSG
KSVASQARTS SGTFLAKREL LMWGTDIYLF MLSPPQPKDE IVSAIEKRVA AWTFLPEENA
ESLQVLRYET GQKYDAHFDY FHDRNNLKLG GQRVATVLMY LTDVNKGGET VFPNAEGSHL
QYKDETWSEC SRSGLAVKPK KGDALLFFNL HVNATADTGS LHGSCPVIEG EKWSATKWIH
VRSFDNPPDV RTDAPCSDDK ELCPRWAAIG ECHRNPTYMV GTKDTLGFCR KSCGICDA
//