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Database: UniProt
Entry: A0A2G9HIQ9_9LAMI
LinkDB: A0A2G9HIQ9_9LAMI
Original site: A0A2G9HIQ9_9LAMI 
ID   A0A2G9HIQ9_9LAMI        Unreviewed;       293 AA.
AC   A0A2G9HIQ9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Prolyl 4-hydroxylase alpha subunit {ECO:0000313|EMBL:PIN17421.1};
DE            EC=1.14.11.2 {ECO:0000313|EMBL:PIN17421.1};
GN   ORFNames=CDL12_09907 {ECO:0000313|EMBL:PIN17421.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN17421.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
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   -!- 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:PIN17421.1}.
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DR   EMBL; NKXS01001671; PIN17421.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9HIQ9; -.
DR   STRING; 429701.A0A2G9HIQ9; -.
DR   OrthoDB; 5488227at2759; -.
DR   Proteomes; UP000231279; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR   GO; GO:0019748; P:secondary metabolic process; IEA:UniProt.
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   PANTHER; PTHR10869:SF159; PROLYL 4-HYDROXYLASE 13; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:PIN17421.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          166..286
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   293 AA;  32935 MW;  7332E632B0010245 CRC64;
     MKIKGSKIGG GNRVSLGLPS IFLLCLFFFL AGFFGSSLFS QQETPGNIKP LMRETAEEKK
     IEFEALQNGE TGEESVEAIP FQILSWYPRA LYFPNFATAE HCQSIIEMAR AHLKPSSLAL
     REGETAENTK GIRTSSGMFI SASEDKTGIL DQIEAKIAKA TMIPKTHGES FNVLRYEIGQ
     RYHSHYDAFN PAEYGPQKSQ RIASFLLYLS DVEEGGETMF PFENEQNMDA NYDFRKCVGL
     KVKPHRGDGL LFYSLFPNGT IDPTSLHGSC PVIKGEKWVA TKWIRDQEQD EEY
//
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