ID A0A0H4VBP9_9SPHN Unreviewed; 218 AA.
AC A0A0H4VBP9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Prolyl 4-hydroxylase, alpha subunit {ECO:0000313|EMBL:AKQ42077.1};
GN ORFNames=CP97_08680 {ECO:0000313|EMBL:AKQ42077.1};
OS Aurantiacibacter atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1648404 {ECO:0000313|EMBL:AKQ42077.1, ECO:0000313|Proteomes:UP000059113};
RN [1] {ECO:0000313|EMBL:AKQ42077.1, ECO:0000313|Proteomes:UP000059113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RX PubMed=26220886; DOI=10.1099/ijsem.0.000481;
RA Zhuang L., Liu Y., Wang L., Wang W., Shao Z.;
RT "Erythrobacter atlanticus sp. nov., a bacterium from ocean sediment able to
RT degrade polycyclic aromatic hydrocarbons.";
RL Int. J. Syst. Evol. Microbiol. 65:3714-3719(2015).
RN [2] {ECO:0000313|Proteomes:UP000059113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RA Zhuang L., Liu Y., Shao Z.;
RT "The complete genome sequence of Erythrobacter sp. s21-N3.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; CP011310; AKQ42077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4VBP9; -.
DR STRING; 1648404.CP97_08680; -.
DR KEGG; ery:CP97_08680; -.
DR PATRIC; fig|1648404.4.peg.1805; -.
DR OrthoDB; 269774at2; -.
DR Proteomes; UP000059113; Chromosome.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000059113};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 105..214
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 218 AA; 24436 MW; 70E5DDDC6EFA85CA CRC64;
MPNPSSIQSG VPGETSAAML LEHQGVRQVP SPRIILLDCP RFLPPELCGE LIALIDKDRR
PSTLADANGD NYFRTSETCD LEEHEPAVQE LERRLFALNG IDPAHGEPVQ GQRYAPGQEF
KPHTDYFEPN GADFEKFCSV SGNRTWTFMI YLNQAEAGGA TRFKVVKKTF QPADGKLVCW
NNHRADGTLN PATLHHGMKV RAGVKYVITK WYREKPWG
//
