ID A0A1C6PB72_9BURK Unreviewed; 278 AA.
AC A0A1C6PB72;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Prolyl 4-hydroxylase {ECO:0000313|EMBL:SCK40475.1};
GN ORFNames=VAR608DRAFT_3829 {ECO:0000313|EMBL:SCK40475.1};
OS Variovorax sp. HW608.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1034889 {ECO:0000313|EMBL:SCK40475.1, ECO:0000313|Proteomes:UP000198203};
RN [1] {ECO:0000313|Proteomes:UP000198203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HW608 {ECO:0000313|Proteomes:UP000198203};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-2016) 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; LT607803; SCK40475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6PB72; -.
DR OrthoDB; 269774at2; -.
DR Proteomes; UP000198203; Chromosome i.
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 Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 167..274
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 278 AA; 30606 MW; 5E24D42C5693E319 CRC64;
MSHGQVISAE LREWITTQLA AGHSVPSLRA SMQAAGWHDA AADAALAEVE RQAMGATEST
KAMPGPDLSN SPLYIDAGDR RVHVLQTMRN PRVVVFGDLL SDEECEALIS AARQRLARSL
TVETQTGGEA LNVDRTSDGM FFERGENPLV ARIEKRIATL LRWPLEFGEG LQILRYAPGA
QYRPHYDYFD PAEPGTPIIL RRGGQRVGTL VMYLHEPEQG GGTTFPDVGL EVAPKRGTAV
FFSYERPDPA TRTLHGGAPV LAGEKWVATK WLREREFK
//