ID I4W399_9GAMM Unreviewed; 284 AA.
AC I4W399;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Procollagen-proline dioxygenase {ECO:0000313|EMBL:EIL93940.1};
GN ORFNames=UU7_06513 {ECO:0000313|EMBL:EIL93940.1};
OS Rhodanobacter spathiphylli B39.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163407 {ECO:0000313|EMBL:EIL93940.1, ECO:0000313|Proteomes:UP000003226};
RN [1] {ECO:0000313|EMBL:EIL93940.1, ECO:0000313|Proteomes:UP000003226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B39 {ECO:0000313|EMBL:EIL93940.1,
RC ECO:0000313|Proteomes:UP000003226};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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:EIL93940.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJXT01000011; EIL93940.1; -; Genomic_DNA.
DR RefSeq; WP_007806560.1; NZ_AJXT01000011.1.
DR AlphaFoldDB; I4W399; -.
DR STRING; 1163407.UU7_06513; -.
DR PATRIC; fig|1163407.3.peg.1306; -.
DR eggNOG; COG3751; Bacteria.
DR OrthoDB; 269774at2; -.
DR Proteomes; UP000003226; Unassembled WGS sequence.
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, ECO:0000313|EMBL:EIL93940.1};
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:UP000003226};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 170..275
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 284 AA; 31217 MW; 11B8EAC211B05A5C CRC64;
MHPRTTITPQ LRDWILTTTR DGHSVTEVLR LMKDNGYDPR QSRSIVAEVL KLPLAALNAA
APGASPRGLR TRHPEAPEVD VDGHLVGISL SVENPALRVL ENLLAAEECE ELIALAQPRL
KRALTVASDG SNQVDQRRTS EGMFFTLNEL PLVGRIEQRL ATLLGMPVSH GEGLQILHYL
PGQEYEPHFD WFDPQQPGYD TITAVGGQRV ASVVMYLNTP AQGGGTAFPE LGLTVTARRG
AAVYFAYEGG DQQSLHAGLP VQRGEKWIAT KWLRERPYGH SHKA
//
