ID Q08ZR2_STIAD Unreviewed; 235 AA.
AC Q08ZR2;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=2-oxoglutarate-Fe(II) oxygenase family enzyme {ECO:0000313|EMBL:ADO74824.1};
DE SubName: Full=Oxidoreductase, 2OG-Fe(II) oxygenase family {ECO:0000313|EMBL:EAU65984.1};
GN OrderedLocusNames=STAUR_7068 {ECO:0000313|EMBL:ADO74824.1};
GN ORFNames=STIAU_8482 {ECO:0000313|EMBL:EAU65984.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU65984.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU65984.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU65984.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO74824.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO74824.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; CP002271; ADO74824.1; -; Genomic_DNA.
DR EMBL; AAMD01000067; EAU65984.1; -; Genomic_DNA.
DR RefSeq; WP_002614687.1; NZ_AAMD01000067.1.
DR STRING; 378806.STAUR_7068; -.
DR KEGG; sur:STAUR_7068; -.
DR PATRIC; fig|378806.16.peg.5091; -.
DR eggNOG; COG3751; Bacteria.
DR HOGENOM; CLU_079367_1_0_7; -.
DR OrthoDB; 269774at2; -.
DR Proteomes; UP000001351; Chromosome.
DR Proteomes; UP000032702; 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:InterPro.
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; IPR037923; HTH-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF51215; Regulatory protein AraC; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 3..221
FT /note="Prolyl 4-hydroxylase alpha subunit"
FT /evidence="ECO:0000259|SMART:SM00702"
SQ SEQUENCE 235 AA; 27054 MW; D6AF923F49DB1B29 CRC64;
MTDFIEIHDG VLDPKLCRDI IDRFNRSSHV QRGRIGHGVD TSKKDSYDLC MNLTPDWEDL
VRLLMDRTFP PLRSYLRKYL YTLIGAVSPA VLDPKTGQRV ALTEQNFAAL GDPLLDQLVG
YFYRYGYLNV QKYIQGSGGY PHWHSEIYPK DASCEPLHRV LAFQFYLNDV SKGGETEFYY
QQRKVESKAG RLIIFPAGFT HTHRGNVPES GDKYIITSWV LFQRSETMYG NNPPT
//