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PKHD-type hydroxylase HNE_1625 (EC 1.14.11.-)

 Y1625_HYPNA             Reviewed;         224 AA.
Q0C1R0;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 1.
07-JUN-2017, entry version 67.
RecName: Full=PKHD-type hydroxylase HNE_1625 {ECO:0000255|HAMAP-Rule:MF_00657};
EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
OrderedLocusNames=HNE_1625;
Hyphomonas neptunium (strain ATCC 15444).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Hyphomonadaceae; Hyphomonas.
NCBI_TaxID=228405;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15444;
PubMed=16980487; DOI=10.1128/JB.00111-06;
Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T.,
Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E.,
Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A.,
Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C.,
Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D.,
Davidsen T.M., Yang Q., Zafar N., Ward N.L.;
"Comparative genomic evidence for a close relationship between the
dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
crescentus.";
J. Bacteriol. 188:6841-6850(2006).
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000255|HAMAP-Rule:MF_00657};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_00657};
-!- COFACTOR:
Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
Evidence={ECO:0000255|HAMAP-Rule:MF_00657};
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EMBL; CP000158; ABI76006.1; -; Genomic_DNA.
RefSeq; WP_011646633.1; NC_008358.1.
ProteinModelPortal; Q0C1R0; -.
SMR; Q0C1R0; -.
STRING; 228405.HNE_1625; -.
EnsemblBacteria; ABI76006; ABI76006; HNE_1625.
KEGG; hne:HNE_1625; -.
eggNOG; ENOG4107E2E; Bacteria.
eggNOG; COG3128; LUCA.
HOGENOM; HOG000236239; -.
OMA; VGCYHNL; -.
OrthoDB; POG091H0LGZ; -.
Proteomes; UP000001959; Chromosome.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro.
HAMAP; MF_00657; Hydroxyl_YbiX; 1.
InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
InterPro; IPR023550; PKHD_hydroxylase.
InterPro; IPR006620; Pro_4_hyd_alph.
Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
SMART; SM00702; P4Hc; 1.
PROSITE; PS51471; FE2OG_OXY; 1.
3: Inferred from homology;
Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
Reference proteome; Vitamin C.
CHAIN 1 224 PKHD-type hydroxylase HNE_1625.
/FTId=PRO_0000346484.
DOMAIN 77 175 Fe2OG dioxygenase. {ECO:0000255|HAMAP-
Rule:MF_00657}.
METAL 95 95 Iron. {ECO:0000255|HAMAP-Rule:MF_00657}.
METAL 97 97 Iron. {ECO:0000255|HAMAP-Rule:MF_00657}.
METAL 156 156 Iron. {ECO:0000255|HAMAP-Rule:MF_00657}.
BINDING 166 166 2-oxoglutarate. {ECO:0000255|HAMAP-
Rule:MF_00657}.
SEQUENCE 224 AA; 24660 MW; 77DF4595765FEB66 CRC64;
MIVIENILGQ DVLTEVAAAL RELRWEDGRN TAGATARRVK RNQQADLSSR TGSKVREVLL
EAVKRHPVVE AYARPLKFAP PLISCSGEGD AYGLHIDNPV MGKGDARLRT DLSFTLFLSP
PESYDGGELE IETVFKTESV KLPAGSMVIY PSTELHRVTP VTSGERFVFV GWIQSAIKDA
AQRAILFDVT NLKAGLARRF PPGSPELLTL AKTESNLIRM WSDI


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