ID   Y3031_ACIBS             Reviewed;         227 AA.
AC   B0VL49;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=PKHD-type hydroxylase ABSDF3031 {ECO:0000255|HAMAP-Rule:MF_00657};
DE            EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN   OrderedLocusNames=ABSDF3031;
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00657};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00657};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00657};
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DR   EMBL; CU468230; CAP02317.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VL49; -.
DR   SMR; B0VL49; -.
DR   EnsemblBacteria; CAP02317; CAP02317; ABSDF3031.
DR   KEGG; abm:ABSDF3031; -.
DR   HOGENOM; CLU_106663_0_0_6; -.
DR   OMA; ESFGYHV; -.
DR   BioCyc; ABAU509170:GCL9-2505-MON; -.
DR   Proteomes; UP000001741; Chromosome.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_00657; Hydroxyl_YbiX; 1.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR041097; PKHD_C.
DR   InterPro; IPR023550; PKHD_hydroxylase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   PANTHER; PTHR41536; PTHR41536; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   Pfam; PF18331; PKHD_C; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT   CHAIN           1..227
FT                   /note="PKHD-type hydroxylase ABSDF3031"
FT                   /id="PRO_1000131203"
FT   DOMAIN          78..178
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         96
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         98
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         159
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         169
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
SQ   SEQUENCE   227 AA;  25960 MW;  CCC7530040DEB1B8 CRC64;
     MIHHIPNVLS KEQVAEFRKL MEEANWVGGK VTAGTLSASV KRNQQLSEQD PLTHHLSDIV
     IKAIWQNPLF QAAALPHKII PPLFNRYDEH ESFGFHVDNS IRLIRGTAEQ IRTDLSCTLF
     LSEPDEYEGG DLVIEDTYGY HEVKLPAGDV VLYPSTSLHE VSSITAGTRF ASFFWVQSLV
     RDDSKRHLLF SLDESIRELR KSHGDSYSEV MKLTNIYHNL IRMWSEL