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Database: UniProt
Entry: A0A1G5TJ42_9SPHN
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ID   A0A1G5TJ42_9SPHN        Unreviewed;       226 AA.
AC   A0A1G5TJ42;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=PKHD-type hydroxylase {ECO:0000313|EMBL:SDA21198.1};
GN   ORFNames=SAMN03159340_01405 {ECO:0000313|EMBL:SDA21198.1};
OS   Sphingomonas sp. NFR15.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1566282 {ECO:0000313|EMBL:SDA21198.1, ECO:0000313|Proteomes:UP000199327};
RN   [1] {ECO:0000313|Proteomes:UP000199327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFR15 {ECO:0000313|Proteomes:UP000199327};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00657};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00657};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961,
CC         ECO:0000256|HAMAP-Rule:MF_00657};
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DR   EMBL; FMWX01000002; SDA21198.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5TJ42; -.
DR   STRING; 1566282.SAMN03159340_01405; -.
DR   OrthoDB; 9812472at2; -.
DR   Proteomes; UP000199327; Unassembled WGS sequence.
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   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   Gene3D; 4.10.860.20; Rabenosyn, Rab binding domain; 1.
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; PKHD-TYPE HYDROXYLASE YBIX; 1.
DR   PANTHER; PTHR41536:SF1; PKHD-TYPE HYDROXYLASE YBIX; 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 {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|HAMAP-
KW   Rule:MF_00657};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00657};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00657};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00657}; Reference proteome {ECO:0000313|Proteomes:UP000199327};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896, ECO:0000256|HAMAP-Rule:MF_00657}.
FT   DOMAIN          78..178
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   BINDING         96
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
FT   BINDING         98
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
FT   BINDING         159
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
FT   BINDING         169
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
SQ   SEQUENCE   226 AA;  25094 MW;  0B21C72F2EF72989 CRC64;
     MLVHIPALFS PDEVREARGL LEAADWHDGR ATAGHRAALV KRNLQLPLDH AISRQLGARI
     LDRLGTTPLF IAATLPLRVL PPRFNRYEGG GDYGAHVDSA IFPLPGSAER VRSDVSSTLF
     FSDPQDYDGG ELVISDTFGE RRVKLAAGDM IVYPGTSLHH VTPVTRGTRY AAFFWTQSLV
     RADERRRLLF DLDTAIQVLG SDHPDHASLD TLTGVYHNLM RQWSET
//
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