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Database: UniProt
Entry: A0A0N0XHL3_9NEIS
LinkDB: A0A0N0XHL3_9NEIS
Original site: A0A0N0XHL3_9NEIS 
ID   A0A0N0XHL3_9NEIS        Unreviewed;       296 AA.
AC   A0A0N0XHL3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=2OG-Fe(II) oxygenase superfamily protein {ECO:0000313|EMBL:KPC49200.1};
GN   ORFNames=WG78_21810 {ECO:0000313|EMBL:KPC49200.1};
OS   Amantichitinum ursilacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Amantichitinum.
OX   NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC49200.1, ECO:0000313|Proteomes:UP000037939};
RN   [1] {ECO:0000313|EMBL:KPC49200.1, ECO:0000313|Proteomes:UP000037939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGB-41 {ECO:0000313|EMBL:KPC49200.1,
RC   ECO:0000313|Proteomes:UP000037939};
RA   Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT   "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT   chitin-degrading bacterium.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KPC49200.1}.
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DR   EMBL; LAQT01000038; KPC49200.1; -; Genomic_DNA.
DR   RefSeq; WP_053939923.1; NZ_LAQT01000038.1.
DR   AlphaFoldDB; A0A0N0XHL3; -.
DR   STRING; 857265.WG78_21810; -.
DR   PATRIC; fig|857265.3.peg.4468; -.
DR   OrthoDB; 269774at2; -.
DR   Proteomes; UP000037939; 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};
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:UP000037939};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   DOMAIN          183..292
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   296 AA;  32999 MW;  3219EF5B9E83B9FD CRC64;
     MEKITSISPE WQNWLLENLG RGCTPQSLID VMVEKNFDPM FASAIVFHFS SSNNQARPAV
     AAKAGAQSIK EKAASGGYQY ETPRLLPGNV IHTNDRAIHV VQRVAKPVVA FFDNVLSHEE
     CDELIRLSEA RLKRSTIVDP TTGKDAVIDD RTSFGTFFTV NETEFIAKLD RRIAELMNWP
     VENGEGLQIL NYKVGGEYKP HFDYFPETDP GSQVHLRNGG QRVSTLVMYL NDVEEGGATT
     FPELGMQVGP KKGAAVYFEY TNSSGQVDPL TLHGGAPVEK GEKWIATKWM RQRKFS
//
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