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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//