ID C7JE98_ACEP3 Unreviewed; 336 AA.
AC C7JE98;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN OrderedLocusNames=APA01_21670 {ECO:0000313|EMBL:BAI00282.1};
OS Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=634452 {ECO:0000313|EMBL:BAI00282.1, ECO:0000313|Proteomes:UP000000948};
RN [1] {ECO:0000313|EMBL:BAI00282.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 3283 {ECO:0000313|EMBL:BAI00282.1};
RX PubMed=19638423; DOI=10.1093/nar/gkp612;
RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT "Whole-genome analyses reveal genetic instability of Acetobacter
RT pasteurianus.";
RL Nucleic Acids Res. 37:5768-5783(2009).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; AP011121; BAI00282.1; -; Genomic_DNA.
DR RefSeq; WP_014457328.1; NC_013209.1.
DR AlphaFoldDB; C7JE98; -.
DR STRING; 634452.APA01_21670; -.
DR KEGG; apt:APA01_21670; -.
DR PATRIC; fig|634452.3.peg.2249; -.
DR eggNOG; COG3128; Bacteria.
DR HOGENOM; CLU_062430_0_0_5; -.
DR BioCyc; APAS634452:APA01_RS11010-MONOMER; -.
DR Proteomes; UP000000948; Chromosome.
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; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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 Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 231..325
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 336 AA; 37916 MW; B1A7B83E04ED7F52 CRC64;
MILPGDPAPI FTQKCSTNWG YYSFDMAAGK YNILVFVPDI QKLFANKVID TLQNLLELKK
SIPIEIFVVT TSFDDKDIKN DNFYYIYDLD CHVHNIFGIN IDEITCVITD PMLRIKEVLP
QHAISYSTIK NNLKNRSSSQ NIPIPALLLT DILEADFCHA LIHYYHYNSP TPSGFLTKNA
DGLAVEKIDP MFKRRYDCKI KNQNLIKGLQ ARIIRRVVPE IRKTFQCTVT GMDRMIISCY
DAAHKGHFAP HRDNTVEGAK HRLFAISINL NDTFEGGELT FPEFSNQGFC PPAGGALIFS
SALLHAVRPV TKGKRYACLP FAFNEDSINS AHQSAS
//
