ID A0A2Y9AIQ1_9RHOB Unreviewed; 390 AA.
AC A0A2Y9AIQ1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:SSA44354.1};
GN ORFNames=BCF38_103133 {ECO:0000313|EMBL:PWJ20318.1},
GN SAMN05421539_103133 {ECO:0000313|EMBL:SSA44354.1};
OS Jannaschia seohaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=475081 {ECO:0000313|EMBL:SSA44354.1, ECO:0000313|Proteomes:UP000251571};
RN [1] {ECO:0000313|EMBL:SSA44354.1, ECO:0000313|Proteomes:UP000251571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25227 {ECO:0000313|EMBL:SSA44354.1,
RC ECO:0000313|Proteomes:UP000251571};
RA Cai Z.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWJ20318.1, ECO:0000313|Proteomes:UP000245839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25227 {ECO:0000313|EMBL:PWJ20318.1,
RC ECO:0000313|Proteomes:UP000245839};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; QGDJ01000003; PWJ20318.1; -; Genomic_DNA.
DR EMBL; UETC01000003; SSA44354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Y9AIQ1; -.
DR OrthoDB; 255432at2; -.
DR Proteomes; UP000245839; Unassembled WGS sequence.
DR Proteomes; UP000251571; Unassembled WGS sequence.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
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; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR000866; AhpC/TSA.
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 InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 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:UP000245839};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 13..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 261..358
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 367..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 43167 MW; 5C294CF40688CCC3 CRC64;
MDSPLKIDAT TLLTPGDPAP SFIQRSVANP RYAFDSAAGR YLVLCFYGSA ADPHAQDALR
AAHDRPDLFD DDRASFFGVS VDPADEAQGR VQNRIPGYRH FWDFDLTVSR RYGVADKAAT
PASGTPLALV RQWVVIDPTM RVIAAIPFRP ERSDLAEVMR LLEALPPPAR FAGVEIMAPI
LFLPRVFEPE LCQHLIGLYE AQGGQESGFM REIDGKTVGV TDPAFKRRKD YDIQDRTLVS
ALQARFLRRV VPEIAKVHQF RVTRMERYII SCYAAEDGGH FSAHRDNTTK GTAHRRFAVS
VNLNDDFDGG EVSFPEYGPR SFKAPPGGAV VFSCSLLHRV SKVTRGRRYA FLPFLYDETA
ARLREENAGH VGTSGSSYRA GTSARAEAAP
//
