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Database: UniProt
Entry: A0A1H9JJ37_9GAMM
LinkDB: A0A1H9JJ37_9GAMM
Original site: A0A1H9JJ37_9GAMM 
ID   A0A1H9JJ37_9GAMM        Unreviewed;       339 AA.
AC   A0A1H9JJ37;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Anthranilate 1,2-dioxygenase reductase subunit {ECO:0000313|EMBL:SEQ87001.1};
GN   ORFNames=SAMN03080615_03058 {ECO:0000313|EMBL:SEQ87001.1};
OS   Amphritea atlantica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Amphritea.
OX   NCBI_TaxID=355243 {ECO:0000313|EMBL:SEQ87001.1, ECO:0000313|Proteomes:UP000198749};
RN   [1] {ECO:0000313|Proteomes:UP000198749}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18887 {ECO:0000313|Proteomes:UP000198749};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; FOGB01000009; SEQ87001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9JJ37; -.
DR   STRING; 355243.SAMN03080615_03058; -.
DR   OrthoDB; 4258484at2; -.
DR   Proteomes; UP000198749; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd06209; BenDO_FAD_NAD; 1.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR047683; BenC-like_FAD_NAD-bd.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Dioxygenase {ECO:0000313|EMBL:SEQ87001.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Oxidoreductase {ECO:0000313|EMBL:SEQ87001.1}.
FT   DOMAIN          2..95
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          103..205
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   339 AA;  37226 MW;  B8458E69B4195035 CRC64;
     MNKVALNFSD GRTRFIGVNS GETVLDAALR QGITIPVDCR EGVCATCKGL CSSGNYQLEY
     VDEDALSAAE LKQGGVLTCQ MRVASDCAIA FDFESTLCTS SGPEELTAVI TNVDLVSESA
     AVVYIDAQAL GDQLDFLPGQ YAHVNVPGTD EWRSYSFACA PNKTNQLQFL IRLLPQGVMS
     DYLRERANPG DRMKLKAPLG AFYLHQIKRP LIFVAGGTGL AAFLGMLDQL VENPERCDQP
     ITLFYGVTQM ADLCEIERLQ QYAEKLPDFT CHSIVMKENE DWPGTVGVVT DLFEDSHFNN
     GEVDLYLCGP PPMVDAVKGW LDQRDMANST IHYEKFSAS
//
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