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
//