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Database: UniProt
Entry: A0A1H7KXW1_9ACTN
LinkDB: A0A1H7KXW1_9ACTN
Original site: A0A1H7KXW1_9ACTN 
ID   A0A1H7KXW1_9ACTN        Unreviewed;       420 AA.
AC   A0A1H7KXW1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=3-phenylpropionate/trans-cinnamate dioxygenase ferredoxin reductase subunit {ECO:0000313|EMBL:SEK91336.1};
GN   ORFNames=SAMN04515665_106112 {ECO:0000313|EMBL:SEK91336.1};
OS   Blastococcus sp. DSM 46786.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1798227 {ECO:0000313|EMBL:SEK91336.1, ECO:0000313|Proteomes:UP000198952};
RN   [1] {ECO:0000313|Proteomes:UP000198952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46786 {ECO:0000313|Proteomes:UP000198952};
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; FOAO01000006; SEK91336.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7KXW1; -.
DR   STRING; 1798227.SAMN04515665_106112; -.
DR   OrthoDB; 4213189at2; -.
DR   Proteomes; UP000198952; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000313|EMBL:SEK91336.1};
KW   Oxidoreductase {ECO:0000313|EMBL:SEK91336.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198952}.
FT   DOMAIN          11..312
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          331..415
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   420 AA;  43303 MW;  E513205E71062BCE CRC64;
     MPPEEREAGT LVVGASQAGV QLVASLRQLG DTAPITLVGA EAHPPYQRPP LSKEFLAGTA
     APETLAFRTT SFYADHDIEL ICGERVVDVA LPSGGRPGLA RTSSGRELPF GRLALTVGAR
     PRRIDVPGAD LDGILYLRDL DDAVSLRDRL ADASRVVVVG GGFIGLEAAA AARAQGKEVV
     VVEAADRLVG RAVAPVVSDF LRAAHERRGS SVLLSVDVVG FSGAGGHVDG VLLADGRSLP
     ADLVMVGIGV VPRTELAEQL GLECDGGIVV DAHARTSAPS VVAAGDCTVL PHPMTGEGRV
     RLESVPSAVA QATLAAATLA GREAVTRSVP WFWSNQGDLK LQIAGLSTGF DRHVVRGDPD
     TESFSVLYYR SGTLLAVDAV NAPADYLAVR KALTQGIALP AELAADAGTP LKALLAAPAA
//
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