ID A0A0P7Y809_9RHOB Unreviewed; 402 AA.
AC A0A0P7Y809;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Ferredoxin--NAD+ reductase {ECO:0000313|EMBL:KPQ16261.1};
DE EC=1.18.1.3 {ECO:0000313|EMBL:KPQ16261.1};
GN Name=hcaD {ECO:0000313|EMBL:KPQ16261.1};
GN ORFNames=HLUCCO18_09050 {ECO:0000313|EMBL:KPQ16261.1};
OS Rhodobacteraceae bacterium HLUCCO18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666917 {ECO:0000313|EMBL:KPQ16261.1, ECO:0000313|Proteomes:UP000050333};
RN [1] {ECO:0000313|EMBL:KPQ16261.1, ECO:0000313|Proteomes:UP000050333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO18 {ECO:0000313|EMBL:KPQ16261.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPQ16261.1}.
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DR EMBL; LJSY01000018; KPQ16261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7Y809; -.
DR STRING; 1666917.HLUCCO18_09050; -.
DR PATRIC; fig|1666917.4.peg.895; -.
DR Proteomes; UP000050333; Unassembled WGS sequence.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:KPQ16261.1}.
FT DOMAIN 3..299
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 318..400
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 402 AA; 42789 MW; BB97B38EE4F233D0 CRC64;
MERIVVVGAG QAGASCVAKL RSEGFTGAIT LIGEEHAPPY QRPPLSKAYL LGEMALERLY
LRPESYYAEN GIALMLDTTV QAIDRADRKV IASGRAIPYD ALVLTTGSVP RRLPGRIGGE
LGGVHVVRTL KDVDEMAPEI AEGRRALIVG GGYIGLEAAA VCRKKGLDVT LIEMADRILA
RVACPETSAW FRALHEGKGV TVLEGVGLTT LTEADGHVAG AVFSDGSEHP FDLVIAGIGI
TPASALAEAA GLTIDNGIAV DALGRTSDPA IWSAGDCASF PYRGERIRLE SVQNAIDQAE
AVARNILGHG EDYVPHPWFW SDQYDVKLQI AGLNTGYTDV MVRDAGDARS HWYYAGDTLV
SVDAMNDPRA YMVGKRLIEA GKSPARDAVA DPEADLKALL RA
//
