ID K8PA77_9BRAD Unreviewed; 412 AA.
AC K8PA77;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Ferredoxin reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9695_02933 {ECO:0000313|EMBL:EKS36515.1};
OS Afipia broomeae ATCC 49717.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=883078 {ECO:0000313|EMBL:EKS36515.1, ECO:0000313|Proteomes:UP000001096};
RN [1] {ECO:0000313|EMBL:EKS36515.1, ECO:0000313|Proteomes:UP000001096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49717 {ECO:0000313|EMBL:EKS36515.1,
RC ECO:0000313|Proteomes:UP000001096};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Afipia broomeae ATCC 49717.";
RL Submitted (APR-2012) 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:EKS36515.1}.
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DR EMBL; AGWX01000004; EKS36515.1; -; Genomic_DNA.
DR RefSeq; WP_006021638.1; NZ_KB375283.1.
DR AlphaFoldDB; K8PA77; -.
DR PATRIC; fig|883078.3.peg.3030; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_4_0_5; -.
DR Proteomes; UP000001096; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001096}.
FT DOMAIN 4..301
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 321..404
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 412 AA; 44536 MW; EE5860E3E06F6816 CRC64;
MSGLVVVGAS YAGIQAALSA RDSGYAERIT VVADDHVLPY QRPPLSKDFL LDKVKQDGLV
LRDDAFFKLK QIDLILETRV HAIDRRARQL SINGSMTLDF DKLFIGTGSH ARRLTIPGSN
LDGVCYLRSI RDAIDLKERQ RTAAEIVIVG GGFIGLEVAA SASKLGKKVT VIESASRLLE
RAVSPVVSQF LLDLHTRHGV DVRLNEGVAE IEDHNGRAGV VRTRSGARLR ADLVLVGIGG
VPNDELARDA QLNCTDGIVV DDHGLTSDPA IYAAGDCANH YNAHAQGWLR LESVQNAQDQ
AKAAGLAIAG KTGPYDSVPR FWSDQYDAKL QTVGISRNFD RQAVRGSLKD GQFSVFYYRR
DKLCAVDSVN RAGDQMAARR LISGGVSPTP EQAADLSFDF KSLLTTIKAV GA
//
