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Database: UniProt
Entry: F3KQM4_9BURK
LinkDB: F3KQM4_9BURK
Original site: F3KQM4_9BURK 
ID   F3KQM4_9BURK            Unreviewed;       417 AA.
AC   F3KQM4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EGI77898.1};
GN   ORFNames=HGR_03737 {ECO:0000313|EMBL:EGI77898.1};
OS   Hylemonella gracilis ATCC 19624.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hylemonella.
OX   NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI77898.1, ECO:0000313|Proteomes:UP000016368};
RN   [1] {ECO:0000313|EMBL:EGI77898.1, ECO:0000313|Proteomes:UP000016368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI77898.1,
RC   ECO:0000313|Proteomes:UP000016368};
RX   PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA   Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA   Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA   Jensen G.J.;
RT   "Structural diversity of bacterial flagellar motors.";
RL   EMBO J. 30:2972-2981(2011).
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:EGI77898.1}.
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DR   EMBL; AEGR01000040; EGI77898.1; -; Genomic_DNA.
DR   RefSeq; WP_006296724.1; NZ_AEGR01000040.1.
DR   AlphaFoldDB; F3KQM4; -.
DR   STRING; 887062.HGR_03737; -.
DR   eggNOG; COG0446; Bacteria.
DR   OrthoDB; 9769238at2; -.
DR   Proteomes; UP000016368; 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; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016368}.
FT   DOMAIN          7..303
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          326..409
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   417 AA;  43725 MW;  3207E180EA699B75 CRC64;
     MARSEPLLIV GASHAGTQLA AAAREQGFDA PIVLLGDEPH TPYQRPPLSK GVLTGKTEVD
     QLALRGPDFY REQGIDLRLG VRVTGLDLST RRLRLADGGQ LDFGWLALAT GARCRPLPVP
     GADLQGVHIL RTLDDAQAVV AALGASQRAC VIGGGFIGLE VAAALSSVGA SVTVVESQPR
     LLARTFPAAM SDYVADAHRR RGVALALGCG VRALHGHQGR VVAVELVDGR RIDCDLVVLG
     IGVQPNSELA EQAGIACDNG ILVDALGRSS APNVLAIGDV ANMALAAVPG GPQRARLESI
     QAANDGARAA ATLLVGRPQP LDAVPWFWSE QHELKFQMAG LPAPGDQTVL RGELASDKFT
     LFYLREGAVR AAHTVNRPAE HMLARKLIAQ GARIAPELLA DPSVDLKSFF TPPRPAG
//
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