ID Q2YKY3_BRUA2 Unreviewed; 409 AA.
AC Q2YKY3;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Pyridine nucleotide-disulphide oxidoreductase, class-II:NAD binding site:Adrenodoxin reductase:Pyridine nucleotide-disulphide {ECO:0000313|EMBL:CAJ12677.1};
GN OrderedLocusNames=BAB2_0511 {ECO:0000313|EMBL:CAJ12677.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ12677.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ12677.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ12677.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AM040265; CAJ12677.1; -; Genomic_DNA.
DR RefSeq; WP_002965913.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YKY3; -.
DR STRING; 359391.BAB2_0511; -.
DR GeneID; 3827608; -.
DR KEGG; bmf:BAB2_0511; -.
DR PATRIC; fig|359391.11.peg.2701; -.
DR HOGENOM; CLU_003291_4_0_5; -.
DR PhylomeDB; Q2YKY3; -.
DR Proteomes; UP000002719; Chromosome II.
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:UP000002719}.
FT DOMAIN 4..301
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 320..404
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 409 AA; 43615 MW; 9DBD6852176F5A92 CRC64;
MDDRCIIIGA GHAGSQAAVS LRQEGYAGEI ILINDETDIP YHKPPLSKSY LKAPEKGSLV
LRPESAYRDN NIEMLFGAHV DAVSIAERTV TLGDGRVLPW SELVFATGAR ARIPDVPGVA
LEGVVTLRRM EDARRIAAMM PDVRNVVIIG GGFIGLEMAH SAIALGKKTV LIEAAPRILG
RSVAAPVSAH VEARSRAADI TLLTGLGVAS IEGENGRAIG VTAGDGTFFP ADLVVIGTGA
VPNVELAAKA GLSIDNGIRV DEHMRTSAPH VYAIGDCASY AHFHAGRHVR LESVQNATDQ
AKHVARTIVG RETPYREVAW FWSDQGDMKL QTAGLSFDAD RHVLSGEPEE NAFSVFHFKG
DRLVAVDSIN RPAGHMIARR LLAAGISPSE ADIMAGMPRL KELLAVVAR
//
