ID F9ZND8_ACICS Unreviewed; 467 AA.
AC F9ZND8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AEK58181.1};
GN OrderedLocusNames=Atc_1532 {ECO:0000313|EMBL:AEK58181.1};
OS Acidithiobacillus caldus (strain SM-1).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK58181.1, ECO:0000313|Proteomes:UP000006135};
RN [1] {ECO:0000313|EMBL:AEK58181.1, ECO:0000313|Proteomes:UP000006135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK58181.1,
RC ECO:0000313|Proteomes:UP000006135};
RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT "Unraveling the Acidithiobacillus caldus complete genome and its central
RT metabolisms for carbon assimilation.";
RL J. Genet. Genomics 38:243-252(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002573; AEK58181.1; -; Genomic_DNA.
DR RefSeq; WP_004872044.1; NC_015850.1.
DR AlphaFoldDB; F9ZND8; -.
DR STRING; 990288.Atc_1532; -.
DR GeneID; 69614136; -.
DR KEGG; acu:Atc_1532; -.
DR HOGENOM; CLU_003291_1_0_6; -.
DR OrthoDB; 9808980at2; -.
DR Proteomes; UP000006135; Chromosome.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43429:SF3; NADH OXIDASE-RELATED; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006135}.
FT DOMAIN 7..304
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 339..438
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 467 AA; 50220 MW; 780CCA919A713B12 CRC64;
MNSSKTDVLI VGGGPAGMMA GITAAQFWPH KEVTVLRPET DAVIPCGIPY IFGTLGGTEE
DMAGRAPLLA AGGKLINGLV QRVDRERREA QLEDGRIIGW ERLVLATGGE NFIPPIPGTD
LHGVFSIRKD YDYLDRLFSQ IIPDVHRLAI IGGGFIGVEF ADEVRKRGIE VHIIEMLPHL
MQAAFDLDAC VAVEKQLRQH GVHIHTEARV EALRPGADGR RVGEVQIADR EPLSVDAVLI
AIGVRPNVAL AKDMGLTLSR SGGVWVDAFQ RSREDPAIFA VGDCAHKQDY FTRKANHAMI
ASQAAAEGRI AGMNLYGLRE LRYNAGSVSI YASEIDGLAF GVAGMTQTQA SAEGFPILVG
EARMPDHHPA AMPDTTEIYC RLIFSANTLQ LLGAQVLGGR TTGELLNTMG LAIQMHATAP
DLASMQFGSQ PRLTPALHPM VAATGDALRR HYALQHPCLS GDSHASL
//
