ID Q3JDI8_NITOC Unreviewed; 738 AA.
AC Q3JDI8;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamide dehydrogenase (E3) component-like enzyme {ECO:0000313|EMBL:ABA57108.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:ABA57108.1};
GN OrderedLocusNames=Noc_0589 {ECO:0000313|EMBL:ABA57108.1};
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261 {ECO:0000313|EMBL:ABA57108.1, ECO:0000313|Proteomes:UP000006838};
RN [1] {ECO:0000313|Proteomes:UP000006838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107
RC {ECO:0000313|Proteomes:UP000006838};
RX PubMed=16957257; DOI=10.1128/AEM.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; CP000127; ABA57108.1; -; Genomic_DNA.
DR RefSeq; WP_002812131.1; NC_007484.1.
DR AlphaFoldDB; Q3JDI8; -.
DR STRING; 323261.Noc_0589; -.
DR KEGG; noc:Noc_0589; -.
DR eggNOG; COG0398; Bacteria.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_0_6; -.
DR InParanoid; Q3JDI8; -.
DR Proteomes; UP000006838; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR032816; VTT_dom.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF09335; SNARE_assoc; 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.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691}; Pyruvate {ECO:0000313|EMBL:ABA57108.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000006838};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..182
FT /note="VTT"
FT /evidence="ECO:0000259|Pfam:PF09335"
FT DOMAIN 237..560
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 582..690
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 716..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 81063 MW; 4FFDC8D79018C4EC CRC64;
MKKAYLLMVI TALVVGFFFF DLDRLLTLEG LKQGLAQFEA WRTDQPMVIG GAFLLLYVLV
TALSLPGAAV MTLAAGALFG LLWGTIIVSF ASTVGATLAF LISRYLLHDT VQKRFGDRLK
PINEGIKKDG AFYLFTLRLV PVFPFFLINL LMGLTPIRAL TFFWVSQVGM LAGTLVYVNA
GTQLAQLDSL SGILSPSLLL SFALLGVFPL LAKKLLAVIK ARRVYAGYQK PSHFDRNLIV
IGAGAGGLVT AYIAAAVKAK VTLIEAHKMG GDCLNYGCVP SKALIKSAKL AHQMRQADHY
GLEATSPHFS FRKVMARVHE VIRQVEPHDS IERYEGLGVE IIQGYARLVD PWTVEIKRND
GSVQQLTSRS IVLATGARPF IPPLPGIKEV GYVTSDTLWD EFAKLDEAPK RLVVLGGGPI
GCELAQSFTR LGSQVTQVEM APRILIREDE EVSEFAKASL QGDGVAVLTN HKALRCEKQG
GTKRLIMEYE GVEKIIEFDT LLCAVGRVAR LQGYGLEELG IETNRTIVTN DYLETLYPNI
YAAGDVAGPY QFTHTAAHQA WYAAVNALFS QFKRFKVDYR IIPWTTFIDP EVAQVGLNEQ
EAKKKGIAFE VTRYGLEDLD RAITDGAAHG FVKVLTEPGK DRILGVTIVG KHGGDLMAEF
VLAMKHGLGL SKILGTIHAY PTWAEANKYA AGEWKRAHAP ERVLIWLEKY HQWRRGNAKT
SPADGPATKH SDASDRLG
//
