ID Q6LQB5_PHOPR Unreviewed; 739 AA.
AC Q6LQB5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=PBPRA2113 {ECO:0000313|EMBL:CAG20511.1};
OS Photobacterium profundum (strain SS9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG20511.1, ECO:0000313|Proteomes:UP000000593};
RN [1] {ECO:0000313|Proteomes:UP000000593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378669; CAG20511.1; -; Genomic_DNA.
DR RefSeq; WP_011218805.1; NC_006370.1.
DR AlphaFoldDB; Q6LQB5; -.
DR STRING; 298386.PBPRA2113; -.
DR KEGG; ppr:PBPRA2113; -.
DR eggNOG; COG0398; Bacteria.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_0_6; -.
DR Proteomes; UP000000593; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; 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};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000000593};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..184
FT /note="VTT"
FT /evidence="ECO:0000259|Pfam:PF09335"
FT DOMAIN 239..560
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 583..688
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 717..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 81155 MW; 3A6FA86E60619B07 CRC64;
MDRKKVVLLV TLITLIGLWF AFDLSQYFTL EQAKAQQLAL QDTIAEKPFL SSLVYFAVYI
LVTALSLPGA AIMTLLGAAL FGFWWSLLLI SFASTIGATL AFLFSRFILR DWVQAKFGNR
IAPINAGIEK DGPFYLFTLR LIPVFPFFLV NLLMGLTPIS TRMFYLVSQL GMLAGTAVYI
NAGTQLGEIE SLSGIISAPV LMSLALLGLF PLIAKFIMNI ITQRRVYANW KRPEKFDQNM
VVIGAGAGGL VSSYIAAAVK AEVTLIERHK MGGDCLNTGC VPSKAIIRAA HTMAEISRAH
EFGITTDKPQ VNFEKVMSRI HNVIDKIEPH DSVERYSSLG VNCISGEAQI LSPWEVEVNG
QRITTRNIVI ATGARPLVPG ISGLQDVNYL TSDSIWSLKV QPKKLLVLGG GPIGCELAQS
FSRLGSDVTL VEMAEQLLIR EDTDASLLVK ESMHKDGVDI KLNHKATRFE SITAEDGTRI
QRAYLEYNGK EVIVEFDAVM LALGRVANVQ GFGLEELGIT TTQRGTVDVN DYLQTKYPNI
YAVGDVAGPF QLTHAAAHQA WYAAVNGLFG QFKKFKADYS VLPAATYTAP EVARVGINEK
EAENLNIEFD VTRYGIDDLD RAITDGEDYG FVKVITPKGK DKILGVTIVG NNASELLAEF
TLAMRHGLGL NKILGTIHPY PTMSEANKYT AGVWKQANAP QALLAWVKKY HAGMRNDKSQ
KITQPTAPNT QAKLEEEQR
//
