ID A3YGV6_9GAMM Unreviewed; 711 AA.
AC A3YGV6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamidedehydrogenase (E3) component and related enzyme {ECO:0000313|EMBL:EAQ63607.1};
GN ORFNames=MED121_00325 {ECO:0000313|EMBL:EAQ63607.1};
OS Marinomonas sp. MED121.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=314277 {ECO:0000313|EMBL:EAQ63607.1, ECO:0000313|Proteomes:UP000003436};
RN [1] {ECO:0000313|EMBL:EAQ63607.1, ECO:0000313|Proteomes:UP000003436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED121 {ECO:0000313|EMBL:EAQ63607.1,
RC ECO:0000313|Proteomes:UP000003436};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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:EAQ63607.1}.
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DR EMBL; AANE01000019; EAQ63607.1; -; Genomic_DNA.
DR RefSeq; WP_009834688.1; NZ_CH672432.1.
DR AlphaFoldDB; A3YGV6; -.
DR STRING; 314277.MED121_00325; -.
DR HOGENOM; CLU_016755_1_0_6; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000003436; Unassembled WGS sequence.
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}; Pyruvate {ECO:0000313|EMBL:EAQ63607.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..109
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..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..257
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..555
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 577..685
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 711 AA; 77547 MW; 081362D2B4954385 CRC64;
MKKSKLIILL LFITLLSAFV IFDVQEYLNL AALKSQQDYF SELKHENAFL ITLSFFIGYI
LITALSLPGA AILTLAAGAI FGLYQGLLIA SFASSIGATL AFLASRYLFK EAVQAKFSNQ
LKAFNKGIEK DGAFYLFTLR LVPAFPFFVI NLLMGLTPIK TKTYYLVSQI GMLAGTAVFV
NAGTQLAKID SLSGILSFDL FLSFALLGVL PIAAKKTIEA IKARNAFSHF KKPKHYDYNL
VAIGAGAGGL VSTYIGAAVK AKVALIEKHK MGGDCLNTGC VPSKALIRSA HAAQEVKDAD
TLGISTQGLE VDFNKVFEGI DNVIKQVEPH DSVERYEGLG VECISGAATL LSPYEIEVDG
KIITTKNIVI ATGARPFIPN IKGLDKINYH TSDTIWSIRE NPGRLIVLGG GPIGSELTQS
FNRLGAKVTQ IERGPRILPR EDEDASLWVS NKFLHEGVNL LTNHEAVEVI IENGEQILIC
QTGDNTIKVV FDNLLIAVGR TPNTSGLGLE KLGIETQANG ALVVDDFLRT NIPNIYGVGD
VIGAYQFTHT AAHQAWFAAV NALFGSLKKF AVDYRVIPWA TFTDPEVARV GVSEDEANAN
SIPYELVKFD LEELDRAIAD RHTDGFVKVL TVPGKDKILG VTIVGNQAGD LIAEYVQAMK
YGLGLNKVLG TIHIYPTMAE ANKYAAGEWK RAHIPEKIMK WLKRFHNWRR G
//
