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Database: UniProt
Entry: A0A139BTX0_9PROT
LinkDB: A0A139BTX0_9PROT
Original site: A0A139BTX0_9PROT 
ID   A0A139BTX0_9PROT        Unreviewed;       621 AA.
AC   A0A139BTX0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   ORFNames=AWT59_1549 {ECO:0000313|EMBL:KXS32343.1};
OS   Candidatus Gallionella acididurans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Gallionella.
OX   NCBI_TaxID=1796491 {ECO:0000313|EMBL:KXS32343.1, ECO:0000313|Proteomes:UP000070578};
RN   [1] {ECO:0000313|EMBL:KXS32343.1, ECO:0000313|Proteomes:UP000070578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS32343.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXS32343.1, ECO:0000313|Proteomes:UP000070578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS32343.1};
RA   Kadnikov V., Ivasenko D., Beletsky A., Mardanov A., Danilova E.,
RA   Pimenov N., Karnachuk O., Ravin N.;
RT   "New uncultured bacterium of the family Gallionellaceae from acid mine
RT   drainage: description and reconstruction of genome based on metagenomic
RT   analysis of microbial community.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) +
CC         N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045,
CC         Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83100; EC=1.8.1.4;
CC         Evidence={ECO:0000256|RuleBase:RU003692};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003692};
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000256|RuleBase:RU003692}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003692}.
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:KXS32343.1}.
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DR   EMBL; LSLI01000033; KXS32343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139BTX0; -.
DR   PATRIC; fig|1796491.3.peg.1700; -.
DR   Proteomes; UP000070578; Unassembled WGS sequence.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
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; IPR006258; Lipoamide_DH.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR01350; lipoamide_DH; 1.
DR   PANTHER; PTHR22912:SF160; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 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.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003692}; Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003692};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003692};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003692};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070578}.
FT   DOMAIN          4..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          85..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  66896 MW;  770CC47E3860DAD8 CRC64;
     MSQTIEVKIP DIGDFKEVEV IEVFVKAGDK VEAEQSLITL ETDKAAMEVP CPAAGVVKAI
     KVKLGDKVSK GSVILTLEQE QGASSKEQVK PAASAPAVAT GKSPAPAPDP ASAPQPFKKG
     DIHAEVLVLG AGPGGYTAAF RAADLGKQVV LVEKFASLGG VCLNVGCIPS KALLHVAKVI
     SEAEEVAHHG VTFAKPKIDI DKTRSWQLSV INKLTGGLAA LAKQRKVQVV QGTAKFTSPN
     HLEVATRDGK KIISFDTAII AAGSSVARIP GFPYDDPRII DSTGALALQD VPKRMLIIGG
     GIIGLEMATV YDALGSKITV VELMDQLMPG ADKDLVKPLH KRIEKRYEAI YLKTKVSKIE
     AQKTGLKVTF EGEQAPEPQL YDRVLMAVGR RPNGRDIGAD AAGVTVNERG FIPVNIQMRT
     NVPHIYAIGD IVGDPMLAHK ATHEGKVAAE VIAGHHAAFE PLTIPSVAYT DPEIAWMGLT
     ETQAKAHRYS LRKSQFPVGR IGPCVVHRPR GRVYQTAARP VHTPHPRCGH SRSECRRTDR
     RSGARAGDGC GHGRHRPDHT PASDFVRDAG LRRRNRGRQH HRPVYAEEKI KTDFSMRPLL
     GAAGDYTGTT IFPAIRVRLW H
//
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