GenomeNet

Database: UniProt
Entry: G2KP96_MICAA
LinkDB: G2KP96_MICAA
Original site: G2KP96_MICAA 
ID   G2KP96_MICAA            Unreviewed;       465 AA.
AC   G2KP96;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
GN   OrderedLocusNames=MICA_663 {ECO:0000313|EMBL:AEP08997.1};
OS   Micavibrio aeruginosavorus (strain ARL-13).
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Micavibrio.
OX   NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP08997.1, ECO:0000313|Proteomes:UP000009286};
RN   [1] {ECO:0000313|EMBL:AEP08997.1, ECO:0000313|Proteomes:UP000009286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARL-13 {ECO:0000313|EMBL:AEP08997.1,
RC   ECO:0000313|Proteomes:UP000009286};
RX   PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA   Wang Z., Kadouri D., Wu M.;
RT   "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT   aeruginosavorus ARL-13.";
RL   BMC Genomics 12:453-453(2011).
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|ARBA:ARBA00001492,
CC         ECO:0000256|RuleBase:RU003692};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3,
CC         ECO:0000256|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3,
CC       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   ---------------------------------------------------------------------------
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; CP002382; AEP08997.1; -; Genomic_DNA.
DR   RefSeq; WP_014102220.1; NC_016026.1.
DR   AlphaFoldDB; G2KP96; -.
DR   STRING; 856793.MICA_663; -.
DR   KEGG; mai:MICA_663; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_1_5; -.
DR   OMA; DAKYGEW; -.
DR   OrthoDB; 9776382at2; -.
DR   Proteomes; UP000009286; Chromosome.
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; IPR006258; Lipoamide_DH.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   NCBIfam; TIGR01350; lipoamide_DH; 1.
DR   PANTHER; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003692};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
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:UP000009286}.
FT   DOMAIN          7..327
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          346..455
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        444
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         54
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         118
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         142..144
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         179..186
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         202
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         312
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         318..321
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        45..50
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   465 AA;  48674 MW;  1633C96CC4FC07A1 CRC64;
     MTDAPSYDVI VIGSGPGGYV CAIRCAQLGL KTACVEKRDT LGGTCLNVGC IPSKALLQAS
     EKFHEAEHAL AAFGVKVGKP ELDLPTMMKH KDAVVESNTK GVEFLFKKNK IDWLKGEGKV
     AAAGVVEVAG KTYNAKNIVI ATGSDVASLP GITIDEKRIV SSTGAIALES VPKHLVVIGG
     GVIGLELGAV WGRLGAKVTV VEYLDRILPT MDGDLSKEAK KIFGKQGMEF KLSSKVTSVK
     DNGKGVTLSV EPAAGGAAET IEADIVLVAV GRKAYTDGLG LDAVGVERDE RGRVKTDAHF
     QSNVKGIFAI GDVIAGPMLA HKAEDEGVIL AEMIAGQTGH IDYNLVPSVV YTWPEVASVG
     QTEDQVKAAN AQYKVGKFPF SANGRARAMN ATEGFVKIIA DAKTDRVLGV HIIGPEAGTL
     IAEAVIAMEF GASAEDIART CHAHPTLEEA VKEAALAVDG RPLHM
//
DBGET integrated database retrieval system