ID A0A1M5ZC00_9BURK Unreviewed; 478 AA.
AC A0A1M5ZC00;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:SHI21689.1};
GN ORFNames=SAMN04488135_113144 {ECO:0000313|EMBL:SHI21689.1};
OS Candidimonas bauzanensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Candidimonas.
OX NCBI_TaxID=658167 {ECO:0000313|EMBL:SHI21689.1, ECO:0000313|Proteomes:UP000184226};
RN [1] {ECO:0000313|EMBL:SHI21689.1, ECO:0000313|Proteomes:UP000184226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10190 {ECO:0000313|EMBL:SHI21689.1,
RC ECO:0000313|Proteomes:UP000184226};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FQXE01000013; SHI21689.1; -; Genomic_DNA.
DR RefSeq; WP_073107027.1; NZ_FQXE01000013.1.
DR AlphaFoldDB; A0A1M5ZC00; -.
DR STRING; 658167.SAMN04488135_113144; -.
DR OrthoDB; 178496at2; -.
DR Proteomes; UP000184226; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
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; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000184226}.
FT DOMAIN 7..326
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 349..452
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 478 AA; 50980 MW; 0DB14CDDFE9EA522 CRC64;
MKQLKTDVAI IGAGTAGLSA YRAVKASGAN AILIEGGPYG TTCARVGCMP SKLLIAAADM
AHAAASAAPF GIHVDGRIRI DGVQVMERVK RERDRFVGFV LESVDGIAGS DKVRGYARYV
SDTVLRVDDH TEIQAARSVI ATGSSPVVEA SYRALGDRVI VNDDVFAWDD LPGSVMVAGA
GVIGLELGQA LARLGVRVRQ INRSASLGGL SDPAVRASAL AAFQAELDLH LETRIIDARR
VGDQVEIRYQ TIGQQEIVER FDYLLVAAGR RPNIDMLDLQ NTSAVLDGKG MPEYDPATLQ
LGRAPIFIAG DVNGVLPVLH EAADDGRIAG QNAALYPEVA PGKRRAPMAV VFSDPQLAQA
GLRFKDLPHR VAIGEVDFAD QGRSRVMLKN HGKLRVYASQ DDGRLLGAEM AGPGMEHIAH
LLAWAVQQKL TIGAMLEMPF YHPVVEEGLR TALRHAAEEL AAARLASVLD AEKIVNSA
//