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Database: UniProt
Entry: A0A1M5ZC00_9BURK
LinkDB: A0A1M5ZC00_9BURK
Original site: A0A1M5ZC00_9BURK 
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
//
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