ID G8RKC4_MYCRN Unreviewed; 541 AA.
AC G8RKC4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component {ECO:0000313|EMBL:AEV73526.1};
GN OrderedLocusNames=MycrhN_2978 {ECO:0000313|EMBL:AEV73526.1},
GN MycrhN_3082 {ECO:0000313|EMBL:AEV73619.1};
OS Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV73526.1, ECO:0000313|Proteomes:UP000005442};
RN [1] {ECO:0000313|EMBL:AEV73526.1, ECO:0000313|Proteomes:UP000005442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV73526.1,
RC ECO:0000313|Proteomes:UP000005442};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL Submitted (DEC-2011) 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; CP003169; AEV73526.1; -; Genomic_DNA.
DR EMBL; CP003169; AEV73619.1; -; Genomic_DNA.
DR AlphaFoldDB; G8RKC4; -.
DR STRING; 710685.MycrhN_2978; -.
DR KEGG; mrh:MycrhN_2978; -.
DR KEGG; mrh:MycrhN_3082; -.
DR PATRIC; fig|710685.3.peg.2974; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_520687_0_0_11; -.
DR Proteomes; UP000005442; Chromosome.
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 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 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 Pyruvate {ECO:0000313|EMBL:AEV73526.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005442}.
FT DOMAIN 60..386
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 408..513
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 541 AA; 60838 MW; 2FED952EC45959CB CRC64;
MLKTAADNLR VRRYRKGWIL MDLIDTTLSM DRWEDLIHDA ETGVVSEPLE NVYRKRGTAF
DVIFVGGGAG GRFGSAYAQA RGLRQLVIDK WPFLGGSCPH QACVPHHLFS EAAREMDYMR
WNSDTLWFPK FEEERASIVD MITLFKKGRN NAHAFMNWQS KEQLDMEYIL NAEAIVIDKH
TVEVNGERFT TQSLVLATGT RTHFPPEIAG LDKAGVYDFA TLIDPGLDYE PTSCVIIGGS
KVAMEYGSFF QATGCHTTIL TRSALMRTES LHHVDEDLRT YVVDNMRLRG MDIIEGCEPL
EVVGDDRAAG VLVRLADGTE EVIETDFVFI GTGERPNTKP YVDALGIEVD KKGFVKVNSR
MQTSVEGVYA IGDLIGSPME MFKARKCGMT AARNISGEAF EFDFTEFPDF LHTTYEVTWV
GLTEQEARDA YGDISVIQMP PKGIRHEELS LPLAEGSMLY GFTRPELTGF QKCIYDNKSR
RLLGAHHCGF GAKDAFQYLD HLIKKGITID EMGEMNELFL NPEHFIQLSR LRAGNPDLQD
L
//
