ID G8RGX0_MYCRN Unreviewed; 648 AA.
AC G8RGX0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Succinate dehydrogenase/fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:AEV72085.1};
GN OrderedLocusNames=MycrhN_1469 {ECO:0000313|EMBL:AEV72085.1};
OS Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV72085.1, ECO:0000313|Proteomes:UP000005442};
RN [1] {ECO:0000313|EMBL:AEV72085.1, ECO:0000313|Proteomes:UP000005442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV72085.1,
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.
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DR EMBL; CP003169; AEV72085.1; -; Genomic_DNA.
DR RefSeq; WP_014209900.1; NC_016604.1.
DR AlphaFoldDB; G8RGX0; -.
DR STRING; 710685.MycrhN_1469; -.
DR KEGG; mrh:MycrhN_1469; -.
DR PATRIC; fig|710685.3.peg.1475; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_8_1_11; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000005442; Chromosome.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF89; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005442}.
FT DOMAIN 21..440
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 501..599
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 512..539
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 648 AA; 71693 MW; AAFA59B689E20294 CRC64;
MAEPEALRAS GSSQVERHEY DVVVIGAGGA GLRAVIEARE RGLRVAVITK SLFGKAHTVM
AEGGCAAAMG NANPKDNWQV HFRDTMRGGK FLNNWRMAEL HAKEAPDRVW ELETYGALFD
RTKDGRISQR NFGGHTYPRL AHVGDRTGLE IIRTLQQKIV SLQQEDKAEF GDYEARIRVF
HECTITDLVK DGDRIAGAFG YWRESGNFIL FETPAVVLAT GGIGKSYKVT SNSWEYTGDG
HALALRAGAT LINMEFVQFH PTGMVWPPSV KGILVTEGVR GDGGVLKNSD GKRFMFDYIP
PVFKGQYAES IEEADQWLKD NDSARRTPDL LPRDEVARAI NSEVKADRGT PHGGVYLDIA
SRLPAEEIKR RLPSMYHQFM ELAEVDITKE PMEVGPTCHY VMGGVEVDPD TGAAKTPGLF
AAGECSGGMH GSNRLGGNSL SDLLVFGRRA GMGAADYVRA LSERPKVSEQ AVDDATKLAL
APFEGPSNGD AAENPYTLQL DLQDSMNTLV GIIRKADEVT EAIEKLKELR ERYKRVRVEG
GRHFNPGWHL AIDLRNMLIV SECIAMAALE RTESRGGHTR DDHPSMDSTW RKTLLVCRAE
GDVVVPDITI TREDQIPMRE DLLELIEVEE LEKYFTPEEL ANHSARRA
//
