ID A0A177HM42_9ACTN Unreviewed; 651 AA.
AC A0A177HM42;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:OAH11679.1};
DE EC=1.3.5.1 {ECO:0000313|EMBL:OAH11679.1};
GN Name=sdhA_2 {ECO:0000313|EMBL:OAH11679.1};
GN ORFNames=STSP_50150 {ECO:0000313|EMBL:OAH11679.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH11679.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH11679.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAH11679.1}.
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DR EMBL; LOHS01000104; OAH11679.1; -; Genomic_DNA.
DR RefSeq; WP_067282165.1; NZ_LOHS01000104.1.
DR AlphaFoldDB; A0A177HM42; -.
DR STRING; 1716141.STSP_50150; -.
DR PATRIC; fig|1716141.3.peg.5270; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000077381; Unassembled WGS sequence.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
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; PR00368; FADPNR.
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 ECO:0000313|EMBL:OAH11679.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077381}.
FT DOMAIN 10..439
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 500..597
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 513..540
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 651 AA; 71955 MW; C5EFD15A01A4B676 CRC64;
MSEVERQQWD VVVVGAGGAG LRAAIEAREQ GARTAVICKS LFGKAHTVMA EGGIAAAMGN
VNERDNWQVH FRDTMRGGKF LNQWRMAELH SQEAPDRVWE LETWGALFDR TKDGRISQRN
FGGHEYPRLA HVGDRTGLEL IRTLQQKIVS LQQEDKRDFG DYEARLKVFQ ECTVTRVLKT
VPDSGSAAGD GRVSGVFCYD RESGRFFVLE APSVVVATGG IGKSFKVTSN SWEYTGDGHA
LALLAGAPLL NMEFVQFHPT GMVWPPSVKG ILVTESVRGD GGVLRNSEGK RFMFDYIPDV
FKDKYAESED EADRWYDDPD NNRRPPELLP RDEVARAINA EVKEGRGSPH GGVFLDVSTR
MPAEVIKRRL PSMYHQFKEL ADVDITAEAM EVGPTCHYVM GGIAVDSDTA AARGVPGLYA
AGEVAGGMHG SNRLGGNSLS DLLVFGRRAG LHAAQYAAGL TGRPIVDAEQ VDAAAAEALR
PFSAEGPTPG EPPENPYTLH QELQQTMNDL VGIIRREAEM EQALRKLAEL RVRARRAGVE
GHRQFNPGWH LALDLRNMLL VSECIARAAL ERTESRGGHT REDYPTMDRE WRHINLLCRL
ADPTGGLAAT DPVRGQISLQ RETTEPIRPD LLALFDKEEL VKYLAEEELY E
//
