ID M6ZYP3_9ACTN Unreviewed; 645 AA.
AC M6ZYP3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 2.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:EMP11533.2};
DE EC=1.3.5.1 {ECO:0000313|EMBL:EMP11533.2};
GN Name=sdhA {ECO:0000313|EMBL:EMP11533.2};
GN ORFNames=ISGA_5458 {ECO:0000313|EMBL:EMP11533.2};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:EMP11533.2, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:EMP11533.2, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:EMP11533.2,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(2013).
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:EMP11533.2}.
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DR EMBL; APHK02000077; EMP11533.2; -; Genomic_DNA.
DR RefSeq; WP_053777923.1; NZ_CP132196.1.
DR AlphaFoldDB; M6ZYP3; -.
DR STRING; 1241906.ISGA_5458; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000011989; 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 GO; GO:0008202; P:steroid 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; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01811; sdhA_Bsu; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF53; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EMP11533.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000011989}.
FT DOMAIN 44..449
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 511..644
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 645 AA; 70027 MW; 0AB8F1A03C3609D3 CRC64;
MSIGPTIEQL LDSGVPEGDP ATAWQRRRDA YRLVGPLNRG KFTVIVVGTG LAGAGCAAAL
GELGYDVHAF TFHDAPRRAH SVAAQGGINA ARARKVDNDS IRRFVVDTVK GGDFRAREAD
AFRLAEESIR VIDHLDAIGA PFAREYGGSL ATRSFGGVQV SRTYYTRGQT GQQLQVAASQ
ALLRQVAAGS VTLHTRSEML DLIVADGRAQ GIVVRDLVTG RIGARTAHAV VLATGGYGTV
FFQSTLARNS NATAAWRAHR RGALMASPSF IQFHPTALPV SAPWQTKTTL MSESLRNDGR
IWVPRTAGDE RAANDIPDAD RDYYLERKYP AYGNLTPRDV ASRAAREQIE AGHGVGPLRN
SVYLDFADAL ARLGRATIAE RYGNLFSMYH DATGENPYEV PMRIAPAAHF TMGGLWSDYD
QMTSIPGLFV GGEAGWGYHG ANRLGANSLL SACVDGWFTL PYSIPNYLAP LLGEGRLPLD
HDAVRAAVGA VTGRITDLLD VGGRTGPDRF HRRLGEILYA GCGVARSPAG LTSAIGEIRS
LREQFWSDVR VVGSASEFNQ ELERAGRVAD FLELAELMCV DALDRDESCG AHFRVDHQTA
QGEARRDDDH WCAVSAWETT TDGRHIRHRE PLAFDAVPLQ TRNYQ
//