ID M0ELP0_9EURY Unreviewed; 609 AA.
AC M0ELP0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=C464_06538 {ECO:0000313|EMBL:ELZ48660.1};
OS Halorubrum coriense DSM 10284.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227466 {ECO:0000313|EMBL:ELZ48660.1, ECO:0000313|Proteomes:UP000011509};
RN [1] {ECO:0000313|EMBL:ELZ48660.1, ECO:0000313|Proteomes:UP000011509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10284 {ECO:0000313|EMBL:ELZ48660.1,
RC ECO:0000313|Proteomes:UP000011509};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
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:ELZ48660.1}.
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DR EMBL; AOJL01000027; ELZ48660.1; -; Genomic_DNA.
DR RefSeq; WP_006112812.1; NZ_AOJL01000027.1.
DR AlphaFoldDB; M0ELP0; -.
DR STRING; 1227466.C464_06538; -.
DR PATRIC; fig|1227466.3.peg.1319; -.
DR OrthoDB; 23539at2157; -.
DR Proteomes; UP000011509; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
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; 4.10.80.40; succinate dehydrogenase protein 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; IPR003952; FRD_SDH_FAD_BS.
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 InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 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 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.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..387
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 480..609
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 609 AA; 66381 MW; BD1C002F54E30021 CRC64;
MYEHDVVVVG AGGAGLRAAI AAQEAGADVA MVSKLHPVRS HTGAAEGGIN AALRDADSWQ
DHAYDTMKGS DYLGDAPAVE ALCQESPEEV IRLEHWGMPF SREDDGRVSQ RPFGGLSFPR
TTYAGAETGH QMLHTMYEQV VKRGITVYDE WHVMDLAVTD EDDPAERTCH GVVAYDIQSG
EISGFRAENG VILATGGMGQ VFDHTTNAVA NTGDGVAMAY RAGVPMEDME FIQFHPTTLP
STGVLISEGV RGEGGILYNS EGERFMFEHG YANNDGELAS RDVVSRAELT EVNEGRGIED
EYVHLDMRHL GEERILDRLE NILHLAEDFE GADGLTEPMP VKPGQHYAMG GIETNEFGET
VIDGLYAAGE CACASVHGAN RLGGNALPEL IVFGKRAGRH AAGEEMGEAE IETGRSGDWQ
PADYEFGVEV GETGGSGTAA ADGGAVVTDA ESVLGGAVDR AQERVDELLS RKGRNHAEIR
SAVQETMTGN VNVFREEGRL EETLGDLREA REAYKDVAVS DPSRTFNTDL IHTIETRNIL
DLAEALTMGA LAREEFRGAH WRKEHQERKD QDWLKHTLIS WNDGEPELWY KPVVLEGENK
TYEPKSRSY
//
