ID C9KNE3_9FIRM Unreviewed; 616 AA.
AC C9KNE3;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Succinate dehydrogenase or fumarate reductase, flavoprotein subunit {ECO:0000313|EMBL:EEX68567.1};
GN ORFNames=MITSMUL_04631 {ECO:0000313|EMBL:EEX68567.1};
OS Mitsuokella multacida DSM 20544.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=500635 {ECO:0000313|EMBL:EEX68567.1, ECO:0000313|Proteomes:UP000003671};
RN [1] {ECO:0000313|EMBL:EEX68567.1, ECO:0000313|Proteomes:UP000003671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20544 {ECO:0000313|EMBL:EEX68567.1,
RC ECO:0000313|Proteomes:UP000003671};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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:EEX68567.1}.
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DR EMBL; ABWK02000017; EEX68567.1; -; Genomic_DNA.
DR RefSeq; WP_005841391.1; NZ_GG697142.2.
DR AlphaFoldDB; C9KNE3; -.
DR STRING; 500635.MITSMUL_04631; -.
DR GeneID; 78516087; -.
DR PATRIC; fig|500635.8.peg.1348; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_2_9; -.
DR Proteomes; UP000003671; Unassembled WGS sequence.
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; 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 InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 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 Pfam; PF10518; TAT_signal; 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; PS51318; TAT; 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 46..432
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 491..616
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 616 AA; 67751 MW; 8A348BB903EA106E CRC64;
MSREISRRTF IKGAAAAGVV LAAGSYFTWN GRNIPEKVQR GDVTYDVLII GSGGAGMRAA
LAAAENKDLK VAVLTKLVPT RSASTMAQGG MNGVTGVTDP NDSFESHAFD TIKGGDYLCD
QDAVEYFVER AGKNIYEMDY MGYPYNRQAD GHFHQRKMGG HAHARAAYFE DRAGHAMVHT
LFEQCLAHDI DFISECQMLE ISMAGEKKDK LAGVIAMDMR SGNIIGIPAK TIIIATGGYG
RAYWVRTSNP YSSTGDGIVA GMNVGIPFKD PEMVQFHPTG LAVNGVLLSE SSRAEGALLI
NKDGERFMQK YAPEKMELAT RDIVARAIAT EIEQGRGIGE GITAGVYLDF TKIPPERIHE
RLGQVADLSL RFAGVDITKE PVLISPTCHY SMGGLEMADF HTGETRVPGI YTAGECSCVS
VHGANRLGAN SLSEVLVFGH TAGDGAAAYA KAHQYEGSQD QLTKDSKKWL DSFEEVTSRP
HDGNRTVPEI RDDMVKTMWF KAGVFRNGPD LEAAAKELSV LEDQYKNCYV GDTSHVYNTA
YEQYVELGNL LQISQAIVQG AIARKESRGA HTRRDYPKRD DQNFLKHTLV FKEDGKYRFE
YKDVVVTKYE PKERKY
//
