ID U2WCJ5_9FIRM Unreviewed; 620 AA.
AC U2WCJ5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Succinate dehydrogenase or fumarate reductase, flavoprotein subunit {ECO:0000313|EMBL:ERL25147.1};
GN ORFNames=HMPREF1985_00205 {ECO:0000313|EMBL:ERL25147.1};
OS Mitsuokella sp. oral taxon 131 str. W9106.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=1321781 {ECO:0000313|EMBL:ERL25147.1, ECO:0000313|Proteomes:UP000016614};
RN [1] {ECO:0000313|EMBL:ERL25147.1, ECO:0000313|Proteomes:UP000016614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9106 {ECO:0000313|EMBL:ERL25147.1,
RC ECO:0000313|Proteomes:UP000016614};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERL25147.1}.
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DR EMBL; AWVT01000003; ERL25147.1; -; Genomic_DNA.
DR AlphaFoldDB; U2WCJ5; -.
DR STRING; 1321781.HMPREF1985_00205; -.
DR PATRIC; fig|1321781.3.peg.197; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_2_9; -.
DR Proteomes; UP000016614; 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 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000016614};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 53..436
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 495..620
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 620 AA; 68259 MW; 6978BCF54EF467F6 CRC64;
MIRREKPMSN EISRRTFIKG AAAAGVVLSA SGCFSWNGRN IPEKVRRGDV TYDVLIIGSG
GAGMRAALAA AGNKDRKVAV MTKLVPTRSA STMAQGGMNG VTGLTDPTDS IESHAFDTIK
GGDYLCDQDA VEYFAERAGK NIFEMDYMGY PYNRQEDGHF HSRKMGGHSH PRAAYFEDRA
GHAMVHTLFE QCLDKGIDFI SECQMLEISM AGDKLAGVIA MDMRTGNFIG IPAKTVLIAT
GGYGRAYWVR TSNPYSSTGD GIVAGMKVGI PFKDPEMVQF HPTGLSVNGV LLSESSRSEG
AILLNKNRER FMEKYAPEKK ELATRDIVAR SIATEIEEGR GVGEGLTAGV YLDFTHIPAE
RIHERLGQVY DLSKRFAGVD ITKEPVLISP TCHYSMGGLE MADFHTGETR VPGIYTAGEC
SCVSVHGANR LGANSLSEVL VFGHTAGDGA AAYAKGHPYE GSQDQLAKDC AKWKDHFDEV
TTRPHEGNRT VPEIRDAMVQ TMWFKAGVFR NGPQLEEAAK ELAKHEEDYK KCYVGDPSHV
YNTAFEQYVE LGNLLQISHA IVQGAIARKE SRGGHTRRDF PKRDDANFLK HTLIFKDETG
YRAEYKDVVI TKYPPKERKY
//
