GenomeNet

Database: UniProt
Entry: A0A0B3SXU7_9RHOB
LinkDB: A0A0B3SXU7_9RHOB
Original site: A0A0B3SXU7_9RHOB 
ID   A0A0B3SXU7_9RHOB        Unreviewed;       600 AA.
AC   A0A0B3SXU7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000256|ARBA:ARBA00019965, ECO:0000256|RuleBase:RU362051};
DE            EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU362051};
GN   ORFNames=OA50_00275 {ECO:0000313|EMBL:KHQ55239.1};
OS   Mameliella alba.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Mameliella.
OX   NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ55239.1, ECO:0000313|Proteomes:UP000030960};
RN   [1] {ECO:0000313|EMBL:KHQ55239.1, ECO:0000313|Proteomes:UP000030960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ55239.1,
RC   ECO:0000313|Proteomes:UP000030960};
RA   Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.;
RT   "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from clonal
RT   culture of toxic dinoflagellate Alexandrium tamiyavanichii.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000030,
CC         ECO:0000256|RuleBase:RU362051};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362051};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (bacterial route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004894, ECO:0000256|RuleBase:RU362051}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004515, ECO:0000256|RuleBase:RU362051};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004515,
CC       ECO:0000256|RuleBase:RU362051}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004515, ECO:0000256|RuleBase:RU362051}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040,
CC       ECO:0000256|RuleBase:RU362051}.
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:KHQ55239.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JSUQ01000001; KHQ55239.1; -; Genomic_DNA.
DR   RefSeq; WP_043136366.1; NZ_JSUQ01000001.1.
DR   AlphaFoldDB; A0A0B3SXU7; -.
DR   STRING; 561184.SAMN05216376_103279; -.
DR   PATRIC; fig|1515334.3.peg.276; -.
DR   OrthoDB; 9806724at2; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000030960; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   NCBIfam; TIGR01816; sdhA_forward; 1.
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   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   Cell inner membrane {ECO:0000256|RuleBase:RU362051};
KW   Cell membrane {ECO:0000256|RuleBase:RU362051};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU362051};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR611281-4};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362051};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362051};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362051};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030960};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN          12..407
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          462..598
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        289
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT   MOD_RES         48
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ   SEQUENCE   600 AA;  64851 MW;  9041A47E582F4A77 CRC64;
     MAAYEYETHD YDVVVVGAGG AGLRATLGMA EQGLRTACVT KVFPTRSHTV AAQGGIAASL
     SNMGPDNWQW HMYDTVKGSD WLGDTDAMEY LAREAPKAVY ELEHYGVPFS RTEEGKIYQR
     PFGGHTTEFG EGPPVQRTCA AADRTGHAIL HTLYGQSLKN NAEFYIEYFA IDLLMEDGEC
     KGVLCWKLDD GTFHVFNAKM VVLATGGYGR AYFSATSAHT CTGDGGGMVA RAGLPLQDME
     FVQFHPTGIY GSGCLITEGA RGEGGYLTNS EGERFMERYA PTYKDLAPRD YVSRSMTMEI
     REGRGVGAEG DHIHLNLSHL PAEALAERLP GISESAKIFA GVDVTKEPIP VLPTVHYNMG
     GIPTNYWGEV LNPSADDPTA VVPGLMAVGE AGCASVHGAN RLGSNSLIDL VVFGRAAAIR
     AGKVVNPETA VPAAPVSEID KAFDRFDGIR NASGTVPTAE LRLEMQKTMQ RDAAVFRTAK
     TMAEGVEAMT AIAAKLDDIK VTDRSLVWNS DLMETLELTN LMPNALATIV GAEARKESRG
     AHAHEDFSER DDENWRVHSV ARVEGNKVDL SYRPVIVDPL TTEDEGGISL KKIAPKARTF
//
DBGET integrated database retrieval system