ID   SDHA_SERS3              Reviewed;         588 AA.
AC   G4V4G6;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Succinate dehydrogenase flavoprotein subunit;
DE            EC=1.3.5.1;
GN   Name=sdhA {ECO:0000303|PubMed:22474332}; ORFNames=Ser39006_01869;
OS   Serratia sp. (strain ATCC 39006).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia; unclassified Serratia.
OX   NCBI_TaxID=104623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], COFACTOR, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 39006 / SC 11482;
RX   PubMed=22474332; DOI=10.1074/jbc.m111.293803;
RA   McNeil M.B., Clulow J.S., Wilf N.M., Salmond G.P., Fineran P.C.;
RT   "SdhE is a conserved protein required for flavinylation of succinate
RT   dehydrogenase in bacteria.";
RL   J. Biol. Chem. 287:18418-18428(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39006 / SC 11482;
RX   PubMed=24336377; DOI=10.1128/genomea.01039-13;
RA   Fineran P.C., Iglesias Cans M.C., Ramsay J.P., Wilf N.M., Cossyleon D.,
RA   McNeil M.B., Williamson N.R., Monson R.E., Becher S.A., Stanton J.A.,
RA   Brugger K., Brown S.D., Salmond G.P.;
RT   "Draft genome sequence of Serratia sp. strain ATCC 39006, a model bacterium
RT   for analysis of the biosynthesis and regulation of prodigiosin, a
RT   carbapenem, and gas vesicles.";
RL   Genome Announc. 1:E01039-E01039(2013).
RN   [3]
RP   COFACTOR, SUBUNIT, AND MUTAGENESIS OF HIS-45.
RC   STRAIN=ATCC 39006 / SC 11482;
RX   PubMed=24070374; DOI=10.1021/bi401006a;
RA   McNeil M.B., Fineran P.C.;
RT   "The conserved RGxxE motif of the bacterial FAD assembly factor SdhE is
RT   required for succinate dehydrogenase flavinylation and activity.";
RL   Biochemistry 52:7628-7640(2013).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 39006 / SC 11482;
RX   PubMed=24374335; DOI=10.1016/j.febslet.2013.12.019;
RA   McNeil M.B., Hampton H.G., Hards K.J., Watson B.N., Cook G.M.,
RA   Fineran P.C.;
RT   "The succinate dehydrogenase assembly factor, SdhE, is required for the
RT   flavinylation and activation of fumarate reductase in bacteria.";
RL   FEBS Lett. 588:414-421(2014).
CC   -!- FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are
CC       responsible for the catalysis of fumarate and succinate
CC       interconversion; the fumarate reductase is used in anaerobic growth,
CC       and the succinate dehydrogenase is used in aerobic growth.
CC       {ECO:0000250|UniProtKB:P0AC41, ECO:0000305|PubMed:24374335}.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:22474332, ECO:0000269|PubMed:24070374};
CC       Note=Flavinylated by SdhE, flavinylation occurs at a very low level in
CC       the absence of SdhE. {ECO:0000269|PubMed:24070374};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (bacterial route): step 1/1.
CC   -!- SUBUNIT: Makes weak or transient interactions with SdhA
CC       (PubMed:22474332, PubMed:24070374). Part of an enzyme complex
CC       containing four subunits: a flavoprotein, an iron-sulfur, cytochrome b-
CC       556, and a hydrophobic anchor protein. The complex forms trimers.
CC       {ECO:0000250|UniProtKB:P0AC41, ECO:0000269|PubMed:22474332,
CC       ECO:0000269|PubMed:24070374}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:22474332}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P0AC41}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P0AC41}.
CC   -!- DISRUPTION PHENOTYPE: No effect on anaerobic growth on glycerol
CC       fumarate medium. {ECO:0000269|PubMed:24374335}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily.
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DR   EMBL; HE580160; CCD22039.1; -; Genomic_DNA.
DR   EMBL; CP025084; ESN64461.1; -; Genomic_DNA.
DR   RefSeq; WP_021015135.1; NZ_CP025085.1.
DR   AlphaFoldDB; G4V4G6; -.
DR   SMR; G4V4G6; -.
DR   STRING; 104623.Ser39006_01869; -.
DR   eggNOG; COG1053; Bacteria.
DR   OrthoDB; 153138at2; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000017700; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; -; 1.
DR   Gene3D; 3.90.700.10; -; 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   PANTHER; PTHR11632; PTHR11632; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   SUPFAM; SSF46977; SSF46977; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF56425; SSF56425; 1.
DR   TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR   TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Electron transport; FAD; Flavoprotein;
KW   Membrane; Oxidoreductase; Reference proteome; Transport;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..588
FT                   /note="Succinate dehydrogenase flavoprotein subunit"
FT                   /id="PRO_0000438887"
FT   ACT_SITE        286
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC41"
FT   MOD_RES         45
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000305|PubMed:24070374"
FT   MUTAGEN         45
FT                   /note="H->S: No binding of FAD."
FT                   /evidence="ECO:0000269|PubMed:24070374"
SQ   SEQUENCE   588 AA;  64536 MW;  32B438FF020D0CE0 CRC64;
     MNLPVREFDA VVIGAGGAGM RAALQISQMG LSCALLSKVF PTRSHTVSAQ GGITVALGNT
     HEDNWEWHMY DTVKGSDYIG DQDAIEYMCK TGPEAVLELE HMGLPFSRLD DGSIYQRPFG
     GQSRNFGGEQ AARTAAAADR TGHALLHTLY QQNLKNHTTI FSEWYALDLV KNQDGAVMGC
     TAICIETGEV VYFKARATVL ATGGAGRIYQ STTNAHINTG DGVGMALRAG VPVQDMEMWQ
     FHPTGIAGAG VLVTEGCRGE GGYLLNKHGE RFMERYAPNA KDLAGRDVVA RSIMIEIREG
     RGCDGPWGPH AKLKLDHLGK DVLESRLPGI LELSRTFAHV DPVKEPIPVI PTCHYMMGGI
     PTKVTGQVLA VNEQGEDVVI PGLFAVGEIA CVSVHGANRL GGNSLLDLIV FGRSAGMHLQ
     ESLEEQGATR DASNSDIEAS LDRLNRWNST RSGEDPVEIR KALQACMQHN FSVFREGDAM
     AKGLEELKVI RERLKNARLD DTSNDFNTQR IECLELDNLM ETAYATAVSA NFRTESRGAH
     SRFDYPDRDD DKWLCHTLYQ PQTESMTRRK VNMQPKLRPA FPPKVRTY