ID E3D9A2_GARV3 Unreviewed; 663 AA.
AC E3D9A2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN OrderedLocusNames=HMPREF0421_20564 {ECO:0000313|EMBL:ADP38646.1};
OS Gardnerella vaginalis (strain ATCC 14019 / 317).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP38646.1, ECO:0000313|Proteomes:UP000001453};
RN [1] {ECO:0000313|EMBL:ADP38646.1, ECO:0000313|Proteomes:UP000001453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA Wilson B.A.;
RT "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT differences in metabolic and virulence potential.";
RL PLoS ONE 5:E12411-E12411(2010).
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 -!- 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}.
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DR EMBL; CP002104; ADP38646.1; -; Genomic_DNA.
DR RefSeq; WP_009994796.1; NC_014644.1.
DR RefSeq; YP_003985669.1; NC_014644.1.
DR AlphaFoldDB; E3D9A2; -.
DR KEGG; gvg:HMPREF0421_20564; -.
DR PATRIC; fig|525284.18.peg.562; -.
DR HOGENOM; CLU_014312_6_1_11; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000001453; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
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; 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 PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF89; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 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 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 30..442
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 526..638
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 663 AA; 73357 MW; 3C1CFD88454C8963 CRC64;
MQSNLSQQKE NTTTVKEKTV QIQVEQSSYD VVIIGAGAAG LSAALGLVKS EEYKTLKSQG
KQPKILVICK LQALRSHTGS AEGGIAASLG NIEKDCWQWH YYDTVHGGDW LSDQDAAKML
AKEARDTVIE LEHFGVAFSR TEDGHINQRF FGGHTADFGQ QPIRRAAYAA DRIGHQILYS
LWQKCIEENI KIEEDVYVTD LAINHKSNSA EGIIALNEKS GKVEKICARN VLIATGGAGR
LFSTTSNSWD LTGDGMSLAL NAGLQLEDIE FIQFHPTGLA HTGILLSEAA RGEGGVLRNC
KNEAFMKNYD DTHADLAPRD VVSRSIVSEI DALRGVEDTT SNIDRKDCVW LDMTRIEKQH
MLEALPQVVE TIEKYAHLDP SKDLIPIRPT AHYTMGGIPI SLNGQVYKLV NNKKQRIIGL
YAAGECACSG VHGANRLGGN SLLDACLFGK LSGKSIAKEL KEQSQEKSQE KHEEHIVDTS
KNVYDSTPNT FENLDKLSEN RVQEIIGLIQ NTSTSSNTTN PYNLLEKLEN IMENAAAVRC
SENTLKDALQ KIDTIIIPQA KILVLHSQNL VFNQELIAIW ELQNMITLAK SVLQASLARH
ESRGAFTRLD YPKRNNNQNP QHSIVDSSGE VQNIPVIIVD FDPNKPINHQ NKDEINKIMT
KID
//
