ID A0A286GLS5_9PROT Unreviewed; 596 AA.
AC A0A286GLS5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05421508_10569 {ECO:0000313|EMBL:SOD95934.1};
OS Caenispirillum bisanense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=414052 {ECO:0000313|EMBL:SOD95934.1, ECO:0000313|Proteomes:UP000219621};
RN [1] {ECO:0000313|EMBL:SOD95934.1, ECO:0000313|Proteomes:UP000219621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 140 {ECO:0000313|EMBL:SOD95934.1,
RC ECO:0000313|Proteomes:UP000219621};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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 ---------------------------------------------------------------------------
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; OCNJ01000005; SOD95934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286GLS5; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00223; UER01005.
DR Proteomes; UP000219621; 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:UP000219621};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT DOMAIN 12..408
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 463..596
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 290
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 596 AA; 64865 MW; 4AD62F38A1AE5FEA CRC64;
MAAYDLIDHE YDVVVVGAGG AGLRATFGMV AAGLKTACVT KVFPTRSHTV AAQGGIGASL
GNMAEDTWQW HMYDTVKGSD WLGDQDAIEY MCREAVPAVY ELEHFGVPFS RTADGKIYQR
PFGGHMRNFG EAPVQRACAA ADRTGHAILH TLYQQSLKHN AEFFVEYFAL DLLMDPVDGT
CRGVIALDMA TGELHRFRAH QTVLATGGYG RAYFSCTSAH TCTGDGNGMA ARAGLPLQDH
EFVQFHPTGI YGSGCLITEG ARGEGGYLTN SAGERFMERY APTAKDLASR DVVSRAMTME
IRESRGVGKD ADHIHLHLEH LGADVLHARL PGITETAKIF AGVDATKEPI PVLPTVHYNM
GGIPTNYMGE VLRPTAENPD AVCGGLMAVG EAACVSVHGA NRLGTNSLLD LVVFGRAAAH
RAAELVKPGT KHKPVPKSCD DLALSRLDRV RNANGSQTTQ EIRSALQRTM QNDAAVFRTS
QSLKEGCDKV SEIAGTLPQL KITDRSLVFN TDLTEALELE NLMTCALATI YGAEARHESR
GAHAHEDFPE RDDETWMKHT LAVVDHDYKV SLDYRPVHTY TLTDEIEYIA PKKRVY
//