ID Q5NYB4_AROAE Unreviewed; 597 AA.
AC Q5NYB4;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 121.
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 Name=sdhA {ECO:0000313|EMBL:CAI09950.1};
GN ORFNames=ebA6690 {ECO:0000313|EMBL:CAI09950.1};
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI09950.1, ECO:0000313|Proteomes:UP000006552};
RN [1] {ECO:0000313|EMBL:CAI09950.1, ECO:0000313|Proteomes:UP000006552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1 {ECO:0000313|EMBL:CAI09950.1,
RC ECO:0000313|Proteomes:UP000006552};
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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}.
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DR EMBL; CR555306; CAI09950.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5NYB4; -.
DR STRING; 76114.ebA6690; -.
DR KEGG; eba:ebA6690; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_1_4; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00223; UER01005.
DR Proteomes; UP000006552; 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: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 PRINTS; PR00411; PNDRDTASEI.
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:UP000006552};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT DOMAIN 9..404
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 462..597
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 534..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT MOD_RES 45
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ SEQUENCE 597 AA; 65036 MW; 5EF89B162A303CD8 CRC64;
MNVAKRTFDA VIVGAGGAGL RAALQLSESG LKTAVLTKVF PTRSHTVAAQ GGVAASLGNT
TEDNWHWHMY DTVKGSDWLG DQDAIEFMCR KANEVVVELE HYGMPFDRTD NGKIYQRPFG
GHSQNYGQAP VSRSCAAADR TGHAMLHALY QRNVRANTQF FVEWMALDLI RDADGDVLGV
TAIEMETGEV CIFHAKATIF ATGGAGRIFY SSTNAFINTG DGLGMAARAG VPLEDMEFWQ
FHPTGVFGAG VLITEGVRGE GGILRNASGE RFMERYAPNL KDLASRDIVS RSMVTEINEG
RGCGPDKDHV LLDITHLSPE TIMKRLPGIR EISIQFAGVD PIKAPIPVVP TAHYQMGGIP
TNFKGQVVAP KDGNPNTPIT GFYAAGECAC ASVHGANRLG TNSLLDLLVF GKSAGESVVE
DFQSGDLSLK PLPADAADVS LARLARLEGQ KNGESVFEVG LEMRRTMQKH AGVFRFDNLL
KEGVARIKEV AERAKRTEIK DKSKVWNTAR TEALELDNLI EVAKATMVSA EARKESRGAH
VRDDAPDTAE FPNGRNDNQW LKHTLWYSEG NRLDYKPVTM EPLSQDVEPI ALAKRTY
//
