UniProt: A0A0Q6Z9T4

Database: UniProt
Entry: A0A0Q6Z9T4_9BRAD

LinkDB:  A0A0Q6Z9T4_9BRAD 
Original site:  A0A0Q6Z9T4_9BRAD

All links

Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (1)   
All databases (21)   

Download RDF

ID   A0A0Q6Z9T4_9BRAD        Unreviewed;       612 AA.
AC   A0A0Q6Z9T4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=ASC80_19350 {ECO:0000313|EMBL:KQW19511.1};
OS   Afipia sp. Root123D2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW19511.1, ECO:0000313|Proteomes:UP000051348};
RN   [1] {ECO:0000313|EMBL:KQW19511.1, ECO:0000313|Proteomes:UP000051348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root123D2 {ECO:0000313|EMBL:KQW19511.1,
RC   ECO:0000313|Proteomes:UP000051348};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW19511.1, ECO:0000313|Proteomes:UP000051348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root123D2 {ECO:0000313|EMBL:KQW19511.1,
RC   ECO:0000313|Proteomes:UP000051348};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQW19511.1}.
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; LMDP01000003; KQW19511.1; -; Genomic_DNA.
DR   RefSeq; WP_056300652.1; NZ_LMDP01000003.1.
DR   AlphaFoldDB; A0A0Q6Z9T4; -.
DR   STRING; 1736436.ASC80_19350; -.
DR   OrthoDB; 9806724at2; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000051348; 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:UP000051348};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN          29..424
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          479..612
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        306
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT   MOD_RES         65
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ   SEQUENCE   612 AA;  66556 MW;  4CF00672A45C24AA CRC64;
     MAANGNSASE PKNAAANGQA YPIEDHTYDV IVVGAGGAGL RAVVGCSEAG LRTACITKVF
     PTRSHTVAAQ GGISASLGNM HPDDWRWHMY DTVKGSDWLG DQDSIEYLVR NAPEAVYELE
     HWGVPFSRTE EGKIYQRPFG GMTIDFGKGQ AQRTCAAADR TGHAMLHTMY GQALRHSAEF
     FIEFFAIDLI MDDQGVCRGV IALKLDDGTI HRFRGQTTIL ATGGYGRAYA SCTSAHTCTG
     DGGGMVLRAG LPLQDMEFVQ FHPTGIYGSG CLVTEGARGE GGYLVNSEGE RFMERYAPSA
     KDLASRDVVS RAMTIEIREG RGVGKKKDHI YLHLDHLDPN ILHERLPGIS ESARIFAGVD
     VTREPIPMIP TVHYNMGGIP TNFHGEVVTK KDGDDNAVVP GLMAVGEAAC VSVHGANRLG
     SNSLIDLVVF GRAAALRCAE KLTPNASQPD LPANSAELAL GRLDHFRYAS GGTPTAKLRD
     SMQHVMQNNC AVFRTGDVLK EGKDLIHKVY GGIGDISVAD RTLVWNSDLM ETLEYDNLIS
     QAVVTMDSAA NRTESRGAHA REDFSERDDK NWMKHTLSWI DSKGVSTIDY RPVHDYTMTN
     DVQYIPPKAR VY
//

DBGET integrated database retrieval system