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Database: UniProt
Entry: I2JJN4_9GAMM
LinkDB: I2JJN4_9GAMM
Original site: I2JJN4_9GAMM 
ID   I2JJN4_9GAMM            Unreviewed;       590 AA.
AC   I2JJN4;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
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:EIF43186.1};
GN   ORFNames=DOK_09981 {ECO:0000313|EMBL:EIF43186.1};
OS   gamma proteobacterium BDW918.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae.
OX   NCBI_TaxID=1168065 {ECO:0000313|EMBL:EIF43186.1, ECO:0000313|Proteomes:UP000003473};
RN   [1] {ECO:0000313|EMBL:EIF43186.1, ECO:0000313|Proteomes:UP000003473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BDW918 {ECO:0000313|EMBL:EIF43186.1,
RC   ECO:0000313|Proteomes:UP000003473};
RX   PubMed=22740675; DOI=10.1128/JB.00678-12;
RA   Kim S.M., Cho S.J., Lee S.B.;
RT   "Genome Sequence of the Unclassified Marine Gammaproteobacterium BDW918.";
RL   J. Bacteriol. 194:3753-3754(2012).
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|PIRSR:PIRSR630664-51, 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:EIF43186.1}.
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DR   EMBL; AJMK01000038; EIF43186.1; -; Genomic_DNA.
DR   AlphaFoldDB; I2JJN4; -.
DR   PATRIC; fig|1168065.3.peg.2094; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_014312_6_1_6; -.
DR   OrthoDB; 9806724at2; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000003473; 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   PRINTS; PR00368; FADPNR.
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, ECO:0000256|PIRSR:PIRSR630664-
KW   51};
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:UP000003473};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN          10..407
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          462..590
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        289
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT   BINDING         15..20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         38..53
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         224
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         390
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         401
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   BINDING         406..407
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT   MOD_RES         46
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ   SEQUENCE   590 AA;  64131 MW;  AF719F195C5BD8EB CRC64;
     MANIRTISFD GVIVGGGGAG MRAALQLAQS GYKTAVISKV FPTRSHTVSA QGGITCAIAS
     SDPQDQWQWH MYDTVKGSDY IGDQEAIEYM CQVGPEAVYE LDHMGMPFSR TEEGRIYQRP
     FGGQSKNFGE GGQAARTCAA ADRTGHALLH TLYQGNLKNN TVFFNEWYAT DLVKNEDGEV
     VGVIAICIET GEVVYVKSKA TVFATGGAGR IYASTTNAHI NTGDGVGMAL RAGFPVQDIE
     MWQFHPTGIA GAGVLVTEGC RGEGGYLVNK DGERFMERYA PNAKDLAGRD VVARSMTLEI
     LEGRGCGPNG DHVYLKLDHL GEEVLESRLP GICELSRTFA HADPVKEPVP VVPTCHYMMG
     GIPTNVNGQA LTVDADGNDT VIPGLFACGE VACVSVHGAN RLGGNSLLDL VVFGRSAGLF
     IEKSLREGVE MRDASEADIE RAMSRLNKIN NTTGGESVSA LRTELQTIMQ NHFGVFRRGD
     FMQEGIKKLA ELRVRIDNAH LEDKSNAYNT ARIEALELHN LFEVAEATAI AAEARTESRG
     AHAREDFTER DDENWLCHSV YFPSEKRVGK RAVNFTPKTR EAFAPKIRTY
//
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