ID D1CFJ6_THET1 Unreviewed; 576 AA.
AC D1CFJ6;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 OrderedLocusNames=Tter_0785 {ECO:0000313|EMBL:ACZ41702.1};
OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC Bacteria; Chloroflexota; Thermobaculum.
OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41702.1, ECO:0000313|Proteomes:UP000000323};
RN [1] {ECO:0000313|EMBL:ACZ41702.1, ECO:0000313|Proteomes:UP000000323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX PubMed=21304745;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M., Tice H.,
RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Lu M., Brettin T., Detter J.C., Goker M.,
RA Tindall B.J., Beck B., McDermott T.R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT "Complete genome sequence of 'Thermobaculum terrenum' type strain (YNP1).";
RL Stand. Genomic Sci. 3:153-162(2010).
RN [2] {ECO:0000313|Proteomes:UP000000323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX DOI=10.4056/sigs.1153107;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T).";
RL Stand. Genomic Sci. 3:153-162(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 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 -!- 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; CP001825; ACZ41702.1; -; Genomic_DNA.
DR AlphaFoldDB; D1CFJ6; -.
DR STRING; 525904.Tter_0785; -.
DR KEGG; ttr:Tter_0785; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_1_0; -.
DR OrthoDB; 9806724at2; -.
DR UniPathway; UPA00223; UER01005.
DR Proteomes; UP000000323; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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:UP000000323};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT DOMAIN 6..397
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 451..576
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 283
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT BINDING 11..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 35..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 380
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 396..397
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT MOD_RES 43
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ SEQUENCE 576 AA; 64570 MW; F86FF56CE5F7FA6E CRC64;
MYHRYDAVIV GAGGAGLMAA LQLAQNPNIR TAVISKLYPT RSHTGAAQGG IGAALGNLEE
DHWEWHMFDT IKGGDYLVDQ DAAEILAREA IEGVYELEHY GLPFSRTPDG KIDQRRFGGH
TRNFGEGPVR RSCFAADRTG HMILQTLYQQ CIKHDVHFFS EFQLLDLIFQ DDACCGVVAL
NIQDGEIHVF HSKAVLLAVG GYGRAWKITS NALACTGDGV AIVYRHGLPL EDMEMYQFHP
TGVYKLGILL TEGARGEGGI LRNNLGERFM ERYAPTLLDL APRDMVSRCI YQEIKEGRGI
DGKDYVHLDL THVGAEVIEK RLPDLAEFVK VYLGIDPVHQ PIPIQPTAHY AMGGIPTDVD
GRVLKDEYNT PVHGLYAAGE CACVSVHGAN RLGTNSLVDL IVFGRRSGKH MAKFVCENDL
LTLPPKPDAP AREQISELLS RKHGESPARI RDQLREEMMD KVSVVRNAKG LLQARECIQE
LKERYQHVAL QDRQTWFNSE LTETLELGSL LDISEAVIEC ALAREESRGA HYREDFPKRD
DARFLKHTLI WNKDGNKEIK YKPVTITKFQ PQERKY
//
