ID K9WG01_9CYAN Unreviewed; 575 AA.
AC K9WG01;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=Mic7113_2670 {ECO:0000313|EMBL:AFZ18457.1};
OS Allocoleopsis franciscana PCC 7113.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ18457.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ18457.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ18457.1,
RC ECO:0000313|Proteomes:UP000010471};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL Submitted (JUN-2012) 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
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DR EMBL; CP003630; AFZ18457.1; -; Genomic_DNA.
DR RefSeq; WP_015182606.1; NC_019738.1.
DR AlphaFoldDB; K9WG01; -.
DR STRING; 1173027.Mic7113_2670; -.
DR KEGG; mic:Mic7113_2670; -.
DR PATRIC; fig|1173027.3.peg.2938; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_6_2_3; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000010471; Chromosome.
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 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; IPR014006; Succ_Dhase_FrdA_Gneg.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AFZ18457.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010471};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Ubiquinone {ECO:0000313|EMBL:AFZ18457.1}.
FT DOMAIN 5..395
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 450..575
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 463..490
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 575 AA; 63868 MW; 8B4CB22EFE4C07DA CRC64;
MLEHDVIIVG GGLAGCRAAL EIKRTDPNLD VALVAKTHPI RSHSVAAQGG MAATLKNVDV
EDTWEAHAFD TVKGSDYLAD QDAVEILTRE AADVVIDLEH MGVLFSRLPD GRIAQRAFGG
HSNRRTCYAA DKTGHAILHE LVNNLKRNGV RLYDEWYVMQ LIVEQGQAKG VVMFRIRDSK
VQVVRAKVVM FATGGYGRVY NTTSNDYAST GDGLAMSAFA GVPLEDMEFV QFHPTGMYPV
GVLLSEAVRG EGAYLINANG DRFMATYAPS RMELAPRDIT SRAIVREIRA GRGIHPDGSA
GGPFIYLDLR HMGREKIMSR IPFCWEEAHR LLGIDAVHEP IPVRPTVHYS MGGIPVNTDG
QVRSGPDGLI EGFFAAGEAA CVSVHGANRL GSNSLLECIV YGRRTGAAIA RYIQDRKLPD
INEQSYIRST QEQINTLMNQ SGTIRIGALR QNFQDCMTQH CGVFRTEELM QEGLNQLKQL
QQQYEQIYLD DKGTTWNTEL IEALELRSLM VVGEIILTSA LNRKESRGAH CREDYTERDD
TNFLKHTMAF YSPAGIDLNY LPVAITRFEP KERKY
//
