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Database: UniProt
Entry: W5T9Y4_9NOCA
LinkDB: W5T9Y4_9NOCA
Original site: W5T9Y4_9NOCA 
ID   W5T9Y4_9NOCA            Unreviewed;       594 AA.
AC   W5T9Y4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
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:AHH15919.1};
GN   ORFNames=NONO_c11120 {ECO:0000313|EMBL:AHH15919.1};
OS   Nocardia nova SH22a.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH15919.1, ECO:0000313|Proteomes:UP000019150};
RN   [1] {ECO:0000313|EMBL:AHH15919.1, ECO:0000313|Proteomes:UP000019150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH22a {ECO:0000313|EMBL:AHH15919.1};
RX   PubMed=24747905;
RA   Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT   "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT   Analysis of the Complete Genome of Nocardia nova SH22a.";
RL   Appl. Environ. Microbiol. 80:3895-3907(2014).
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   -!- 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; CP006850; AHH15919.1; -; Genomic_DNA.
DR   RefSeq; WP_025347438.1; NZ_CP006850.1.
DR   AlphaFoldDB; W5T9Y4; -.
DR   STRING; 1415166.NONO_c11120; -.
DR   KEGG; nno:NONO_c11120; -.
DR   PATRIC; fig|1415166.3.peg.1127; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_014312_6_1_11; -.
DR   OrthoDB; 9805351at2; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000019150; 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:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
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   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:UP000019150};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN          13..406
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          460..594
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        292
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT   MOD_RES         48
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ   SEQUENCE   594 AA;  65736 MW;  6D49D416A7C1CF57 CRC64;
     MSESRPVQEH RYDVVIVGAG GAGMRAAIEA GPRARTAVLT KLYPTRSHTG AAQGGMCAAL
     ANVEEDNWEW HTFDTVKGGD YLVDQDAAEI MAKEAIDAVL DLEKMGLPFN RTPEGKIDQR
     RFGGHTRDHG KAPVRRACYA ADRTGHMILQ TLYQNCVKHD VEFYNEFYVL DLVLTETERG
     SVATGVVAYE LATGEIHVFH AKSIIFATGG SGRMYKTTSN AHTLTGDGMA IVFRKGLPLE
     DMEFHQFHPT GLAGLGILIS EAVRGEGGIL RNASGERFME RYAPTIKDLA PRDIVARSMV
     KEVLEGRGGG PNKDYVFIDV THLGEDVLEE KLPDITEFAR TYLGVDPVKE PVPVMPTCHY
     VMGGIPTRIR GEVLRNNTDV LPGLYAAGEC ACVSVHGSNR LGTNSLLDIN VFGRRSGIAA
     AEYATRTEFV ELPENPAQMV QDWLTLLLSD HGNERVADIR TDLQVTMDAN AAVFRTEETL
     KTALTDIHAL KERYQHISVQ DKGKRYNSDL LEAVELGFLL ELAEVTVVGA LNRKESRGGH
     AREDYPDRDD VNFMRHTMAY KQVEAGKPAE LIADIQLDFK PVVQTRYEPM ERKY
//
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