ID L7N501_MYCTO Unreviewed; 590 AA.
AC L7N501;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
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:AAK47761.1};
GN OrderedLocusNames=MT3419 {ECO:0000313|EMBL:AAK47761.1};
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331 {ECO:0000313|EMBL:AAK47761.1, ECO:0000313|Proteomes:UP000001020};
RN [1] {ECO:0000313|EMBL:AAK47761.1, ECO:0000313|Proteomes:UP000001020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh {ECO:0000313|Proteomes:UP000001020};
RX PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J., DeBoy R., Dodson R., Gwinn M., Haft D., Hickey E.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M., Salzberg S.L.,
RA Delcher A., Utterback T., Weidman J., Khouri H., Gill J., Mikula A.,
RA Bishai W., Jacobs Jr W.R.Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK47761.1; -; Genomic_DNA.
DR PIR; E70843; E70843.
DR RefSeq; WP_003417273.1; NZ_KK341227.1.
DR AlphaFoldDB; L7N501; -.
DR SMR; L7N501; -.
DR KEGG; mtc:MT3419; -.
DR PATRIC; fig|83331.31.peg.3678; -.
DR HOGENOM; CLU_014312_6_1_11; -.
DR UniPathway; UPA00223; UER01005.
DR Proteomes; UP000001020; 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 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:UP000001020};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT DOMAIN 8..401
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 456..590
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT MOD_RES 43
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ SEQUENCE 590 AA; 64826 MW; 63AB833980D73AC1 CRC64;
MICQHRYDVV IVGAGGAGMR AAVEAGPRVR TAVLTKLYPT RSHTGAAQGG MCAALANVED
DNWEWHTFDT VKGGDYLADQ DAVEIMCKEA IDAVLDLEKM GMPFNRTPEG RIDQRRFGGH
TRDHGKAPVR RACYAADRTG HMILQTLYQN CVKHDVEFFN EFYALDLALT QTPSGPVATG
VIAYELATGD IHVFHAKAVV IATGGSGRMY KTTSNAHTLT GDGIGIVFRK GLPLEDMEFH
QFHPTGLAGL GILISEAVRG EGGRLLNGEG ERFMERYAPT IVDLAPRDIV ARSMVLEVLE
GRGAGPLKDY VYIDVRHLGE EVLEAKLPDI TEFARTYLGV DPVTELVPVY PTCHYLMGGI
PTTVTGQVLR DNTSVVPGLY AAGECACVSV HGANRLGTNS LLDINVFGRR AGIAAASYAQ
GHDFVDMPPN PEAMVVGWVS DILSEHGNER VADIRGALQQ SMDNNAAVFR TEETLKQALT
DIHALKERYS RITVHDKGKR FNTDLLEAIE LGFLLELAEV TVVGALNRKE SRGGHAREDY
PNRDDVNYMR HTMAYKEIGA DKEGPELRSD VRLDFKPVVQ TRYEPKERKY
//
