UniProt/TrEMBL: A0A0N9Y3R2

Database: UniProt/TrEMBL
Entry: A0A0N9Y3R2_MYCFO

LinkDB:  A0A0N9Y3R2_MYCFO 
Original site:  A0A0N9Y3R2_MYCFO

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (12)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   A0A0N9Y3R2_MYCFO        Unreviewed;       584 AA.
AC   A0A0N9Y3R2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 45.
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_1 {ECO:0000313|EMBL:STZ72715.1};
GN   ORFNames=NCTC1542_00253 {ECO:0000313|EMBL:STZ72715.1}, XA26_17610
GN   {ECO:0000313|EMBL:ALI25608.1};
OS   Mycolicibacterium fortuitum (Mycobacterium fortuitum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1766 {ECO:0000313|EMBL:ALI25608.1, ECO:0000313|Proteomes:UP000057134};
RN   [1] {ECO:0000313|EMBL:ALI25608.1, ECO:0000313|Proteomes:UP000057134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT6 {ECO:0000313|EMBL:ALI25608.1,
RC   ECO:0000313|Proteomes:UP000057134};
RX   PubMed=26507234; DOI=10.1128/mBio.01520-15;
RA   Costa K.C., Bergkessel M., Saunders S., Korlach J., Newman D.K.;
RT   "Enzymatic Degradation of Phenazines Can Generate Energy and Protect
RT   Sensitive Organisms from Toxicity.";
RL   MBio 6:e01520-e01515(2015).
RN   [2] {ECO:0000313|EMBL:STZ72715.1, ECO:0000313|Proteomes:UP000255389}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC1542 {ECO:0000313|EMBL:STZ72715.1,
RC   ECO:0000313|Proteomes:UP000255389};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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         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; CP011269; ALI25608.1; -; Genomic_DNA.
DR   EMBL; UGQY01000001; STZ72715.1; -; Genomic_DNA.
DR   RefSeq; WP_003882377.1; NZ_VHPZ01000076.1.
DR   STRING; 1766.XA26_17610; -.
DR   GeneID; 83874531; -.
DR   KEGG; mft:XA26_17610; -.
DR   PATRIC; fig|1766.6.peg.1741; -.
DR   OrthoDB; 9805351at2; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000057134; Chromosome.
DR   Proteomes; UP000255389; Unassembled WGS sequence.
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:UP000057134};
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          455..584
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   584 AA;  64310 MW;  01EAC47ADDC049E6 CRC64;
     MIQEHRYDVV IVGAGGAGMR AAVEAGPRVR TAVLTKLYPT RSHTGAAQGG MCAALANVEE
     DNWEWHTFDT VKGGDYLADQ DAVEIMAKEA IDAVLDLEKM GMPFNRTPEG RIDQRRFGGH
     TRDHGKAPVR RACYAADRTG HMILQTLYQN CVKHDVEFFN EFYALDIALT ETPAGPVATG
     VIAYELATGD IHIFHAKAIV FATGGSGRMY KTTSNAHTLT GDGLGIIFRK GLPLEDMEFH
     QFHPTGLAGL GILISEAVRG EGGRLLNGEG ERFMERYAPT IVDLAPRDIV ARSMVLEVLE
     GRGAGPNKDY VYIDVRHLGE DVLEAKLPDI TEFARTYLGV DPVKELVPVY PTCHYVMGGI
     PTTVHGQVLR DNTNVIPGLY AAGECACVSV HGANRLGTNS LLDINVFGRR AGIAAAEYAA
     NHNHVDLPEN PADMVVGWVG DILSEHGNER VADIRTALQQ SMDNNAAVFR TEETLKQALT
     DIHALKERYS RITVHDKGKR YNSDLLEAIE LGFLLELAEV TVVGALNRKE SRGGHAREDY
     PDRDDTNYMR HTMAYKEGPG LLADIRLDYK PVVQTRYEPM ERKY
//

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