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Database: UniProt
Entry: A0A2Z6I9X7_9BURK
LinkDB: A0A2Z6I9X7_9BURK
Original site: A0A2Z6I9X7_9BURK 
ID   A0A2Z6I9X7_9BURK        Unreviewed;       486 AA.
AC   A0A2Z6I9X7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:BBF23301.1};
GN   ORFNames=SUTMEG_11920 {ECO:0000313|EMBL:BBF23301.1};
OS   Sutterella megalosphaeroides.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=2494234 {ECO:0000313|EMBL:BBF23301.1, ECO:0000313|Proteomes:UP000271003};
RN   [1] {ECO:0000313|EMBL:BBF23301.1, ECO:0000313|Proteomes:UP000271003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6FBBBH3 {ECO:0000313|EMBL:BBF23301.1,
RC   ECO:0000313|Proteomes:UP000271003};
RX   PubMed=30394865; DOI=10.1099/ijsem.0.003096;
RA   Sakamoto M., Ikeyama N., Kunihiro T., Iino T., Yuki M., Ohkuma M.;
RT   "Mesosutterella multiformis gen. nov., sp. nov., a member of the family
RT   Sutterellaceae and Sutterella megalosphaeroides sp. nov., isolated from
RT   human faeces.";
RL   Int. J. Syst. Evol. Microbiol. 68:3942-3950(2018).
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|RuleBase:RU366062}.
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DR   EMBL; AP018786; BBF23301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z6I9X7; -.
DR   KEGG; sutt:SUTMEG_11920; -.
DR   Proteomes; UP000271003; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding 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; IPR010960; Flavocytochrome_c.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU366062};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU366062};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU366062};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271003}.
FT   DOMAIN          40..468
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   486 AA;  51641 MW;  E93B03D4BD5D5AF5 CRC64;
     MLNRRHFIAG AVASTATFAG AERAEDLCAK PAQWDESFEV VVIGAGGAGL SAAIVARGAG
     AKTLLLEKMA FAGGNTLIAG GGMNAAVKAD YEKAGIKDSP ELHAEQTLAA GDYRADPALV
     EVLTKGAPES VAWLKKLGVN FRDHIYQIYG GLYPRCRNPI EPKGEGYIKA LAEEAKRVGV
     DIRYGAKVTR IFRESPLEGR VTGVEVEIKG KKFAIEAKSG VVSAAGGFSA NAAMCGLHDP
     RLEKLGTTNQ PGATGEVLVA MVDIGADTTG LDYIQCVPGT PKDVKSQPSL ISHVDRFLFI
     NHEGKRFVAE DSRRDILRDA VLAQTKMEAF TLVDRAGFAM DKNSTEAQHE AARKAGALYV
     GNTVEEIARA MGVPADALKA TLDDYNRAVE TKKDSFGRHE DMLVHAIAEP PFYAVRIVMA
     RHHTMGGVRI DTKARVVDRR GKAIPGLYAA GEVTGGIHGT NRVGGNALAD VFTFGRIAGE
     SAAKKL
//
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