ID D2EJQ0_PEDAC Unreviewed; 460 AA.
AC D2EJQ0;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:EFA26722.1};
DE EC=1.3.1.6 {ECO:0000313|EMBL:EFA26722.1};
GN ORFNames=HMPREF9024_01012 {ECO:0000313|EMBL:EFA26722.1};
OS Pediococcus acidilactici 7_4.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus; Pediococcus acidilactici group.
OX NCBI_TaxID=563194 {ECO:0000313|EMBL:EFA26722.1, ECO:0000313|Proteomes:UP000005738};
RN [1] {ECO:0000313|EMBL:EFA26722.1, ECO:0000313|Proteomes:UP000005738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_4 {ECO:0000313|EMBL:EFA26722.1,
RC ECO:0000313|Proteomes:UP000005738};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., McDonald J., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Pediococcus acidilactici strain 7_4.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; GG730085; EFA26722.1; -; Genomic_DNA.
DR RefSeq; WP_002830094.1; NZ_GG730085.1.
DR AlphaFoldDB; D2EJQ0; -.
DR HOGENOM; CLU_011398_4_5_9; -.
DR Proteomes; UP000005738; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016156; F:fumarate reductase (NADH) activity; IEA:UniProtKB-EC.
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; PR00411; PNDRDTASEI.
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}.
FT DOMAIN 17..441
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 460 AA; 49331 MW; 8B23FB391724075E CRC64;
MTQSQSIQSI AAENQFDTVI VGAGSAGLVS ALALAEAGKR VIVLEKMAKP GGNSIRASSG
MNAAKTVVQE HAGIKDTYES FFEDTYRGGG RKNNVDMLRY FTSHAAEAVD WLKEHGIVLD
DLTLTGGMSV KRAHRPSSAP AIGGYLIHHL VDDLTQKQVP ILCQTKVVNI MRMESGDFQL
IAENQAGDRQ TLRSATVILA TGGFSASQDL IAYYRPDLLH YRTTNQPGAT GDGLRLAQQL
GAQLIDMAEV QVHPTVYQDS ARTFLIGETV RGEGAILVNH QGRRFVNELA TRKEVTAAIN
AQSPANAFLI FNQALINRVV AVQFYDQIGL VTHGATLAEL ADQLEIPQAA LDTTMATWQT
VVHQQHDAEF GRTTGLVDDF ATGPFAAIPV APAVHYTMGG VKVNVETQVL DDQQQPIAGL
YAAGETVGGL HGNNRLGGNS IAETVVFGLA AARQIENYQV
//
