ID I6T3S4_ENTHA Unreviewed; 503 AA.
AC I6T3S4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:AFM69226.1};
DE EC=1.3.1.6 {ECO:0000313|EMBL:AFM69226.1};
GN OrderedLocusNames=EHR_01170 {ECO:0000313|EMBL:AFM69226.1};
OS Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=768486 {ECO:0000313|EMBL:AFM69226.1, ECO:0000313|Proteomes:UP000002895};
RN [1] {ECO:0000313|EMBL:AFM69226.1, ECO:0000313|Proteomes:UP000002895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB
RC 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R
RC {ECO:0000313|Proteomes:UP000002895};
RX PubMed=22933757; DOI=10.1128/JB.01075-12;
RA Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT a model organism for the study of ion transport, bioenergetics, and copper
RT homeostasis.";
RL J. Bacteriol. 194:5126-5127(2012).
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; CP003504; AFM69226.1; -; Genomic_DNA.
DR RefSeq; WP_010738297.1; NZ_KB946233.1.
DR AlphaFoldDB; I6T3S4; -.
DR KEGG; ehr:EHR_01170; -.
DR PATRIC; fig|768486.10.peg.2434; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_5_9; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000002895; Chromosome.
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; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000002895};
KW Signal {ECO:0000256|RuleBase:RU366062}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT CHAIN 23..503
FT /evidence="ECO:0000256|RuleBase:RU366062"
FT /id="PRO_5010500748"
FT DOMAIN 60..482
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT REGION 22..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 53745 MW; 6B836C80B0E62089 CRC64;
MKKVLKSLVV ITSVLTMGAC SADSKEKTTT STKSSEKTEV SSGASEQTYT NPAEMKDSYD
IIIVGAGGAG MTAAIEAKDA GLNPVIFEKM PVAGGNTLKS SSGMNASATK FQQADGINDS
NEAFYEETLK GGGGTNDQEL LHYFVDHSAA AIDWLDQNGI KLDNLTITGG MSEKRTHRPS
DGSAIGGYLV DGLLKNVHER KIPIFVNTDV TDIKENSGKV NEVTVQVQGE EPKEIKGNAI
VVTTGGYGAN QEVIEKYRLD LAGYVTTNQV GSTGDGITMI EKLGGQTVDM DKIQIHPTVQ
QDEGVLIGEA VRGEGAILVN QEGQRFVNEL DTRDKVSAAI TALPEKSAYL IFDQGVRDRA
KAIDFYEQKG YVTSGDDLAE LAEKVNVPAD NLAQTLEFWN KAVDTQKDDA FNRTTAVDNG
LTEPKYYAIK IAPGIHYTMG GVKINTKTEV LNKENQPITG LYAAGEVTGG LHGNNRIGGN
SVAEIIIFGR QAGQQAAKFV SEN
//
