ID A4ZGX2_LACHE Unreviewed; 458 AA.
AC A4ZGX2;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 13-SEP-2023, entry version 57.
DE SubName: Full=Fumarate reductase {ECO:0000313|EMBL:ABH11564.1};
GN Name=frdC {ECO:0000313|EMBL:ABH11564.1};
OS Lactobacillus helveticus CNRZ32.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=326425 {ECO:0000313|EMBL:ABH11564.1};
RN [1] {ECO:0000313|EMBL:ABH11564.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNRZ32 {ECO:0000313|EMBL:ABH11564.1};
RX PubMed=17322329; DOI=10.1128/AEM.00005-07;
RA Smeianov V.V., Wechter P., Broadbent J.R., Hughes J.E., Rodriguez B.T.,
RA Christensen T.K., Ardo Y., Steele J.L.;
RT "Comparative high-density microarray analysis of gene expression during
RT growth of Lactobacillus helveticus in milk versus rich culture medium.";
RL Appl. Environ. Microbiol. 73:2661-2672(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ826060; ABH11564.1; -; Genomic_DNA.
DR RefSeq; WP_003628121.1; NC_021744.1.
DR AlphaFoldDB; A4ZGX2; -.
DR KEGG; lhv:lhe_0911; -.
DR PATRIC; fig|326425.4.peg.1174; -.
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}.
FT DOMAIN 12..436
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 458 AA; 49595 MW; 59A0A3EE2157898E CRC64;
MPNNKELKNK YDAIIVGSGG TGLTAALQAR KLGLNVVILE KNEKTGGNTS RASSGMNASE
SLVQLQEGII DNNRDFYEET LKGGGLLNDR AMLKYFVNHS ALAISWLMKY GVNLTDLTIT
GGMSKKRAHR PGSMEPVGFY LTSRLTTQVK KAGVDIFTSA KVSKLLQDKN GRVNGVEVET
EDGVKTIKAK AVLLATGGFG ASKDIIKKYR PDLVDYKTTN QPGATGDGLK LAENVGAQLI
QMNFIQVHPT ADTDNPHVYL IGEGLRGEGA ILVNKAGERF VNELSTRKIV SNAITDLHED
GAYLIFDYGV RAHFAAVEFY DQIGLVVHGD SLDQLAEKIG VDPYNLNETV SNWNKAVETH
KDKAFGRTTG MDRLLDRGPY FAIHIHPAIH YTMGGIHIDT DTEVLDTNGN VIKGLYAAGE
ASGGLHGNNR IGGNSIAETV IFGRQAGIQM TKYARTIK
//
