ID A0A0R2J0K7_9LACO Unreviewed; 496 AA.
AC A0A0R2J0K7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Fumarate reductase (Flavoprotein) {ECO:0000313|EMBL:KRN67501.1};
GN ORFNames=IV80_GL000040 {ECO:0000313|EMBL:KRN67501.1};
OS Pediococcus cellicola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=319652 {ECO:0000313|EMBL:KRN67501.1, ECO:0000313|Proteomes:UP000051568};
RN [1] {ECO:0000313|EMBL:KRN67501.1, ECO:0000313|Proteomes:UP000051568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17757 {ECO:0000313|EMBL:KRN67501.1,
RC ECO:0000313|Proteomes:UP000051568};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRN67501.1}.
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DR EMBL; JQBR01000001; KRN67501.1; -; Genomic_DNA.
DR RefSeq; WP_057747789.1; NZ_JQBR01000001.1.
DR AlphaFoldDB; A0A0R2J0K7; -.
DR STRING; 319652.IV80_GL000040; -.
DR PATRIC; fig|319652.3.peg.41; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000051568; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
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 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051568}.
FT DOMAIN 4..461
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 496 AA; 54609 MW; D8455637392F1D3F CRC64;
MEADVVIVGA GAAGIGAAIT LADAGKKVIL LEKGDKYGGA GMFGAQGLFA VESDQQKAAG
EHYTIKQAYQ ELATYGHYRT NLSLTKSILQ QSASTISWLD DHGLKTELVA NTQEAHQHHP
RVYHQYIDKF AGFKRLIRHY QTHGGQLLLN TAGEEILQSG HEIIGVKAKH EEKEFIINCS
VVIVADGGFI GNAKMVKKYL SIDPDNLYSM GERKATGDGI RMLAQLGADT RHLGIFENHA
ASVVSPENHR WHNDTIFSLT NLPFLWVDHA GKRFVDESVC YDFALWGNAT YAAGGFYYIL
LDQRFVDFIS NHELNWTDAF ERTFKSLAHQ QTSHTVGPFS QIDVYLEEAI EMKAAWKAEN
VADLAMQLHV PATNLRATIT RYNSLIKNHA DKDFYKPANF LRFPLVQGPF YALKAKSTSL
GTIGGIETNE KLEALTAEKT PILGAFVAGN DASGMYDTSY PTLEGISCAF AWNSGRIAGK
SAIAFLQKVS SDSVKF
//
