ID Q1GA48_LACDA Unreviewed; 489 AA.
AC Q1GA48;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Putative fumarate reductase (Flavoprotein) {ECO:0000313|EMBL:CAI97914.1};
DE EC=1.3.1.6 {ECO:0000313|EMBL:CAI97914.1};
GN OrderedLocusNames=Ldb1095 {ECO:0000313|EMBL:CAI97897.1}, Ldb1112
GN {ECO:0000313|EMBL:CAI97914.1};
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI97914.1, ECO:0000313|Proteomes:UP000001259};
RN [1] {ECO:0000313|EMBL:CAI97914.1, ECO:0000313|Proteomes:UP000001259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 {ECO:0000313|EMBL:CAI97914.1}, and ATCC 11842 / DSM
RC 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712
RC / WDCM 00102 / Lb 14 {ECO:0000313|Proteomes:UP000001259};
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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DR EMBL; CR954253; CAI97897.1; -; Genomic_DNA.
DR EMBL; CR954253; CAI97914.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1GA48; -.
DR STRING; 390333.Ldb1095; -.
DR KEGG; ldb:Ldb1095; -.
DR KEGG; ldb:Ldb1112; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_3_9; -.
DR BioCyc; LDEL390333:LDB_RS10060-MONOMER; -.
DR BioCyc; LDEL390333:LDB_RS10075-MONOMER; -.
DR Proteomes; UP000001259; Chromosome.
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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR43400:SF12; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING 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 ECO:0000313|EMBL:CAI97914.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001259}.
FT DOMAIN 4..461
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 489 AA; 54065 MW; ED3E730FE827C7D8 CRC64;
MNFDIVVVGA GASGISAALT ASECGAKVAL LEKGDKFGGA GMFGAQGLFA VESRAQKEAG
VKYSLKDAYE EIINYTHHSS NALMVKAILE ESAATIDWMA ESGLETELVT NTQEVHQEHP
RTYHQFIDKF NGFKRVMNNF LENGGVLMTE TSAEKIVQEQ GKVTAVKANR KGEEITLETK
AVILADGGFV GNKDEIKRTL AIDPDDLYSM GERKATGDGL QMLKEAGGVS DYKRIFENHA
ATVYSKTDPK WHNASLFDLT NIPLLWVNRE GKRFTNEDVV YDFALWGDSV YQIGGYYYFL
FDQATVDYLR QQALDWTSSF ERTFRLLDKK LMTYQVGPYP QLDQDLNEGI SQGAVFKADN
IQKLAEKITV DPANLTATVN RYNELVVEGK DMDLYKDDRF MTLSVKEGPF YAVRANSTTL
GTVGGALVNE HFEALNVKRQ VIDGIYAVGN DASSLYDSSY PTIEGLSNAF AWNSGRIAGR
YASAYAAKN
//
