ID C7NA53_LEPBD Unreviewed; 443 AA.
AC C7NA53;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ACV39034.1};
GN OrderedLocusNames=Lebu_1138 {ECO:0000313|EMBL:ACV39034.1};
OS Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS 10249 / C-1013-b).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=523794 {ECO:0000313|EMBL:ACV39034.1, ECO:0000313|Proteomes:UP000001910};
RN [1] {ECO:0000313|EMBL:ACV39034.1, ECO:0000313|Proteomes:UP000001910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b
RC {ECO:0000313|Proteomes:UP000001910};
RX PubMed=21304648; DOI=10.4056/sigs.1854;
RA Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT b).";
RL Stand. Genomic Sci. 1:126-132(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; CP001685; ACV39034.1; -; Genomic_DNA.
DR RefSeq; WP_015769378.1; NC_013192.1.
DR AlphaFoldDB; C7NA53; -.
DR STRING; 523794.Lebu_1138; -.
DR KEGG; lba:Lebu_1138; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_0_0; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000001910; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 1..305
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 333..428
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 443 AA; 49443 MW; 9BA73013F83D28D7 CRC64;
MKVVVIGCTH AGTAAILNLR KINPNAEITV FERNDNISFL SCGIALYVGG VVKDPQGLFY
CSPEKLRELN VDTRMRHEVK NVDIEGKKVR VVNLETGIEF NETFDKLIIT SGSWPIIPPI
EGIDLNNILL CKNYNHSNEI IERAKHSQKV VVVGAGYIGV ELVEAFRDNG KEVVLVDAEE
RILSKYFDKE FTDVAEESFK HRGIVIATGE KVVKFEGSNG NVTKVVTDKN EYEADMVIMC
VGFLPSTSLF KGQLEMLLNG AIKVDEYMRT SNKDVMAAGD CCSVFYNPLQ KERYIPLATN
AVRMGTLAGI NLLENKVKHL GTQGTSGIKI YENNMAATGL TEESAKEEGI EVESVIAVDN
YRPEFMPTYE KVTLKVVFEK NSRRILGAQL TSKIDLTQSI NTLSVCIQNK MTVEELAFVD
FFFQPHYNKP WNFLNLAGLN SLK
//
