ID E5BEL3_9FUSO Unreviewed; 815 AA.
AC E5BEL3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EFS20544.1};
GN ORFNames=FSBG_00041 {ECO:0000313|EMBL:EFS20544.1};
OS Fusobacterium gonidiaformans 3-1-5R.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=469605 {ECO:0000313|EMBL:EFS20544.1, ECO:0000313|Proteomes:UP000002975};
RN [1] {ECO:0000313|EMBL:EFS20544.1, ECO:0000313|Proteomes:UP000002975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_5R {ECO:0000313|EMBL:EFS20544.1,
RC ECO:0000313|Proteomes:UP000002975};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E.,
RA Nusbaum C., Galagan J., Birren B.;
RT "The Genome Sequence of Fusobacterium sp. 3_1_5R.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the sulfur carrier protein TusA family.
CC {ECO:0000256|ARBA:ARBA00008984}.
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DR EMBL; GG657971; EFS20544.1; -; Genomic_DNA.
DR AlphaFoldDB; E5BEL3; -.
DR HOGENOM; CLU_003291_3_1_0; -.
DR BioCyc; FSP469605-HMP:GTSP-42-MONOMER; -.
DR Proteomes; UP000002975; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.1260.10; DsrEFH-like; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 3.30.110.40; TusA-like domain; 1.
DR InterPro; IPR032836; DsrE2-like.
DR InterPro; IPR027396; DsrEFH-like.
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 InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001455; TusA-like.
DR InterPro; IPR036868; TusA-like_sf.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 1.
DR Pfam; PF13686; DrsE_2; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF01206; TusA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF75169; DsrEFH-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF64307; SirA-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS01148; UPF0033; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002975}.
FT DOMAIN 472..556
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 815 AA; 90831 MW; 291685D6409B079F CRC64;
MIYIVLEEKR KMSKKIVIVG GVAGGASTAT RLRRLSEEYE IIMFEKGPYP SFANCGLPYH
IGNIIPERES LIVQTPEKFK SRFQIDVRTL SEVIAVNTKE KKVQVRIQNG KLYEESYDVL
VLSPGAKAWK AEIEGIHSHN IFSLKTIPDM DKIIAKLKNK VCKRVAIIGG GFIGIEAAEN
IKHLGIETIL IEAGDHILSS FDSEFSENLE EEMREQGVEL YLKQRVVKFQ DGKELSLFLE
NGEIVEVDFV IMAMGVRPDT AFLKNSGITL GKRGEILVNE YLETNIQDVY ALGDAIPGVA
LAGPANRQGR IVANNIFGKR EKYCGSIGSS IIKVFDIVGA AAGKNEKQLK VEGIEYETVH
LYPNSHAGYY PNATQLHAKI LFEKESGILL GAQCIGYEGV DKFIDVMATS MHFKGTIYDL
SELELCYAPP FGSAKSPVNM AGFIGRNIED HLMETVSKEE MEDFNIQKHF RLDLRNPEES
SVALAECEAS IPLDELRDHL EELPKEKEIW CYCAVGLRGY LATRILMQHG FRVKNILGGY
RLLPKDWKIE NSKEETSNIE KKEEETLYQK KEMEILNVTG LSCPGPLMKL KSKMESMEEG
KDLHIIASDP AFANDVQAWV KASGNHLYEV KKEKGFVHAY LSKKESGLVH SSDTKVMETK
EGMTIVVFSG DYDKAMAAFV IANGALAMGK RVTMFFTFWG LSILKKENPI AVKKSFIDCL
FSVCLPKSWK NLPLSKMNFG GLGAKMMQVI MKRKNIESLD SLIQNAKENG VHIIACTMSM
DAMGIVKEEL LDGIDFGGVA QYLGAANEGN PNLFI
//
