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Database: UniProt
Entry: D3I176_9BACT
LinkDB: D3I176_9BACT
Original site: D3I176_9BACT 
ID   D3I176_9BACT            Unreviewed;       816 AA.
AC   D3I176;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EFC74789.1};
GN   ORFNames=HMPREF0649_02258 {ECO:0000313|EMBL:EFC74789.1};
OS   Prevotella buccae D17.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=575611 {ECO:0000313|EMBL:EFC74789.1, ECO:0000313|Proteomes:UP000005080};
RN   [1] {ECO:0000313|EMBL:EFC74789.1, ECO:0000313|Proteomes:UP000005080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D17 {ECO:0000313|EMBL:EFC74789.1,
RC   ECO:0000313|Proteomes:UP000005080};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Sibley C.D., White A., Allen-Vercoe E., Strauss J., Crowley S.,
RA   Surette M.G., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella buccae Oral Taxon 560 strain D17.";
RL   Submitted (NOV-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; GG739955; EFC74789.1; -; Genomic_DNA.
DR   RefSeq; WP_004343252.1; NZ_GG739955.1.
DR   AlphaFoldDB; D3I176; -.
DR   HOGENOM; CLU_003291_3_0_10; -.
DR   OrthoDB; 9792592at2; -.
DR   Proteomes; UP000005080; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd01524; RHOD_Pyr_redox; 1.
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:SF7; NITRIC OXIDE REDUCTASE FLRD-NAD(+) REDUCTASE; 1.
DR   Pfam; PF13686; DrsE_2; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF01206; TusA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SMART; SM00450; RHOD; 1.
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;
FT   DOMAIN          463..551
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   816 AA;  88265 MW;  B99648901AED1EE9 CRC64;
     MKHLIIGGVA GGATAAARIR RADEQAEIVM IEKGKYISYA NCGLPYYIGG TIAEREKLFV
     QTPESFGRRF NIDVRVENEA TAIDTAAKTV TVRRRDGSEY TETYDRLLLS PGAVPVRPPL
     PGIDLEGIFT LRNVADTDRI KTYLDTHSVR EAVVVGGGFI GLEMAENLHA AGARVSVVEM
     AQQVMAPVDF SIASHVHSEL MGQGVDLYLG KGVERFEQAD GRLAVCLATG ERIEADLVLL
     SIGVRPATEL AASAGIALGS RGIRVDSYLQ TSAPDVYAVG DAIEFAHPLT GQPWLNYLAN
     PANRQGRIVA DNMVFGNHTE YEGAIGTSIA KVFDLTVGST GLPAKRLKQE GIDYRSSITC
     SPSHAGYYPG SFMLTTKLTF DPVSGKLYGA QCVGHEGVDK RIDEAALVIK QGGTVDDLIR
     LEHTYAPPFS SAKDPIAIAG YTARNIISGA MPIVWWREID ALDRSQVTLV DVRTPEEYAL
     GTLRGAVNIP LDDLRERLGE IPADRPVVLF CAVGLRGYLA QRILMGRGFK DVRNLSGGYK
     TYQLATQPVV NRRSGACGAA ENCGTLLPPA TGAPQPGIIR VDACGLQCPG PIMKLKQTVD
     SMAVGDCVEV TATDAGFPRD ARAWCASTGN SVEAAHAEGG RHTVIIRKGA PQAPVAAAAG
     ERNKTFIMFS DDLDRALATF VLANGAAATG RKVSIFFTFW GLNVIKKEHK PAVRKDIFGR
     MFSWMLPSDS RRLKLSKMSM LGIGDRMMRY IMRSKNIYSL EEMRRQALDN GVEFIACQMS
     MDMMGIVQEE LLDGVTIGGV ATYMERAEQA NVNLFI
//
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