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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//