ID R5KBR1_9BACT Unreviewed; 810 AA.
AC R5KBR1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:CCY64165.1};
GN ORFNames=BN467_00125 {ECO:0000313|EMBL:CCY64165.1};
OS Prevotella sp. CAG:1124.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262920 {ECO:0000313|EMBL:CCY64165.1, ECO:0000313|Proteomes:UP000017956};
RN [1] {ECO:0000313|EMBL:CCY64165.1, ECO:0000313|Proteomes:UP000017956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1124 {ECO:0000313|Proteomes:UP000017956};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCY64165.1}.
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DR EMBL; CAYO010000013; CCY64165.1; -; Genomic_DNA.
DR AlphaFoldDB; R5KBR1; -.
DR Proteomes; UP000017956; 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: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; 1.
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:UP000017956}.
FT DOMAIN 463..551
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 810 AA; 87851 MW; C114F6405B6EBC25 CRC64;
MKHVIIGGVA GGATAAARLR RVDETSEIIL LEKGKYISYA NCGLPYYIGG VIEERSKLLL
QTPESFGKRF RIDVRVENEV TVLHPDKKTI TVRRADGSEY EETYDKLLLS PGSTPVRLPL
EGIDLDGIFT LRNVEDTDRI KHYLTEKQVR RTVVVGAGFI GLEMAENLHH AGVSVSIVEM
GNQVMAPIDY SMAAPIHQHL ADKGVALYLE EGVTGFSHEK NGLLVHLKSG KSIATDMVLL
SIGVRPATAL AKAAGIKLGE TGGIWVDSYL QTSEKDIYAV GDAIEFPHPL TGKPWLNYLA
NPANRQGRIV ADNMALGNSV TYEGAIGTSI AKVFDLTVAS TGLAAKRLKQ MGMEYRSSIT
HSSSHAGYYP DALPLTLKLT FHPTTGRLYG AQCVGHEGVD KRIDQIAQLI KHGGTVYDLI
ETEHTYAPPF SSAKDPIAIA GYVASNIISG AMPVITWREL QAEKEHILLI DTRTHEEFSF
GTIPGAVNIP VDEMRNRLND IPKDKPVVLF CAVGLRGYLA TRILAGHGYK NVRNLTGGYK
TYSAAVAPVP PPTPQSPKTA PATDNNNDGN ILKINACGLQ CPGPIMKVKQ AIDNAEPGQR
IEVTATDAVF ARDASAWCNT TGNKLIEKTE SDGRYTVVIE KGSAGPAPAT ASTGRRGKTL
ILFSDDLDKA LATFVLANGA AATGQKVSIF FTFWGLNVLK KVQKPQVQKD IFGKMFGWML
PSSSLKLKLS KMNMGGMGSR MMRYLMKRKG VDSLETLRAQ AQQQGVEFIA CQMSMDVMGI
SREELLDGVT IGGVATYMER ADQANVNLFI
//
