ID D3QZE6_MAGIU Unreviewed; 565 AA.
AC D3QZE6;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ADC91820.1};
GN OrderedLocusNames=HMPREF0868_1589 {ECO:0000313|EMBL:ADC91820.1};
OS Mageeibacillus indolicus (strain UPII9-5) (Clostridiales genomosp. BVAB3
OS (strain UPII9-5)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Mageeibacillus.
OX NCBI_TaxID=699246 {ECO:0000313|EMBL:ADC91820.1, ECO:0000313|Proteomes:UP000008234};
RN [1] {ECO:0000313|Proteomes:UP000008234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPII9-5 {ECO:0000313|Proteomes:UP000008234};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; CP001850; ADC91820.1; -; Genomic_DNA.
DR RefSeq; WP_012992782.1; NC_013895.2.
DR AlphaFoldDB; D3QZE6; -.
DR STRING; 699246.HMPREF0868_1589; -.
DR KEGG; clo:HMPREF0868_1589; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000008234; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
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 PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 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 PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008234}.
FT DOMAIN 463..551
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 565 AA; 62062 MW; 519D00CC1636BDCD CRC64;
MGKKVVIIGG VAGGASTAAR VRRLDEFAEI KMFEMGPYVS FSNCCIPFHI SGTVKKSENL
ILMTPEEFKN QYNIDAVVNH QVISINREKK YVEVKNLLTE EVFQEKYDVL VMAPGAKAVR
PKSIAGVDGK NVFVMKTVPD LQAFMFYAEA NKVKDVAVIG GGFIGVEVAE NAKKAGYNVA
IIEAEKQILA PLDYDMVQIV NRHLYNQGVE LHLGDGVKAI ESDKVVLQSG KTVPAQAVIL
SIGVAPNTQL AREAGLELNE AGYIKVNHHY QTNDPDIYAV GDAIEVKDFF TGKATKLTLA
GPAQRQARAA ADHMYGRTYV NTGVIGSSSV KVFDMNVAST GMNEKQCQAQ GIKYGFSYII
PKDGVGLMPG SKNLFFKLLY AEPSGQVLGA QAVGLGNVTK RIDVIATTIM LHGNLEDLKE
LELEYSPNYG TAKDVVNHAA LVALNLLNGE FKKVPVTAAR KLVEENAFII DAREENEYAV
GHVVNAINIP LSQFRNRLDE IPHDRPVYIY CRSSQRSYNM VRALGQRGYT NVYNMDGSFL
GISEYEFYND QVTGRKPIVT AYNFN
//
