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Database: UniProt
Entry: G7W5P4_DESOD
LinkDB: G7W5P4_DESOD
Original site: G7W5P4_DESOD 
ID   G7W5P4_DESOD            Unreviewed;       561 AA.
AC   G7W5P4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=NAD(FAD)-dependent dehydrogenase {ECO:0000313|EMBL:AET66982.1};
GN   OrderedLocusNames=Desor_1320 {ECO:0000313|EMBL:AET66982.1};
OS   Desulfosporosinus orientis (strain ATCC 19365 / DSM 765 / NCIMB 8382 / VKM
OS   B-1628 / Singapore I) (Desulfotomaculum orientis).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=768706 {ECO:0000313|EMBL:AET66982.1, ECO:0000313|Proteomes:UP000006346};
RN   [1] {ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Pester M.,
RA   Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA   Woyke T.;
RT   "Complete sequence of Desulfosporosinus orientis DSM 765.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AET66982.1, ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR   EMBL; CP003108; AET66982.1; -; Genomic_DNA.
DR   RefSeq; WP_014183803.1; NC_016584.1.
DR   AlphaFoldDB; G7W5P4; -.
DR   STRING; 768706.Desor_1320; -.
DR   KEGG; dor:Desor_1320; -.
DR   PATRIC; fig|768706.3.peg.1304; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG0607; Bacteria.
DR   HOGENOM; CLU_003291_1_2_9; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000006346; 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; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR   PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 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; 1.
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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006346}.
FT   DOMAIN          474..560
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   561 AA;  60355 MW;  E4D19E509B4FFE93 CRC64;
     MNVIIVGGVA IGPKVAARLR RISPEAVITI IERGSLISYG GCGLPLYVGN LVPKLDDLMM
     TSYGVLRDSE FFRKQKNINV RTQTEALKID RGNKTVLVRD LVANTEEALP YDYLILATGA
     KPSIPPIPGV DLGQIFTFHH PQDAQKVKEL IKLKKIKHVT IIGSGLIGIE TADALASPRL
     KVTVCEADSR VLPKLLDSDM SKLVEQKMKG HDVELLLSCK VKGFEGDAEG NVCRVVTEQG
     TINTEAVIIA TGVRPEISLA QEAGLTIGNT GAIKVDEHQL TSDPAIYAGG DCTEQRHLIT
     EEPVYIPLAS TANKQGRVIA DHIAGLPSRF APVEGTSILQ AFDFNIGRTG LSEEEARKRG
     YNVVTSVSSG LDATHYYPMH GLITIKLIAE HENGRLLGAQ VCGIGESAKR LDVLVTALKF
     GAKVKDLIDL DLAYAPPFAT AIDVLIHAAT TLENIRRGIA IGITAEDVTK RLNAGEKLCI
     LDIREPDEVA ANPLAVPGTM VIGLGELRER WKEIPRDCLI VTVCGLGIRG YEAACMLQAK
     GITQVAFLEG GLNVGSAFFK Q
//
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