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Database: UniProt
Entry: C7N6Z1_SLAHD
LinkDB: C7N6Z1_SLAHD
Original site: C7N6Z1_SLAHD 
ID   C7N6Z1_SLAHD            Unreviewed;       563 AA.
AC   C7N6Z1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=NAD(FAD)-dependent dehydrogenase {ECO:0000313|EMBL:ACV22676.1};
GN   OrderedLocusNames=Shel_16570 {ECO:0000313|EMBL:ACV22676.1};
OS   Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 /
OS   RHS 1) (Peptococcus heliotrinreducens).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Slackia.
OX   NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV22676.1, ECO:0000313|Proteomes:UP000002026};
RN   [1] {ECO:0000313|EMBL:ACV22676.1, ECO:0000313|Proteomes:UP000002026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1
RC   {ECO:0000313|Proteomes:UP000002026};
RX   PubMed=21304663; DOI=10.4056/sigs.37633;
RA   Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L., Kuske C.,
RA   Brettin T., Detter J.C., Han C., Pitluck S., Pati A., Mavrommatis K.,
RA   Ivanova N., Ovchinnikova G., Chen A., Palaniappan K., Schneider S.,
RA   Rohde M., Chain P., D'haeseleer P., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT   "Complete genome sequence of Slackia heliotrinireducens type strain (RHS
RT   1).";
RL   Stand. Genomic Sci. 1:234-241(2009).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP001684; ACV22676.1; -; Genomic_DNA.
DR   RefSeq; WP_012798778.1; NC_013165.1.
DR   AlphaFoldDB; C7N6Z1; -.
DR   STRING; 471855.Shel_16570; -.
DR   KEGG; shi:Shel_16570; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG0607; Bacteria.
DR   HOGENOM; CLU_003291_1_2_11; -.
DR   Proteomes; UP000002026; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002026}.
FT   DOMAIN          465..547
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   563 AA;  60393 MW;  7E61080179502892 CRC64;
     MKVVIVGGVA GGASAAARIR RLDETAEIIV FERTGYVSYA NCGLPYFVGG VITDPGALTL
     QTPESFLRRF RVDMRVHHEV EAINPDLKTV TVRNLETGEV FDEPYDKLLL SPGAKPTVPR
     LAGVDGKRVF TLRTVEDTFA MRNFVVEKAP KSAVVAGGGF IGLEVAENLC EMGVEVTIVQ
     RPKQVLAPLD ADMACQLHAL LRSHGIGLKL GSSVAGFEER DGKVSTLLEG EEPLVSDMVV
     LAIGVTPDTA IAQAAGLEMG PKGSIVVNDR METSVPDIYA VGDAVQVVDA VTGLDALVPL
     AGPANKQGRI AADNICGGYS YYRGSQRSSV IKLFNMTAAT TGINEKLAQA AGIDYEKVVL
     SPANHAGYYP GGKVMTCKIL YERGSLRLLG AQIVGYEGVD KRIDVLATAI FAGLNAVDLK
     DLDLAYAPPY SSAKDPVNMA GFMIENIEEG RVKQFHWHDV ADLPRDGSVT LLDARTPAEY
     ARGCAEGFVN IPLDELRGRL DEIPLDKPLY VMCQSGLRSY LACCILAQNG YDCYNFSGGY
     RFYNMVTSDL LAADQAHPCG ADK
//
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