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
//