ID D2QY80_PIRSD Unreviewed; 556 AA.
AC D2QY80;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ADB16294.1};
DE Flags: Precursor;
GN OrderedLocusNames=Psta_1619 {ECO:0000313|EMBL:ADB16294.1};
OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS staleyi).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Pirellula.
OX NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB16294.1, ECO:0000313|Proteomes:UP000001887};
RN [1] {ECO:0000313|EMBL:ADB16294.1, ECO:0000313|Proteomes:UP000001887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC {ECO:0000313|Proteomes:UP000001887};
RX PubMed=21304671; DOI=10.4056/sigs.51657;
RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL Stand. Genomic Sci. 1:308-316(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP001848; ADB16294.1; -; Genomic_DNA.
DR RefSeq; WP_012910557.1; NC_013720.1.
DR AlphaFoldDB; D2QY80; -.
DR STRING; 530564.Psta_1619; -.
DR KEGG; psl:Psta_1619; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_0; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000001887; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase 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 InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF7; NITRIC OXIDE REDUCTASE FLRD-NAD(+) REDUCTASE; 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; PS00380; RHODANESE_1; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT DOMAIN 465..552
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 556 AA; 59899 MW; 70D961AEEDF29BEB CRC64;
MKLVIVGGVA GGASAAARAR RLDESAEIIL LERGPDVSFA NCGMPYYIGQ QIVDRKRLLV
VTPERLRERL NLDVRPQTEA IAIDRAKKQL RVRNLANDEE YDLTYDKLIL APGASPFRPA
VPGFDLLRVM TLRNLSDMDR IAAASSAAKH VVVMGAGFIG LEMIENLVHR GISCTLVQNQ
SQVLSPLDAE MTTPLAEELV KRGVDLALSD SATSIETVES TGRMRVQLQS GREVETDLVV
VGIGVRPENQ LAIAAGLALG DRGGIAVNEA MQTSDPDIYA VGDVVETRDV VSGVKQLMPL
AGPANRQGRI AADHLFGRPA KFRGTQATAI VGLWKLTAAM TGLSEKVCRL RNIPFCAVYI
HPAHHATYYP GAEPMSLKVL FDPTSGRILG AQGVGGAGVD KRIDILSIAI QSKMTVFDLE
EAELCYAPQF GSAKDPINMV GFVAAGMLRG DHPQIDVREL LAMDPSVRPL VLDVRTSEEF
AAGHLPGAIS ISVDQLRGRL SELDPTRKIA AYCQVGQRGY FATRILLQHG FDVVNVSGGY
KTYLLHFPAG YSANAS
//
