ID Q1Q0R7_KUEST Unreviewed; 555 AA.
AC Q1Q0R7;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Putative pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:QII12173.1};
DE EC=1.6.99.3 {ECO:0000313|EMBL:CAJ73591.1, ECO:0000313|EMBL:QII12173.1};
DE SubName: Full=Similar to pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:CAJ73591.1};
GN Name=nox {ECO:0000313|EMBL:CAJ73591.1};
GN ORFNames=KsCSTR_27940 {ECO:0000313|EMBL:QII12173.1}, KSMBR1_0011
GN {ECO:0000313|EMBL:SOH02533.1}, kuste2839
GN {ECO:0000313|EMBL:CAJ73591.1};
OS Kuenenia stuttgartiensis.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Kuenenia.
OX NCBI_TaxID=174633 {ECO:0000313|EMBL:CAJ73591.1};
RN [1] {ECO:0000313|EMBL:CAJ73591.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16598256; DOI=10.1038/nature04647;
RA Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., Taylor M.W.,
RA Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., Fonknechten N.,
RA Vallenet D., Segurens B., Schenowitz-Truong C., Medigue C., Collingro A.,
RA Snel B., Dutilh B.E., OpDenCamp H.J.M., vanDerDrift C., Cirpus I.,
RA vanDePas-Schoonen K.T., Harhangi H.R., vanNiftrik L., Schmid M.,
RA Keltjens J., vanDeVossenberg J., Kartal B., Meier H., Frishman D.,
RA Huynen M.A., Mewes H., Weissenbach J., Jetten M.S.M., Wagner M.,
RA LePaslier D.;
RT "Deciphering the evolution and metabolism of an anammox bacterium from a
RT community genome.";
RL Nature 440:790-794(2006).
RN [2] {ECO:0000313|EMBL:CAJ73591.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SOH02533.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kuenenia_mbr1_ru-nijmegen {ECO:0000313|EMBL:SOH02533.1};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000221734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Frank J.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QII12173.1, ECO:0000313|Proteomes:UP000501926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSTR1 {ECO:0000313|EMBL:QII12173.1,
RC ECO:0000313|Proteomes:UP000501926};
RA Ding C., Adrian L.;
RT "Newly sequenced genome of strain CSTR1 showed variability in Candidatus
RT Kuenenia stuttgartiensis genomes.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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; CT573071; CAJ73591.1; -; Genomic_DNA.
DR EMBL; CP049055; QII12173.1; -; Genomic_DNA.
DR EMBL; LT934425; SOH02533.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1Q0R7; -.
DR KEGG; kst:KSMBR1_0011; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000221734; Chromosome Kuenenia_stuttgartiensis_MBR1.
DR Proteomes; UP000501926; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Oxidoreductase {ECO:0000313|EMBL:CAJ73591.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000221734}.
FT DOMAIN 470..555
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 555 AA; 60310 MW; 0136A96002E81B10 CRC64;
MGPKRMVIIG AVASGTKTAA KARREDPDAE ITLITEEADI SYAACGTPYF ISDIIKDSSS
LIIRTPDYFL KMLNINVLTE HRVEAINPGG KDIAVRNLKT NSSAFLPYDF LVLATGAKPY
VPECEGVESG NIFTLHNIKS AMRIKSVLQQ KKIGHAIIVG GGFIALEIAE SLMEYGIKAH
IIIRREHILS HIDKNIALLV QNHVRAKGVH IHEDDEVIKY EADSEGNVSK VITKKQTLPA
EIVVLATGIK PNVSLAKNAG IAIGQTGAIQ VNERLETNIP DIYAVGDCVE TTHMVTGKPV
WIPLATTANK QGRIGGINIC GGNDTFPGVM GTFIVKVFDW TVAKTGLSEK EAIRNGFDVV
SVIVPSHDKP HYYPGSKLII VKLIAEKGSG ILLGAEIAGE GVVDKRIDVV SAALMGRVTA
GQLSKYDLSY APPYSSPMDP LITAANVLRN KLEGKIQSIS PLITKQKLER KDDFVLLDVR
TKHEHDKGHI EGSLHIPLNE LKSRSGALDK TREIITYCGV GLRASQAHLL LKTEGFENVK
FMEGSLLAWP YAIEK
//
