ID Q7UMA9_RHOBA Unreviewed; 560 AA.
AC Q7UMA9;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Probable NADH oxidase {ECO:0000313|EMBL:CAD76008.1};
DE EC=1.6.99.3 {ECO:0000313|EMBL:CAD76008.1};
GN Name=noxA {ECO:0000313|EMBL:CAD76008.1};
GN OrderedLocusNames=RB8937 {ECO:0000313|EMBL:CAD76008.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD76008.1, ECO:0000313|Proteomes:UP000001025};
RN [1] {ECO:0000313|EMBL:CAD76008.1, ECO:0000313|Proteomes:UP000001025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC {ECO:0000313|Proteomes:UP000001025};
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; BX294148; CAD76008.1; -; Genomic_DNA.
DR RefSeq; NP_868631.1; NC_005027.1.
DR RefSeq; WP_011122081.1; NC_005027.1.
DR AlphaFoldDB; Q7UMA9; -.
DR SMR; Q7UMA9; -.
DR STRING; 243090.RB8937; -.
DR EnsemblBacteria; CAD76008; CAD76008; RB8937.
DR KEGG; rba:RB8937; -.
DR PATRIC; fig|243090.15.peg.4290; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_0; -.
DR InParanoid; Q7UMA9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd01524; RHOD_Pyr_redox; 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; 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 Oxidoreductase {ECO:0000313|EMBL:CAD76008.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001025}.
FT DOMAIN 474..551
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 560 AA; 59978 MW; 0562B0FB1C14CCC8 CRC64;
MSVEHNAPVR LVIVGGVAGG ASAATRARRM NEQAEIILFE KDEDVSFANC GLPYHIGEEI
KNRDALVVAS ADFLRRRFQL DVRTREEVVS INREKRCVTV VRHGATSEKD KTYEQPYDKL
ILAPGASPIV PALPGVDASN VLTLRNLVDM DRIKARVDSG SVRRAVVVGA GYIGLEMVEQ
LRRREMDVDL IELREQVLPL LDHEMARPIE DALRRNNVGI HLGVGLESIQ LDGDRATSVR
LSDGTELSTD LVILGIGVRP NSELAKEAGL EIGSTGGITI DEFSRTSDSD IYAVGDASEP
VYGPTGTPMR VPLAGPANRS GRLAGEHAVT GQSAAATPVW GTSVVRVFDV SVGMTGLTRA
SAKRFGKDAT SVTIVAKHHA GYFPGAEVMT LKLAFEPATG KVLGAQCVGG EGIDKRIDVI
ATAMHFGGTV RDLAGLDLAY APPFGSAKDP VHMAAFAACN ALDEIESFRD SDDSLDEVQV
VDVRGAGEIE KTPLREASGA IHIPVDELRE RLSELDRSKP TVVSCAVGVR GHIAARILRQ
NGFDVQNLSG GATVRNRCFE
//
