Searching for up to 100 curated homologs for WP_013450727.1 NCBI__GCF_000183405.1:WP_013450727.1 (559 a.a.)
Found high-coverage hits (≥70%) to 55 curated proteins.
You can add additional sequences or change the %identity threshold for inclusion. Once you have selected sequences, you can build an alignment and a tree.
8a56B / Q82ZQ9 Coenzyme a-persulfide reductase (coapr) from enterococcus faecalis (see paper)
41% identity, 97% coverage of query (389 bits)
3ictA / A0A6L7H7X4 Crystal structure of reduced bacillus anthracis coadr-rhd (see paper)
40% identity, 93% coverage of query (384 bits)
3icsB Crystal structure of partially reduced bacillus anthracis coadr-rhd
40% identity, 93% coverage of query (384 bits)
ORFY / CBY83974.1 putative NADH oxidase from Serratia sp. ATCC 39006 (see paper)
40% identity, 93% coverage of query (383 bits)
3nt6A / A3QAV3 Structure of the shewanella loihica pv-4 nadh-dependent persulfide reductase c43s/c531s double mutant (see paper)
39% identity, 97% coverage of query (362 bits)
6pfzA / O29847 Structure of a NAD-dependent persulfide reductase from a. Fulgidus (see paper)
37% identity, 96% coverage of query (326 bits)
3cgbA / A0A6L7HMK7 Pyridine nucleotide complexes with bacillus anthracis coenzyme a- disulfide reductase: a structural analysis of dual NAD(p)h specificity (see paper)
32% identity, 78% coverage of query (270 bits)
3cgeA Pyridine nucleotide complexes with bacillus anthracis coenzyme a- disulfide reductase: a structural analysis of dual NAD(p)h specificity
32% identity, 78% coverage of query (270 bits)
3cgdA Pyridine nucleotide complexes with bacillus anthracis coenzyme a- disulfide reductase: a structural analysis of dual NAD(p)h specificity
32% identity, 78% coverage of query (270 bits)
NSR_THEKO / Q5JGP4 NAD(P)H sulfur oxidoreductase (CoA-dependent); NSR; NAD(P)H oxidase (H2O-forming); NOX; EC 1.8.1.18; EC 1.6.3.2 from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) (see 2 papers)
Q5JGP4 NAD(P)H oxidase (H2O2-forming) (EC 1.6.3.1); NAD(P)H oxidase (H2O-forming) (EC 1.6.3.2); NAD(P)H sulfur oxidoreductase (CoA-dependent) (EC 1.8.1.18) from Thermococcus kodakarensis (see 2 papers)
34% identity, 78% coverage of query (253 bits)
GB|AAB98641.1 NADH oxidase; EC 1.-.-.- from Methanocaldococcus jannaschii DSM 2661 (see paper)
35% identity, 78% coverage of query (250 bits)
Q58065 NADH oxidase (H2O2-forming) (EC 1.6.3.3) from Methanocaldococcus jannaschii (see paper)
35% identity, 78% coverage of query (250 bits)
PF1186 / Q8U1M0 NAD(P)H sulfur oxidoreductase (CoA-dependent) (EC 1.8.1.18) from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 2 papers)
NSR_PYRFU / Q8U1M0 NAD(P)H sulfur oxidoreductase (CoA-dependent); NSR; Coenzyme A disulfide reductase; CoA-disulfide reductase; CoADR; NAD(P)H oxidase; NOX; EC 1.8.1.18; EC 1.8.1.14; EC 1.6.3.- from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 4 papers)
Q8U1M0 NAD(P)H sulfur oxidoreductase (CoA-dependent) (EC 1.8.1.18) from Pyrococcus furiosus (see 3 papers)
34% identity, 78% coverage of query (240 bits)
B2G3S1 NAD(P)H oxidase (H2O-forming) (EC 1.6.3.2) from Thermococcus profundus (see 2 papers)
33% identity, 78% coverage of query (236 bits)
Q72HK3 NADH:ubiquinone reductase (H+-translocating) (EC 7.1.1.2) from Thermus thermophilus (see paper)
6ruzA / Q72HK3 Nadh-dependent coenzyme a disulfide reductase (see paper)
32% identity, 79% coverage of query (233 bits)
6rvhA Nadh-dependent coenzyme a disulfide reductase soaked with menadione
32% identity, 79% coverage of query (233 bits)
6rvbA Nadh-dependent coenzyme a disulfide reductase soaked with nadh
32% identity, 79% coverage of query (233 bits)
O29852 NADH oxidase (H2O2-forming) (EC 1.6.3.3) from Archaeoglobus fulgidus (see paper)
33% identity, 79% coverage of query (229 bits)
NCPPR_PYRHO / O58308 NAD(P)H coenzyme A polysulfide/persulfide reductase; Coenzyme A disulfide reductase; CoA-disulfide reductase; CoADR; Polysulfide reductase; EC 1.8.1.-; EC 1.8.1.14 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see 3 papers)
O58308 CoA-disulfide reductase (EC 1.8.1.14) from Pyrococcus horikoshii (see paper)
33% identity, 78% coverage of query (224 bits)
4fx9B / O58308 Structure of the pyrococcus horikoshii coa persulfide/polysulfide reductase (see paper)
33% identity, 78% coverage of query (223 bits)
O29985 NADH oxidase (H2O2-forming) (EC 1.6.3.3) from Archaeoglobus fulgidus (see paper)
32% identity, 74% coverage of query (218 bits)
Q5JFZ8 NAD(P)H oxidase (H2O2-forming) (EC 1.6.3.1) from Thermococcus kodakarensis (see 2 papers)
31% identity, 79% coverage of query (217 bits)
Q2FIA5 CoA-disulfide reductase (EC 1.8.1.14) from Staphylococcus aureus (see paper)
31% identity, 77% coverage of query (196 bits)
4em3A / Q2FIA5 Crystal structure of staphylococcus aureus bound with the covalent inhibitor mevs-coa (see paper)
31% identity, 77% coverage of query (196 bits)
CDR_STAA8 / O52582 Coenzyme A disulfide reductase; CoA-disulfide reductase; CoADR; EC 1.8.1.14 from Staphylococcus aureus (strain NCTC 8325 / PS 47) (see 2 papers)
31% identity, 77% coverage of query (196 bits)
4emwA Crystal structure of staphylococcus aureus bound with the covalent inhibitor etvc-coa
31% identity, 77% coverage of query (196 bits)
4em4A Crystal structure of staphylococcus aureus bound with the covalent inhibitor pethyl-vs-coa
31% identity, 77% coverage of query (196 bits)
1yqzA Structure of coenzyme a-disulfide reductase from staphylococcus aureus refined at 1.54 angstrom resolution
31% identity, 77% coverage of query (196 bits)
Build an alignment for WP_013450727.1 and 28 homologs with ≥ 30% identity
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F6IXY6 NADH oxidase (H2O-forming) (EC 1.6.3.4) from Lactiplantibacillus pentosus (see paper)
29% identity, 79% coverage of query (177 bits)
Q8KRG4 NADH oxidase (H2O-forming) (EC 1.6.3.4) from Levilactobacillus brevis (see paper)
28% identity, 78% coverage of query (165 bits)
5er0A / Q03Q85 Water-forming nadh oxidase from lactobacillus brevis (lbnox) (see paper)
27% identity, 78% coverage of query (163 bits)
5vn0A Water-forming nadh oxidase from lactobacillus brevis (lbnox) bound to nadh.
27% identity, 78% coverage of query (163 bits)
Q2WFW5 NADH oxidase (H2O-forming) (EC 1.6.3.4) from Anaerocolumna aminovalerica (see 2 papers)
30% identity, 79% coverage of query (159 bits)
Q5JJB9 NAD(P)H oxidase (H2O2-forming) (EC 1.6.3.1) from Thermococcus kodakarensis (see paper)
29% identity, 76% coverage of query (157 bits)
2bc0A / Q5XC60 Structural analysis of streptococcus pyogenes nadh oxidase: wild-type nox (see paper)
29% identity, 80% coverage of query (156 bits)
Q54453 NADH oxidase (H2O-forming) (EC 1.6.3.4) from Streptococcus mutans (see 2 papers)
29% identity, 77% coverage of query (156 bits)
Q8E5N5 NADH oxidase (H2O-forming) (EC 1.6.3.4) from Streptococcus agalactiae (see paper)
31% identity, 79% coverage of query (155 bits)
NAPE_ENTFA / P37062 NADH peroxidase; NPXase; Npx; EC 1.11.1.1 from Enterococcus faecalis (strain ATCC 700802 / V583) (see 2 papers)
27% identity, 79% coverage of query (155 bits)
1f8wA / P37062 Crystal structure of nadh peroxidase mutant: r303m (see paper)
27% identity, 79% coverage of query (154 bits)
2npxA Nadh binding site and catalysis of nadh peroxidase
27% identity, 79% coverage of query (154 bits)
NAOX_STRP6 / Q5XC60 NADH oxidase; NOXase; EC 1.6.3.4 from Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394) (see paper)
29% identity, 79% coverage of query (153 bits)
2bcpA Structural analysis of streptococcus pyogenes nadh oxidase: c44s nox with azide
29% identity, 80% coverage of query (152 bits)
5vohA Crystal structure of engineered water-forming NADPH oxidase (tpnox) bound to NADPH. The g159a, d177a, a178r, m179s, p184r mutant of lbnox.
27% identity, 78% coverage of query (152 bits)
NAOX_STRPN / A0A0H2UQZ4 NADH oxidase; NOXase; EC 1.6.3.4 from Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) (see paper)
28% identity, 79% coverage of query (146 bits)
NAOX_LACLM / A2RIB7 NADH oxidase; NOXase; EC 1.6.3.4 from Lactococcus lactis subsp. cremoris (strain MG1363)
A2RIB7 NADH oxidase (H2O-forming) (EC 1.6.3.4) from Lactococcus cremoris (see 4 papers)
27% identity, 79% coverage of query (145 bits)
NAOX_STREE / O84925 NADH oxidase; NOXase; EC 1.6.3.4 from Streptococcus pneumoniae (see 2 papers)
27% identity, 79% coverage of query (144 bits)
2cduA / Q9F1X5 The crystal structure of water-forming NAD(p)h oxidase from lactobacillus sanfranciscensis (see paper)
26% identity, 79% coverage of query (144 bits)
NAOX_STRR6 / Q8DP70 NADH oxidase; NOXase; EC 1.6.3.4 from Streptococcus pneumoniae (strain ATCC BAA-255 / R6) (see paper)
27% identity, 79% coverage of query (144 bits)
P37061 NADH oxidase; NOXase; EC 1.6.3.4 from Enterococcus faecalis (strain ATCC 700802 / V583)
30% identity, 78% coverage of query (142 bits)
NAOX_MYCGE / Q49408 NADH oxidase; NOXase; EC 1.6.3.4 from Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) (Mycoplasmoides genitalium) (see paper)
25% identity, 80% coverage of query (118 bits)
3oc4A / Q833L5 Crystal structure of a pyridine nucleotide-disulfide family oxidoreductase from the enterococcus faecalis v583
25% identity, 79% coverage of query (114 bits)
5x1yB / D9J041 Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
27% identity, 71% coverage of query (100 bits)
MERA_LYSSH / D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
D9J041 mercury(II) reductase (EC 1.16.1.1) from Lysinibacillus sphaericus (see 2 papers)
27% identity, 70% coverage of query (100 bits)
DLDH1_GEOSE / P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
P11959 dihydrolipoyl dehydrogenase (EC 1.8.1.4) from Geobacillus stearothermophilus (see 2 papers)
pdhD / GB|CAA37631.1 dihydrolipoyl dehydrogenase; EC 1.8.1.4 from Geobacillus stearothermophilus (see 4 papers)
25% identity, 75% coverage of query (79.0 bits)
1ebdA / P11959 Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
25% identity, 72% coverage of query (79.0 bits)
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Lawrence Berkeley National Laboratory