Searching in Shewanella loihica PV-4 (PV4)
Found 65 curated entries in PaperBLAST's database that match '3.7.1.2'.
These curated entries have 46 distinct sequences.
Running ublast with E ≤ 0.01
Found 10 relevant proteins in Shewanella loihica PV-4, or try another query
| Shew_1438: fumarylacetoacetate (FAA) hydrolase (RefSeq) is similar to: | PaperBLAST |
SO1670: fumarylacetoacetate hydrolase (EC 3.7.1.2) from Shewanella oneidensis | 86% id, 100% cov |
Psest_3512: fumarylacetoacetate (FAA) hydrolase (EC 3.7.1.2) from Pseudomonas stutzeri | 68% id, 99% cov |
| Shew_1535: fumarylacetoacetate (FAA) hydrolase (RefSeq) is similar to: | PaperBLAST |
A0A0D5YDA5: fumarylacetoacetase (EC 3.7.1.2) from Acinetobacter baumannii | 39% id, 99% cov |
A0A080VH08: 3-fumarylpyruvate hydrolase (EC 3.7.1.20) from Pseudomonas aeruginosa | 31% id, 86% cov |
A0A1B0ZSC0: fumarylacetoacetase (EC 3.7.1.2) from Phaeobacter gallaeciensis | 31% id, 85% cov |
| Shew_0289: acetolactate synthase 2 catalytic subunit (RefSeq) is similar to: | PaperBLAST |
HSERO_RS12130: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) from Herbaspirillum seropedicae | 28% id, 92% cov |
Q9L3I0: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (ring-opening) (EC 3.7.1.22) from Rhizobium leguminosarum | 27% id, 91% cov |
SMc01166: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) from Sinorhizobium meliloti | 27% id, 92% cov |
| Shew_1860: alpha/beta hydrolase fold (RefSeq) is similar to: | PaperBLAST |
TODF_PSEP1 / P23133: 2-hydroxy-6-oxo-2,4-heptadienoate hydrolase; HOHH; EC 3.7.1.25 from Pseudomonas putida | 27% id, 94% cov |
| Shew_1776: acetolactate synthase 3 catalytic subunit (RefSeq) is similar to: | PaperBLAST |
PS417_11870: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) from Pseudomonas simiae | 28% id, 89% cov |
Pf1N1B4_4279: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) from Pseudomonas fluorescens | 27% id, 89% cov |
BWI76_RS03090: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) from Klebsiella michiganensis | 26% id, 89% cov |
| Shew_1670: enoyl-CoA hydratase (RefSeq) is similar to: | PaperBLAST |
BAMA_GEOMG / Q39TV7: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-OCH-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; EC 3.7.1.21 from Geobacter metallireducens | 28% id, 63% cov |
| Shew_2864: 3-hydroxyacyl-CoA dehydrogenase, NAD-binding (RefSeq) is similar to: | PaperBLAST |
BAMA_GEOMG / Q39TV7: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-OCH-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; EC 3.7.1.21 from Geobacter metallireducens | 30% id, 48% cov |
| Shew_0019: multifunctional fatty acid oxidation complex subunit alpha (RefSeq) is similar to: | PaperBLAST |
BAMA_GEOMG / Q39TV7: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-OCH-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; EC 3.7.1.21 from Geobacter metallireducens | 24% id, 43% cov |
BAMA_THAAR / O87872: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; Beta-oxoacyl-CoA hydrolase; Oah; EC 3.7.1.21 from Thauera aromatica | 25% id, 36% cov |
| Shew_1671: enoyl-CoA hydratase/isomerase (RefSeq) is similar to: | PaperBLAST |
BAMA_THAAR / O87872: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; Beta-oxoacyl-CoA hydrolase; Oah; EC 3.7.1.21 from Thauera aromatica | 26% id, 37% cov |
BAMA_GEOMG / Q39TV7: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-OCH-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; EC 3.7.1.21 from Geobacter metallireducens | 25% id, 36% cov |
| Shew_3018: alpha/beta hydrolase fold (RefSeq) is similar to: | PaperBLAST |
TODF_PSEP1 / P23133: 2-hydroxy-6-oxo-2,4-heptadienoate hydrolase; HOHH; EC 3.7.1.25 from Pseudomonas putida | 29% id, 33% cov |
The hits are sorted by %identity * %coverage (highest first)
Running ublast against the 6-frame translation. All reading frames of at least 30 codons are included.
Found hits to 8 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory