Curated BLAST

Curated BLAST for Genomes

Curated BLAST

Searching in Methylosarcina fibrata AML-C10 (GCF_000372865.1)

Found 62 curated entries in PaperBLAST's database that match '4.2.1.17' as complete word(s).

These curated entries have 44 distinct sequences.

Running ublast with E ≤ 0.01

Found 2 relevant proteins in Methylosarcina fibrata AML-C10, or try another query

A3OW_RS0123285 WP_020565869.1: 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase family protein is similar to:	PaperBLAST
Q0KEG0: 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35); enoyl-CoA hydratase (EC 4.2.1.17) from Cupriavidus necator	34% id, 99% cov
BPHYT_RS17335: 2,3-dehydroadipyl-CoA hydratase / enoyl-CoA hydratase (EC 4.2.1.17) from Burkholderia phytofirmans	25% id, 84% cov
FADB_BACSU / P94549: Probable enoyl-CoA hydratase; EC 4.2.1.17 from Bacillus subtilis	27% id, 68% cov
H281DRAFT_05725: 2,3-dehydroadipyl-CoA hydratase / enoyl-CoA hydratase (EC 4.2.1.17) from Paraburkholderia bryophila	25% id, 74% cov
Psest_2437: Enoyl-CoA hydratase [valine degradation] (EC 4.2.1.17) from Pseudomonas stutzeri	30% id, 55% cov
Sama_0032: Enoyl-CoA hydratase (EC 4.2.1.17); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) from Shewanella amazonensis	30% id, 52% cov
HP15_1512: Enoyl-CoA hydratase (EC 4.2.1.17) from Marinobacter adhaerens	27% id, 56% cov
MFPA_CUCSA / Q39659: Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Cucumis sativus	29% id, 52% cov
PAAF_ECOLI / P76082: 2,3-dehydroadipyl-CoA hydratase; Enoyl-CoA hydratase; EC 4.2.1.17 from Escherichia coli YdbR / b1393: putative 2,3-dehydroadipyl-CoA hydratase (EC 4.2.1.17) from Escherichia coli P76082: enoyl-CoA hydratase (EC 4.2.1.17) from Escherichia coli	33% id, 45% cov
Q0KEG0: 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35); enoyl-CoA hydratase (EC 4.2.1.17) from Cupriavidus necator	33% id, 44% cov
FADJ_ECOLI / P77399: Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 1.1.1.35 from Escherichia coli FadJ / b2341: 3-hydroxyacyl-CoA dehydrogenase FadJ (EC 1.1.1.35; EC 1.1.1.211; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8) from Escherichia coli fadJ / RF\|NP_416843: fatty acid oxidation complex subunit alpha; EC 1.1.1.35; EC 4.2.1.17; EC 5.1.2.3 from Escherichia coli fadJ / P77399: multifunctional 3-hydroxyacyl-CoA dehydrogenase/3-hydroxyacyl-CoA epimerase/enoyl-CoA hydratase FadJ (EC 1.1.1.35; EC 4.2.1.17; EC 4.2.1.74; EC 5.1.2.3; EC 5.3.3.8) from Escherichia coli	29% id, 51% cov
ECH17_MYCBO / Q7TXE1: Probable enoyl-CoA hydratase EchA17; EC 4.2.1.17 from Mycobacterium bovis ECH17_MYCTU / P9WNN3: Probable enoyl-CoA hydratase EchA17; EC 4.2.1.17 from Mycobacterium tuberculosis	26% id, 56% cov
Shewana3_0024: Enoyl-CoA hydratase (EC 4.2.1.17); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) from Shewanella sp.	28% id, 52% cov
FADB_ECOLI / P21177: Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Escherichia coli OldB / b3846: multifunctional enoyl-CoA hydratase, 3-hydroxyacyl-CoA epimerase, Δ³-cis- Δ²-trans-enoyl-CoA isomerase, L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35; EC 1.1.1.211; EC 4.2.1.17; EC 5.3.3.8; EC 5.1.2.3) from Escherichia coli fadB / P21177: multifunctional enoyl-CoA hydratase, 3-hydroxyacyl-CoA epimerase, Δ³-cis- Δ²-trans-enoyl-CoA isomerase, L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35; EC 4.2.1.17; EC 4.2.1.74; EC 5.3.3.8; EC 5.1.2.3) from Escherichia coli	29% id, 48% cov
paaF / Q845K2: 2,3-dehydroadipyl-CoA hydratase (EC 4.2.1.17) from Pseudomonas sp.	28% id, 49% cov
MFP2_ARATH / Q9ZPI5: Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2; AtMPF2; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Arabidopsis thaliana MFP2 / Q9ZPI5: peroxisomal fatty acid β-oxidation multifunctional protein MFP2 (EC 1.1.1.35; EC 4.2.1.17) from Arabidopsis thaliana Q9ZPI5: enoyl-CoA hydratase (EC 4.2.1.17) from Arabidopsis thaliana	26% id, 52% cov
AIM1_ARATH / Q9ZPI6: Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1; Protein ABNORMAL INFLORESCENCE MERISTEM 1; AtAIM1; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Arabidopsis thaliana AIM1 / Q9ZPI6: peroxisomal fatty acid β-oxidation multifunctional protein AIM1 (EC 1.1.1.35; EC 4.2.1.17) from Arabidopsis thaliana	28% id, 48% cov
ECHM_RAT / P14604: Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus P14604: enoyl-CoA hydratase (EC 4.2.1.17); DELTA3,5-DELTA2,4-dienoyl-CoA isomerase (EC 5.3.3.21) from Rattus norvegicus	28% id, 46% cov
FADB_PSEFR / P28793: Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Pseudomonas fragi	31% id, 41% cov
ECHM_MOUSE / Q8BH95: Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Mus musculus	27% id, 46% cov
MFP_ORYSJ / Q8W1L6: Peroxisomal fatty acid beta-oxidation multifunctional protein; MFP; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Oryza sativa	30% id, 42% cov
fadB / Q88L02: FadB (EC 5.3.3.8; EC 1.1.1.35; EC 5.1.2.3; EC 4.2.1.17; EC 1.1.1.36) from Pseudomonas putida	31% id, 39% cov
ECHM_HUMAN / P30084: Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Homo sapiens ECHS1 / P30084: short-chain enoyl-CoA hydratase monomer (EC 4.2.1.17) from Homo sapiens P30084: enoyl-CoA hydratase (EC 4.2.1.17) from Homo sapiens	29% id, 40% cov
ECHP_MOUSE / Q9DBM2: Peroxisomal bifunctional enzyme; PBE; PBFE; L-peroxisomal bifunctional enzyme; L-PBE; Multifunctional enzyme 1; MFE1; Multifunctional protein 1; MFP-1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Mus musculus	28% id, 40% cov
DPGD_AMYOR / G4V4T7: Enoyl-CoA-hydratase; EC 4.2.1.17 from Amycolatopsis orientalis	51% id, 18% cov
FADB_PSEFR / P28793: Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Pseudomonas fragi	23% id, 39% cov
Shewana3_0024: Enoyl-CoA hydratase (EC 4.2.1.17); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) from Shewanella sp.	23% id, 39% cov
MFP_ORYSJ / Q8W1L6: Peroxisomal fatty acid beta-oxidation multifunctional protein; MFP; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Oryza sativa	27% id, 27% cov
MFPA_CUCSA / Q39659: Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Cucumis sativus	26% id, 28% cov
AIM1_ARATH / Q9ZPI6: Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1; Protein ABNORMAL INFLORESCENCE MERISTEM 1; AtAIM1; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Arabidopsis thaliana AIM1 / Q9ZPI6: peroxisomal fatty acid β-oxidation multifunctional protein AIM1 (EC 1.1.1.35; EC 4.2.1.17) from Arabidopsis thaliana	25% id, 27% cov
FADB_ECOLI / P21177: Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Escherichia coli OldB / b3846: multifunctional enoyl-CoA hydratase, 3-hydroxyacyl-CoA epimerase, Δ³-cis- Δ²-trans-enoyl-CoA isomerase, L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35; EC 1.1.1.211; EC 4.2.1.17; EC 5.3.3.8; EC 5.1.2.3) from Escherichia coli fadB / P21177: multifunctional enoyl-CoA hydratase, 3-hydroxyacyl-CoA epimerase, Δ³-cis- Δ²-trans-enoyl-CoA isomerase, L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35; EC 4.2.1.17; EC 4.2.1.74; EC 5.3.3.8; EC 5.1.2.3) from Escherichia coli	24% id, 26% cov
ECHA_RAT / Q64428: Trifunctional enzyme subunit alpha, mitochondrial; Monolysocardiolipin acyltransferase; TP-alpha; EC 2.3.1.-; EC 4.2.1.17; EC 1.1.1.211 from Rattus norvegicus	29% id, 21% cov
ECHA_MOUSE / Q8BMS1: Trifunctional enzyme subunit alpha, mitochondrial; Monolysocardiolipin acyltransferase; TP-alpha; EC 2.3.1.-; EC 4.2.1.17; EC 1.1.1.211 from Mus musculus	29% id, 21% cov
Sama_0032: Enoyl-CoA hydratase (EC 4.2.1.17); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) from Shewanella amazonensis	32% id, 19% cov
HP15_1512: Enoyl-CoA hydratase (EC 4.2.1.17) from Marinobacter adhaerens	28% id, 21% cov
ECHP_HUMAN / Q08426: Peroxisomal bifunctional enzyme; PBE; PBFE; L-bifunctional protein; LBP; Multifunctional enzyme 1; MFE1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Homo sapiens EHHADH / Q08426: peroxisomal bifunctional enzyme (EC 4.2.1.17; EC 1.1.1.35) from Homo sapiens	34% id, 17% cov
MFP2_ARATH / Q9ZPI5: Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2; AtMPF2; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Arabidopsis thaliana MFP2 / Q9ZPI5: peroxisomal fatty acid β-oxidation multifunctional protein MFP2 (EC 1.1.1.35; EC 4.2.1.17) from Arabidopsis thaliana Q9ZPI5: enoyl-CoA hydratase (EC 4.2.1.17) from Arabidopsis thaliana	29% id, 20% cov
fadB / Q88L02: FadB (EC 5.3.3.8; EC 1.1.1.35; EC 5.1.2.3; EC 4.2.1.17; EC 1.1.1.36) from Pseudomonas putida	27% id, 21% cov
ECHP_RAT / P07896: Peroxisomal bifunctional enzyme; PBE; PBFE; Multifunctional enzyme 1; MFE1; Multifunctional protein 1; MFP1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Rattus norvegicus Ehhadh / RF\|NP_598290.1: noyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase/3-hydroxyacyl-CoA dehydrogenase; EC 1.1.1.35; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus P07896: enoyl-CoA hydratase (EC 4.2.1.17) from Rattus norvegicus	31% id, 17% cov
ECHP_MOUSE / Q9DBM2: Peroxisomal bifunctional enzyme; PBE; PBFE; L-peroxisomal bifunctional enzyme; L-PBE; Multifunctional enzyme 1; MFE1; Multifunctional protein 1; MFP-1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Mus musculus	30% id, 17% cov
More...

A3OW_RS0118385 WP_020564926.1: hydrogenase maturation protein is similar to:	PaperBLAST
ECH17_MYCBO / Q7TXE1: Probable enoyl-CoA hydratase EchA17; EC 4.2.1.17 from Mycobacterium bovis ECH17_MYCTU / P9WNN3: Probable enoyl-CoA hydratase EchA17; EC 4.2.1.17 from Mycobacterium tuberculosis	28% id, 69% 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 2 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory