Searching in Pseudovibrio axinellae Ad2 (GCF_001623255.1)
Found 11 curated entries in PaperBLAST's database that match '6.2.1.16' as complete word(s).
These curated entries have 7 distinct sequences.
Running ublast with E ≤ 0.01
Found 15 relevant proteins in Pseudovibrio axinellae Ad2, or try another query
PsAD2_RS03405 PsAD2_00694 WP_068002231.1: long-chain fatty acid--CoA ligase is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 31% id, 95% cov |
AACS_MOUSE / Q9D2R0: Acetoacetyl-CoA synthetase; EC 6.2.1.16 from Mus musculus | 22% id, 83% cov |
AACS_RAT / Q9JMI1: Acetoacetyl-CoA synthetase; EC 6.2.1.16 from Rattus norvegicus | 21% id, 83% cov |
PsAD2_RS06330 PsAD2_01288 WP_068003987.1: acyl-CoA synthetase is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 29% id, 96% cov |
PsAD2_RS15660 PsAD2_03172 WP_068007866.1: AMP-binding protein is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 30% id, 92% cov |
PsAD2_RS22240 PsAD2_04454 WP_068010795.1: acyl-CoA synthetase is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 27% id, 96% cov |
PsAD2_RS06350 PsAD2_01292 WP_068003990.1: propionyl-CoA synthetase is similar to: | PaperBLAST |
aacS / D6EQU8: acetoacetate-CoA ligase (EC 6.2.1.16) from Streptomyces lividans | 27% id, 93% cov |
AACS_RAT / Q9JMI1: Acetoacetyl-CoA synthetase; EC 6.2.1.16 from Rattus norvegicus | 25% id, 92% cov |
AACS_HUMAN / Q86V21: Acetoacetyl-CoA synthetase; Acyl-CoA synthetase family member 1; Protein sur-5 homolog; EC 6.2.1.16 from Homo sapiens | 25% id, 93% cov |
PsAD2_RS20115 PsAD2_04039 WP_068010027.1: AMP-binding protein is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 28% id, 88% cov |
acs PsAD2_RS07830 PsAD2_01597 WP_068004687.1: acetate--CoA ligase is similar to: | PaperBLAST |
aacS / D6EQU8: acetoacetate-CoA ligase (EC 6.2.1.16) from Streptomyces lividans | 26% id, 92% cov |
AACS_RAT / Q9JMI1: Acetoacetyl-CoA synthetase; EC 6.2.1.16 from Rattus norvegicus | 25% id, 89% cov |
AACS_MOUSE / Q9D2R0: Acetoacetyl-CoA synthetase; EC 6.2.1.16 from Mus musculus | 25% id, 89% cov |
PsAD2_RS08265 PsAD2_01686 WP_068004813.1: long-chain fatty acid--CoA ligase is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 29% id, 76% cov |
PsAD2_RS09605 PsAD2_01951 WP_068005323.1: malonyl-CoA synthase is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 32% id, 62% cov |
aacS / D6EQU8: acetoacetate-CoA ligase (EC 6.2.1.16) from Streptomyces lividans | 34% id, 12% cov |
PsAD2_RS19145 PsAD2_03861 WP_068009600.1: AMP-binding protein is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 32% id, 62% cov |
PsAD2_RS15085 PsAD2_03058 WP_175485046.1: AMP-binding protein is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 29% id, 61% cov |
PsAD2_RS06005 PsAD2_01223 WP_175485038.1: AMP-binding protein is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 26% id, 42% cov |
PsAD2_RS13220 PsAD2_02679 WP_068006650.1: AMP-binding protein is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 33% id, 24% cov |
PsAD2_RS16160 PsAD2_03275 WP_068008162.1: non-ribosomal peptide synthetase is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 25% id, 31% cov |
PsAD2_RS20445 PsAD2_04108 WP_068010148.1: non-ribosomal peptide synthetase is similar to: | PaperBLAST |
Ac3H11_3009: Acetoacetate--CoA ligase (EC 6.2.1.16) from Acidovorax sp. | 26% id, 19% 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 18 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory