Curated BLAST for Genomes

 

Curated BLAST

Searching in Lacinutrix himadriensis E4-9a (GCF_001418105.1)

Found 15 curated entries in PaperBLAST's database that match '1.2.1.31' as complete word(s).

These curated entries have 11 distinct sequences.

Running ublast with E ≤ 0.01

Found 11 relevant proteins in Lacinutrix himadriensis E4-9a, or try another query

AMD28_RS11385 WP_055444227.1: aldehyde dehydrogenase family protein
is similar to:
PaperBLAST

amaB / Q88CC3: L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Pseudomonas putida

58% id,
99% cov

SMc04385: L-2-aminoadipate semialdehyde dehydrogenase (EC 1.2.1.31) from Sinorhizobium meliloti

55% id,
100% cov

AL7A1_HUMAN / P49419: Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Homo sapiens
ALDH7A1 / P49419: Alpha-aminoadipic semialdehyde dehydrogenase (EC 1.2.1.8; EC 1.2.1.31) from Homo sapiens
P49419: aldehyde dehydrogenase (NAD+) (EC 1.2.1.3); L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Homo sapiens

54% id,
92% cov

More...

AMD28_RS04480 WP_055442960.1: aldehyde dehydrogenase
is similar to:
PaperBLAST

SMc04385: L-2-aminoadipate semialdehyde dehydrogenase (EC 1.2.1.31) from Sinorhizobium meliloti

29% id,
92% cov

AL7A1_RAT / Q64057: Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Rattus norvegicus

28% id,
86% cov

AL7A1_MOUSE / Q9DBF1: Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Mus musculus
Q9DBF1: aldehyde dehydrogenase (NAD+) (EC 1.2.1.3); L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Mus musculus

27% id,
86% cov

More...

aldA AMD28_RS12250 WP_055444436.1: aldehyde dehydrogenase
is similar to:
PaperBLAST

SMc04385: L-2-aminoadipate semialdehyde dehydrogenase (EC 1.2.1.31) from Sinorhizobium meliloti

29% id,
90% cov

AL7A1_HUMAN / P49419: Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Homo sapiens
ALDH7A1 / P49419: Alpha-aminoadipic semialdehyde dehydrogenase (EC 1.2.1.8; EC 1.2.1.31) from Homo sapiens
P49419: aldehyde dehydrogenase (NAD+) (EC 1.2.1.3); L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Homo sapiens

27% id,
85% cov

AL7A1_RAT / Q64057: Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Rattus norvegicus

26% id,
85% cov

More...

AMD28_RS06035 WP_055443259.1: aldehyde dehydrogenase family protein
is similar to:
PaperBLAST

SMc04385: L-2-aminoadipate semialdehyde dehydrogenase (EC 1.2.1.31) from Sinorhizobium meliloti

27% id,
92% cov

AMD28_RS02025 WP_055442489.1: NAD-dependent succinate-semialdehyde dehydrogenase
is similar to:
PaperBLAST

amaB / Q88CC3: L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Pseudomonas putida

27% id,
92% cov

SMc04385: L-2-aminoadipate semialdehyde dehydrogenase (EC 1.2.1.31) from Sinorhizobium meliloti

27% id,
90% cov

AL7A1_RAT / Q64057: Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Rattus norvegicus

26% id,
86% cov

More...

paaZ AMD28_RS12855 WP_055444545.1: phenylacetic acid degradation bifunctional protein PaaZ
is similar to:
PaperBLAST

amaB / Q88CC3: L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Pseudomonas putida

26% id,
93% cov

AL7A1_MOUSE / Q9DBF1: Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Mus musculus
Q9DBF1: aldehyde dehydrogenase (NAD+) (EC 1.2.1.3); L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Mus musculus

24% id,
80% cov

AL7A1_RAT / Q64057: Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Rattus norvegicus

26% id,
66% cov

More...

AMD28_RS08100 WP_055443647.1: NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
is similar to:
PaperBLAST

SMc04385: L-2-aminoadipate semialdehyde dehydrogenase (EC 1.2.1.31) from Sinorhizobium meliloti

23% id,
94% cov

amaB / Q88CC3: L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Pseudomonas putida

24% id,
90% cov

AL7A1_MOUSE / Q9DBF1: Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Mus musculus
Q9DBF1: aldehyde dehydrogenase (NAD+) (EC 1.2.1.3); L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Mus musculus

24% id,
79% cov

More...

AMD28_RS08960 WP_055443797.1: aldehyde dehydrogenase family protein
is similar to:
PaperBLAST

amaB / Q88CC3: L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Pseudomonas putida

22% id,
75% cov

AL7A1_HUMAN / P49419: Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Homo sapiens
ALDH7A1 / P49419: Alpha-aminoadipic semialdehyde dehydrogenase (EC 1.2.1.8; EC 1.2.1.31) from Homo sapiens
P49419: aldehyde dehydrogenase (NAD+) (EC 1.2.1.3); L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Homo sapiens

23% id,
64% cov

AL7A1_MOUSE / Q9DBF1: Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Mus musculus
Q9DBF1: aldehyde dehydrogenase (NAD+) (EC 1.2.1.3); L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Mus musculus

22% id,
64% cov

More...

AMD28_RS05985 WP_055443249.1: acetate--CoA ligase
is similar to:
PaperBLAST

LYS2_SCHPO / P40976: L-2-aminoadipate reductase; Alpha-aminoadipate reductase; Alpha-AR; L-aminoadipate-semialdehyde dehydrogenase; EC 1.2.1.31; EC 1.2.1.95 from Schizosaccharomyces pombe
lys1 / RF|NP_594314.1: aminoadipate-semialdehyde dehydrogenase; EC 1.2.1.31 from Schizosaccharomyces pombe

23% id,
38% cov

acs AMD28_RS05980 WP_055443248.1: acetate--CoA ligase
is similar to:
PaperBLAST

Q8NJ21: L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Kluyveromyces lactis

24% id,
17% cov

AMD28_RS01395 WP_055442371.1: AMP-dependent synthetase/ligase
is similar to:
PaperBLAST

Q4L235: L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) from Homo sapiens

27% id,
12% 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 9 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory