Curated BLAST

Curated BLAST for Genomes

Curated BLAST

Searching in Sulfurimonas denitrificans DSM 1251 (GCF_000012965.1)

Found 36 curated entries in PaperBLAST's database that match '1.2.1.88' as complete word(s).

These curated entries have 27 distinct sequences.

Running ublast with E ≤ 0.01

Found 2 relevant proteins in Sulfurimonas denitrificans DSM 1251, or try another query

SUDEN_RS06940 Suden_1327 WP_011372957.1: bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase is similar to:	PaperBLAST
Q9RW56: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Deinococcus radiodurans	32% id, 98% cov
Q72IB9: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Thermus thermophilus	31% id, 98% cov
Q9K9B2: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Alkalihalobacillus halodurans	29% id, 97% cov
ROCA2_BACSU / P94391: 1-pyrroline-5-carboxylate dehydrogenase 2; P5C dehydrogenase 2; L-glutamate gamma-semialdehyde dehydrogenase; EC 1.2.1.88 from Bacillus subtilis	28% id, 99% cov
Q4DRT8: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Trypanosoma cruzi	30% id, 89% cov
Q65NN2: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Bacillus licheniformis	27% id, 99% cov
AL4A1_HUMAN / P30038: Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial; P5C dehydrogenase; Aldehyde dehydrogenase family 4 member A1; L-glutamate gamma-semialdehyde dehydrogenase; EC 1.2.1.88 from Homo sapiens ALDH4A1 / P30038: Δ¹-pyrroline-5-carboxylate dehydrogenase, mitochondrial subunit (EC 1.2.1.88) from Homo sapiens P30038: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Homo sapiens	29% id, 91% cov
AL4A1_MOUSE / Q8CHT0: Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial; P5C dehydrogenase; Aldehyde dehydrogenase family 4 member A1; L-glutamate gamma-semialdehyde dehydrogenase; EC 1.2.1.88 from Mus musculus Q8CHT0: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Mus musculus	28% id, 88% cov
Shewana3_0819: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Shewanella sp.	28% id, 79% cov
HP15_2688: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Marinobacter adhaerens	28% id, 70% cov
Sama_2676: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Shewanella amazonensis	35% id, 44% cov
Psest_3079: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Pseudomonas stutzeri	31% id, 47% cov
A0A2H4PMI3: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Zea mays	26% id, 56% cov
A9S190: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Physcomitrium patens	26% id, 54% cov
PUTA_ECOLI / P09546: Bifunctional protein PutA; EC 1.5.5.2; EC 1.2.1.88 from Escherichia coli PutA / B1014: fused DNA-binding transcriptional repressor / proline dehydrogenase / 1-pyrroline-5-carboxylate dehydrogenase PutA (EC 1.5.5.2; EC 1.2.1.88) from Escherichia coli PutA / P09546: fused DNA-binding transcriptional repressor / proline dehydrogenase / 1-pyrroline-5-carboxylate dehydrogenase PutA (EC 1.5.5.2; EC 1.2.1.88) from Escherichia coli P09546: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); proline dehydrogenase (EC 1.5.5.2) from Escherichia coli	28% id, 48% cov
F7X6I3: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Sinorhizobium meliloti	31% id, 42% cov
AL121_ARATH / Q8VZC3: Delta-1-pyrroline-5-carboxylate dehydrogenase 12A1, mitochondrial; AtP5CDH; P5C dehydrogenase; Aldehyde dehydrogenase family 12 member A1; L-glutamate gamma-semialdehyde dehydrogenase; EC 1.2.1.88 from Arabidopsis thaliana Q8VZC3: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Arabidopsis thaliana	23% id, 56% cov
AZOBR_RS23695: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Azospirillum brasilense	33% id, 35% cov
HSERO_RS00905: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Herbaspirillum seropedicae	32% id, 36% cov
AO353_12810: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Pseudomonas fluorescens	33% id, 34% cov
RR42_RS20125: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Cupriavidus basilensis	34% id, 32% cov
putA / P10503: trifunctional transcriptional regulator/proline dehydrogenase/L-glutamate γ-semialdehyde dehydrogenase (EC 1.2.1.88; EC 1.5.5.2) from Salmonella typhimurium	32% id, 33% cov
putA / Q88D80: proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase (EC 1.2.1.88; EC 1.5.5.2) from Pseudomonas putida	32% id, 32% cov
BWI76_RS10795: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Klebsiella michiganensis	31% id, 33% cov
PGA1_c11750: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Phaeobacter inhibens	33% id, 26% cov
Ac3H11_2850: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Acidovorax sp.	32% id, 23% cov
Ac3H11_2850: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Acidovorax sp.	28% id, 19% cov
PGA1_c11750: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Phaeobacter inhibens	46% id, 8% cov
More...

SUDEN_RS09855 Suden_1899 WP_011373513.1: aldehyde dehydrogenase family protein is similar to:	PaperBLAST
Q72IB9: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Thermus thermophilus	30% id, 90% cov
ROCA2_BACSU / P94391: 1-pyrroline-5-carboxylate dehydrogenase 2; P5C dehydrogenase 2; L-glutamate gamma-semialdehyde dehydrogenase; EC 1.2.1.88 from Bacillus subtilis	29% id, 89% cov
Q65NN2: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Bacillus licheniformis	29% id, 89% cov
Q9K9B2: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Alkalihalobacillus halodurans	30% id, 86% cov
Q9RW56: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Deinococcus radiodurans	27% id, 90% cov
AL4A1_HUMAN / P30038: Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial; P5C dehydrogenase; Aldehyde dehydrogenase family 4 member A1; L-glutamate gamma-semialdehyde dehydrogenase; EC 1.2.1.88 from Homo sapiens ALDH4A1 / P30038: Δ¹-pyrroline-5-carboxylate dehydrogenase, mitochondrial subunit (EC 1.2.1.88) from Homo sapiens P30038: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Homo sapiens	27% id, 84% cov
A0A2H4PMI3: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Zea mays	24% id, 78% cov
A9S190: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Physcomitrium patens	23% id, 77% cov
AL121_ARATH / Q8VZC3: Delta-1-pyrroline-5-carboxylate dehydrogenase 12A1, mitochondrial; AtP5CDH; P5C dehydrogenase; Aldehyde dehydrogenase family 12 member A1; L-glutamate gamma-semialdehyde dehydrogenase; EC 1.2.1.88 from Arabidopsis thaliana Q8VZC3: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Arabidopsis thaliana	25% id, 55% cov
Psest_3079: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Pseudomonas stutzeri	25% id, 44% cov
Sama_2676: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Shewanella amazonensis	25% id, 43% cov
Shewana3_0819: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Shewanella sp.	25% id, 41% cov
PGA1_c11750: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Phaeobacter inhibens	26% id, 39% cov
F7X6I3: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Sinorhizobium meliloti	27% id, 35% cov
HSERO_RS00905: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Herbaspirillum seropedicae	25% id, 37% cov
Ac3H11_2850: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Acidovorax sp.	25% id, 36% cov
HP15_2688: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Marinobacter adhaerens	25% id, 35% cov
AZOBR_RS23695: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Azospirillum brasilense	26% id, 34% cov
RR42_RS20125: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Cupriavidus basilensis	24% id, 34% cov
putA / Q88D80: proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase (EC 1.2.1.88; EC 1.5.5.2) from Pseudomonas putida	24% id, 34% cov
BWI76_RS10795: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Klebsiella michiganensis	24% id, 33% cov
PUTA_ECOLI / P09546: Bifunctional protein PutA; EC 1.5.5.2; EC 1.2.1.88 from Escherichia coli PutA / B1014: fused DNA-binding transcriptional repressor / proline dehydrogenase / 1-pyrroline-5-carboxylate dehydrogenase PutA (EC 1.5.5.2; EC 1.2.1.88) from Escherichia coli PutA / P09546: fused DNA-binding transcriptional repressor / proline dehydrogenase / 1-pyrroline-5-carboxylate dehydrogenase PutA (EC 1.5.5.2; EC 1.2.1.88) from Escherichia coli P09546: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); proline dehydrogenase (EC 1.5.5.2) from Escherichia coli	25% id, 32% cov
putA / P10503: trifunctional transcriptional regulator/proline dehydrogenase/L-glutamate γ-semialdehyde dehydrogenase (EC 1.2.1.88; EC 1.5.5.2) from Salmonella typhimurium	24% id, 32% cov
AO353_12810: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Pseudomonas fluorescens	25% id, 29% cov
More...

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