Searching for up to 100 curated homologs for AO353_12810 FitnessBrowser__pseudo3_N2E3:AO353_12810 (1317 a.a.)
Found high-coverage hits (≥70%) to 30 curated proteins.
Removed hits that are identical to the query, leaving 29
You can add additional sequences or change the %identity threshold for inclusion. Once you have selected sequences, you can build an alignment and a tree.
putA / Q88D80 proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase (EC 1.2.1.88; EC 1.5.5.2) from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see 11 papers)
88% identity, 100% coverage of query (2398 bits)
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 K-12 substr. MG1655 (see 41 papers)
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 (strain K12) (see 39 papers)
PUTA_ECOLI / P09546 Bifunctional protein PutA; EC 1.5.5.2; EC 1.2.1.88 from Escherichia coli (strain K12) (see paper)
P09546 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); proline dehydrogenase (EC 1.5.5.2) from Escherichia coli (see 6 papers)
putA / GB|BAA35791.1 proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase; EC 1.5.1.12; EC 1.5.99.8 from Escherichia coli K12 (see 9 papers)
74% identity, 100% coverage of query (1999 bits)
BWI76_RS10795 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Klebsiella michiganensis M5al
73% identity, 100% coverage of query (1970 bits)
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 (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
73% identity, 100% coverage of query (1954 bits)
RR42_RS20125 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Cupriavidus basilensis FW507-4G11
74% identity, 100% coverage of query (1920 bits)
Ac3H11_2850 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Acidovorax sp. GW101-3H11
70% identity, 93% coverage of query (1727 bits)
AZOBR_RS23695 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Azospirillum brasilense Sp245
63% identity, 94% coverage of query (1498 bits)
F7X6I3 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Sinorhizobium meliloti (see paper)
60% identity, 94% coverage of query (1410 bits)
6x9dA / F7X6I3 Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
60% identity, 94% coverage of query (1409 bits)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site
60% identity, 94% coverage of query (1408 bits)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane
60% identity, 94% coverage of query (1408 bits)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site
60% identity, 94% coverage of query (1407 bits)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site
60% identity, 94% coverage of query (1405 bits)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene
60% identity, 94% coverage of query (1405 bits)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site
60% identity, 94% coverage of query (1404 bits)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site
60% identity, 94% coverage of query (1403 bits)
HSERO_RS00905 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Herbaspirillum seropedicae SmR1
60% identity, 94% coverage of query (1397 bits)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site
60% identity, 94% coverage of query (1397 bits)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21
60% identity, 94% coverage of query (1393 bits)
6ufpA Structure of proline utilization a with the fad covalently modified by l-thiazolidine-2-carboxylate and three cysteines (cys46, cys470, cys638) modified to s,s-(2-hydroxyethyl)thiocysteine
59% identity, 94% coverage of query (1367 bits)
PUTA / CAA55136.1 proline dehydrogenase from Escherichia coli (see paper)
55% identity, 100% coverage of query (1287 bits)
PGA1_c11750 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Phaeobacter inhibens BS107
48% identity, 93% coverage of query (992 bits)
HP15_2688 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Marinobacter adhaerens HP15
45% identity, 93% coverage of query (969 bits)
Psest_3079 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Pseudomonas stutzeri RCH2
50% identity, 77% coverage of query (954 bits)
Shewana3_0819 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Shewanella sp. ANA-3
48% identity, 77% coverage of query (923 bits)
Sama_2676 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Shewanella amazonensis SB2B
50% identity, 75% coverage of query (922 bits)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites
47% identity, 77% coverage of query (860 bits)
3hazA / Q89E26 Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
47% identity, 77% coverage of query (857 bits)
Build an alignment for AO353_12810 and 28 homologs with ≥ 30% identity
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5ux5A / A0A1X8XLF1 Structure of proline utilization a (puta) from corynebacterium freiburgense (see paper)
29% identity, 71% coverage of query (226 bits)
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Lawrence Berkeley National Laboratory