Searching for up to 100 curated homologs for WP_036264374.1 NCBI__GCF_000746085.1:WP_036264374.1 (1033 a.a.)
Found high-coverage hits (≥70%) to 38 curated proteins.
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.
3hazA / Q89E26 Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
60% identity, 98% coverage of query (1156 bits)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites
60% identity, 98% coverage of query (1140 bits)
SO3774 proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.5.2; EC 1.2.1.88) from Shewanella oneidensis MR-1
48% identity, 97% coverage of query (926 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, 97% coverage of query (921 bits)
Sama_2676 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Shewanella amazonensis SB2B
49% identity, 97% coverage of query (917 bits)
Psest_3079 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Pseudomonas stutzeri RCH2
49% identity, 99% coverage of query (912 bits)
AZOBR_RS23695 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Azospirillum brasilense Sp245
52% identity, 94% coverage of query (882 bits)
AO353_12810 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Pseudomonas fluorescens FW300-N2E3
48% identity, 97% coverage of query (865 bits)
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)
49% identity, 97% coverage of query (859 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
48% identity, 96% coverage of query (853 bits)
BWI76_RS10795 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Klebsiella michiganensis M5al
48% identity, 96% coverage of query (848 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)
47% identity, 97% coverage of query (842 bits)
HSERO_RS00905 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Herbaspirillum seropedicae SmR1
49% identity, 94% coverage of query (826 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
49% identity, 97% coverage of query (825 bits)
F7X6I3 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Sinorhizobium meliloti (see paper)
50% identity, 94% coverage of query (822 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)
48% identity, 95% coverage of query (820 bits)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site
49% identity, 96% coverage of query (813 bits)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site
49% identity, 96% coverage of query (813 bits)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site
49% identity, 96% coverage of query (813 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)
50% identity, 94% coverage of query (812 bits)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site
49% identity, 96% coverage of query (812 bits)
HP15_2688 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Marinobacter adhaerens HP15
44% identity, 96% coverage of query (811 bits)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site
50% identity, 94% coverage of query (810 bits)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene
50% identity, 94% coverage of query (810 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, 96% coverage of query (809 bits)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site
50% identity, 94% coverage of query (809 bits)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane
50% identity, 94% coverage of query (809 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
49% identity, 96% coverage of query (807 bits)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21
49% identity, 96% coverage of query (806 bits)
PUTA / CAA55136.1 proline dehydrogenase from Escherichia coli (see paper)
36% identity, 95% coverage of query (493 bits)
5ur2B / Q6MNK1 Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
30% identity, 85% coverage of query (359 bits)
4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid
30% identity, 83% coverage of query (285 bits)
4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite
30% identity, 85% coverage of query (285 bits)
4nmeA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine
31% identity, 83% coverage of query (283 bits)
4nmfA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite
30% identity, 85% coverage of query (283 bits)
Build an alignment for WP_036264374.1 and 35 homologs with ≥ 30% identity
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4nmfB Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite
29% identity, 85% coverage of query (281 bits)
7na0A / Q746X3 Structure of geobacter sulfurreducens proline utilization a (puta) variant a206w (see paper)
30% identity, 83% coverage of query (278 bits)
4nmcA / Q746X3 Crystal structure of oxidized proline utilization a (puta) from geobacter sulfurreducens pca complexed with zwittergent 3-12 (see paper)
29% identity, 83% coverage of query (259 bits)
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Lawrence Berkeley National Laboratory