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Searching for up to 100 curated homologs for WP_011384888.1 AMB_RS12610 bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA (1039 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.

Hits with ≥ 30% identity

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, 96% coverage of query (940 bits)

HP15_2688 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Marinobacter adhaerens HP15
    48% identity, 97% coverage of query (937 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)
    52% identity, 92% coverage of query (930 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 (929 bits)

3hazA / Q89E26 Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
    52% identity, 98% coverage of query (926 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
    51% identity, 92% coverage of query (923 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
    54% identity, 91% coverage of query (919 bits)

6bsnA Structure of proline utilization a (puta) with proline bound in remote sites
    51% identity, 98% coverage of query (918 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, 95% coverage of query (917 bits)

HSERO_RS00905 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Herbaspirillum seropedicae SmR1
    52% identity, 97% coverage of query (914 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)
    49% identity, 97% coverage of query (908 bits)

BWI76_RS10795 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Klebsiella michiganensis M5al
    51% identity, 92% coverage of query (904 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, 92% coverage of query (899 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)
    49% identity, 96% coverage of query (894 bits)

PGA1_c11750 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Phaeobacter inhibens BS107
    51% identity, 96% coverage of query (875 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
    51% identity, 91% coverage of query (875 bits)

F7X6I3 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Sinorhizobium meliloti (see paper)
    50% identity, 96% coverage of query (845 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)
    49% identity, 97% coverage of query (840 bits)

7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site
    49% identity, 97% coverage of query (838 bits)

7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane
    49% identity, 97% coverage of query (838 bits)

7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene
    49% identity, 97% coverage of query (838 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, 97% coverage of query (836 bits)

7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site
    49% identity, 97% coverage of query (836 bits)

6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site
    49% identity, 97% coverage of query (836 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, 97% coverage of query (834 bits)

6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site
    49% identity, 97% coverage of query (834 bits)

5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21
    49% identity, 97% coverage of query (828 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, 97% coverage of query (820 bits)

PUTA / CAA55136.1 proline dehydrogenase from Escherichia coli (see paper)
    37% identity, 94% coverage of query (557 bits)

5ur2B / Q6MNK1 Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
    32% identity, 84% coverage of query (423 bits)

4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite
    31% identity, 83% coverage of query (337 bits)

4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid
    32% identity, 83% coverage of query (336 bits)

4nmfB Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite
    31% identity, 83% coverage of query (335 bits)

7na0A / Q746X3 Structure of geobacter sulfurreducens proline utilization a (puta) variant a206w (see paper)
    31% identity, 83% coverage of query (333 bits)

4nmeA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine
    31% identity, 83% coverage of query (333 bits)

4nmfA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite
    32% identity, 83% coverage of query (329 bits)

4nmcA / Q746X3 Crystal structure of oxidized proline utilization a (puta) from geobacter sulfurreducens pca complexed with zwittergent 3-12 (see paper)
    31% identity, 84% coverage of query (314 bits)

Build an alignment

Build an alignment for WP_011384888.1 and 37 homologs with ≥ 30% identity

Select sequences

Add sequences from UniProt, PDB, RefSeq, or MicrobesOnline (separate identifiers with commas or spaces):

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Change minimum %identity:

Additional hits (identity < 30%)

5ux5A / A0A1X8XLF1 Structure of proline utilization a (puta) from corynebacterium freiburgense (see paper)
    29% identity, 80% coverage of query (204 bits)

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by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory