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Searching for up to 100 curated homologs for WP_090216616.1 NCBI__GCF_002796795.1:WP_090216616.1 (1135 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

PGA1_c11750 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Phaeobacter inhibens BS107
    77% identity, 99% coverage of query (1726 bits)

HP15_2688 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Marinobacter adhaerens HP15
    54% identity, 98% coverage of query (1217 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
    49% identity, 97% coverage of query (1007 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, 100% coverage of query (999 bits)

HSERO_RS00905 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Herbaspirillum seropedicae SmR1
    51% identity, 96% coverage of query (995 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, 95% coverage of query (975 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
    49% identity, 95% coverage of query (974 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, 97% coverage of query (971 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)
    48% identity, 97% coverage of query (969 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, 95% coverage of query (961 bits)

AZOBR_RS23695 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Azospirillum brasilense Sp245
    49% identity, 95% coverage of query (949 bits)

F7X6I3 L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88) from Sinorhizobium meliloti (see paper)
    49% identity, 97% coverage of query (943 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 (935 bits)

6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site
    48% identity, 97% coverage of query (935 bits)

7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site
    48% identity, 97% coverage of query (933 bits)

7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane
    48% identity, 97% coverage of query (933 bits)

7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene
    48% identity, 97% coverage of query (933 bits)

6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site
    48% identity, 97% coverage of query (932 bits)

6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site
    48% identity, 97% coverage of query (932 bits)

7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site
    48% identity, 97% coverage of query (931 bits)

6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site
    48% identity, 97% coverage of query (931 bits)

5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21
    48% identity, 97% coverage of query (928 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
    48% identity, 97% coverage of query (917 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, 87% coverage of query (914 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, 86% coverage of query (913 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
    47% identity, 85% coverage of query (880 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, 85% coverage of query (879 bits)

3hazA / Q89E26 Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
    49% identity, 84% coverage of query (867 bits)

6bsnA Structure of proline utilization a (puta) with proline bound in remote sites
    49% identity, 84% coverage of query (857 bits)

PUTA / CAA55136.1 proline dehydrogenase from Escherichia coli (see paper)
    40% identity, 83% coverage of query (590 bits)

5ur2B / Q6MNK1 Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
    32% identity, 74% coverage of query (390 bits)

4nmfB Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite
    32% identity, 73% coverage of query (338 bits)

4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite
    32% identity, 73% coverage of query (338 bits)

4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid
    33% identity, 72% coverage of query (337 bits)

7na0A / Q746X3 Structure of geobacter sulfurreducens proline utilization a (puta) variant a206w (see paper)
    32% identity, 72% coverage of query (335 bits)

4nmfA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite
    32% identity, 73% coverage of query (333 bits)

4nmeA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine
    32% identity, 73% coverage of query (330 bits)

Build an alignment

Build an alignment for WP_090216616.1 and 37 homologs with ≥ 30% identity

Select sequences

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

Or download the sequences

Change minimum %identity:

Additional hits (identity < 30%)

5ux5A / A0A1X8XLF1 Structure of proline utilization a (puta) from corynebacterium freiburgense (see paper)
    28% identity, 74% coverage of query (212 bits)

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by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory