Comparing WP_011975609.1 NCBI__GCF_000017145.1:WP_011975609.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
2x5dD Crystal structure of a probable aminotransferase from pseudomonas aeruginosa (see paper)
53% identity, 92% coverage: 14:385/405 of query aligns to 1:372/380 of 2x5dD
6l1nA Substrate bound bacf structure from bacillus subtillis (see paper)
39% identity, 92% coverage: 14:387/405 of query aligns to 20:386/393 of 6l1nA
Sites not aligning to the query:
6l1lB Apo-bacf structure from bacillus subtillis (see paper)
38% identity, 94% coverage: 7:387/405 of query aligns to 9:387/393 of 6l1lB
6l1oB Product bound bacf structure from bacillus subtillis (see paper)
38% identity, 94% coverage: 7:387/405 of query aligns to 9:387/392 of 6l1oB
2o1bA Structure of aminotransferase from staphylococcus aureus
32% identity, 86% coverage: 32:381/405 of query aligns to 21:365/376 of 2o1bA
1gdeA Crystal structure of pyrococcus protein a-1 e-form (see paper)
30% identity, 90% coverage: 27:390/405 of query aligns to 21:384/388 of 1gdeA
1gd9A Crystall structure of pyrococcus protein-a1 (see paper)
30% identity, 90% coverage: 27:390/405 of query aligns to 21:384/388 of 1gd9A
1o4sB Crystal structure of aspartate aminotransferase (tm1255) from thermotoga maritima at 1.90 a resolution (see paper)
29% identity, 95% coverage: 8:390/405 of query aligns to 12:384/384 of 1o4sB
Q56232 Aspartate/prephenate aminotransferase; AspAT / PAT; Transaminase A; EC 2.6.1.1; EC 2.6.1.78 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see 3 papers)
30% identity, 96% coverage: 5:391/405 of query aligns to 6:385/385 of Q56232
1bkgA Aspartate aminotransferase from thermus thermophilus with maleate (see paper)
30% identity, 95% coverage: 5:388/405 of query aligns to 6:382/382 of 1bkgA
1bjwA Aspartate aminotransferase from thermus thermophilus (see paper)
30% identity, 95% coverage: 5:388/405 of query aligns to 6:382/382 of 1bjwA
3jtxB Crystal structure of aminotransferase (np_283882.1) from neisseria meningitidis z2491 at 1.91 a resolution
29% identity, 93% coverage: 7:384/405 of query aligns to 5:388/393 of 3jtxB
1b5oA Thermus thermophilus aspartate aminotransferase single mutant 1 (see paper)
30% identity, 95% coverage: 5:388/405 of query aligns to 6:382/382 of 1b5oA
1gc4A Thermus thermophilus aspartate aminotransferase tetra mutant 2 complexed with aspartate (see paper)
30% identity, 95% coverage: 5:388/405 of query aligns to 6:382/382 of 1gc4A
1gc3A Thermus thermophilus aspartate aminotransferase tetra mutant 2 complexed with tryptophan (see paper)
30% identity, 95% coverage: 5:388/405 of query aligns to 6:382/382 of 1gc3A
Q58097 (5-formylfuran-3-yl)methyl phosphate transaminase; 4-HFC-P:alanine aminotransferase; EC 2.6.1.108 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
29% identity, 91% coverage: 21:389/405 of query aligns to 20:369/370 of Q58097
8wkjA The crystal structure of aspartate aminotransferases lpg0070 from legionella pneumophila (see paper)
30% identity, 89% coverage: 29:389/405 of query aligns to 30:391/391 of 8wkjA
1j32A Aspartate aminotransferase from phormidium lapideum
29% identity, 95% coverage: 6:388/405 of query aligns to 6:384/388 of 1j32A
6f77A Crystal structure of the prephenate aminotransferase from rhizobium meliloti (see paper)
29% identity, 95% coverage: 7:391/405 of query aligns to 7:398/399 of 6f77A
Q02635 Aspartate/prephenate aminotransferase; AspAT / PAT; Transaminase A; EC 2.6.1.1; EC 2.6.1.79 from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) (see paper)
29% identity, 95% coverage: 7:391/405 of query aligns to 8:399/400 of Q02635
>WP_011975609.1 NCBI__GCF_000017145.1:WP_011975609.1
MEEFHKVRRLPPYVFEQVNRLKASARAAGADIIDLGMGNPDLPTPQSIVDKLCEVVQDPR
THRYSSSKGIPGLRRAQAAYYARRFGVKLNPETQVVATLGSKEGFANMAQAITAPGDVIL
CPNPTYPIHAFGFLMAGGVIRSISVEPDESFFPPLERAVRHSIPKPLALVLNYPSNPTAQ
VATLDFYKDVVAFAKKHDIIVLSDLAYSEIYFNDAPPPSVLEVPGATDVTVEFTSMSKTF
SMPGWRMGFAVGNERLIAALTRVKSYLDYGAFTPIQVAATQALNGDGSDIAEVRSIYKRR
RDVMVESFGKAGFEVPPPPATMFAWAKIPEKFRHLGSLEFSKLLVEKADVAVAPGIGFGE
QGDDYVRLALVENEHRIRQAARNIKRFLSSADETMHNVISLNAHR
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SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory