Comparing WP_012333617.1 NCBI__GCF_000019365.1:WP_012333617.1 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)
5ktlA Dihydrodipicolinate synthase from the industrial and evolutionarily important cyanobacteria anabaena variabilis. (see paper)
27% identity, 90% coverage: 5:273/299 of query aligns to 4:274/295 of 5ktlA
4pfmA Shewanella benthica dhdps with lysine and pyruvate
29% identity, 89% coverage: 13:279/299 of query aligns to 10:278/295 of 4pfmA
3s8hA Structure of dihydrodipicolinate synthase complexed with 3- hydroxypropanoic acid(hpa)at 2.70 a resolution
32% identity, 69% coverage: 8:214/299 of query aligns to 4:210/292 of 3s8hA
3puoA Crystal structure of dihydrodipicolinate synthase from pseudomonas aeruginosa(psdhdps)complexed with l-lysine at 2.65a resolution (see paper)
32% identity, 69% coverage: 8:214/299 of query aligns to 4:210/292 of 3puoA
Sites not aligning to the query:
4ptnA Crystal structure of yage, a kdg aldolase protein in complex with magnesium cation coordinated l-glyceraldehyde (see paper)
29% identity, 89% coverage: 6:272/299 of query aligns to 3:275/298 of 4ptnA
4onvA Crystal structure of yage, a kdg aldolase protein in complex with 2- keto-3-deoxy gluconate
29% identity, 89% coverage: 6:272/299 of query aligns to 3:275/298 of 4onvA
4oe7D Crystal structure of yage, a kdg aldolase protein, in complex with aldol condensed product of pyruvate and glyoxal
29% identity, 89% coverage: 6:272/299 of query aligns to 3:275/298 of 4oe7D
4oe7B Crystal structure of yage, a kdg aldolase protein, in complex with aldol condensed product of pyruvate and glyoxal
29% identity, 89% coverage: 6:272/299 of query aligns to 3:275/298 of 4oe7B
4oe7A Crystal structure of yage, a kdg aldolase protein, in complex with aldol condensed product of pyruvate and glyoxal
29% identity, 89% coverage: 6:272/299 of query aligns to 3:275/298 of 4oe7A
3nevA Crystal structure of yage, a prophage protein from e. Coli k12 in complex with kdgal (see paper)
29% identity, 89% coverage: 6:272/299 of query aligns to 3:275/298 of 3nevA
4dxvA Crystal structure of dihydrodipicolinate synthase from acinetobacter baumannii complexed with mg and cl ions at 1.80 a resolution
24% identity, 96% coverage: 8:293/299 of query aligns to 4:290/291 of 4dxvA
3u8gA Crystal structure of the complex of dihydrodipicolinate synthase from acinetobacter baumannii with oxalic acid at 1.80 a resolution
24% identity, 96% coverage: 8:293/299 of query aligns to 4:290/291 of 3u8gA
3tdfA Crystal structure of the complex of dihydrodipicolinate synthase from acinetobacter baumannii with 2-ketobutanoic acid at 1.99 a resolution
24% identity, 96% coverage: 8:293/299 of query aligns to 4:290/291 of 3tdfA
3tceA Crystal structure of the complex of dihydrodipicolinate synthase from acinetobacter baumannii with 5-hydroxylysine at 2.6 a resolution
24% identity, 96% coverage: 8:293/299 of query aligns to 4:290/291 of 3tceA
3rk8A Crystal structure of the chloride inhibited dihydrodipicolinate synthase from acinetobacter baumannii complexed with pyruvate at 1.8 a resolution
24% identity, 96% coverage: 8:293/299 of query aligns to 4:290/291 of 3rk8A
3pueB Crystal structure of the complex of dhydrodipicolinate synthase from acinetobacter baumannii with lysine at 2.6a resolution
24% identity, 96% coverage: 8:293/299 of query aligns to 4:290/291 of 3pueB
5t25A Kinetic, spectral and structural characterization of the slow binding inhibitor acetopyruvate with dihydrodipicolinate synthase from escherichia coli.
27% identity, 96% coverage: 6:293/299 of query aligns to 3:292/293 of 5t25A
2atsA Dihydrodipicolinate synthase co-crystallised with (s)-lysine
27% identity, 96% coverage: 6:293/299 of query aligns to 2:291/292 of 2atsA
P0A6L2 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 from Escherichia coli (strain K12) (see 7 papers)
27% identity, 96% coverage: 6:293/299 of query aligns to 2:291/292 of P0A6L2
Q07607 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; Protein MosA; EC 4.3.3.7 from Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti) (see paper)
28% identity, 96% coverage: 6:293/299 of query aligns to 2:290/292 of Q07607
>WP_012333617.1 NCBI__GCF_000019365.1:WP_012333617.1
MANIDWGGIFPVLVTPFGPDGSINELRYKELIDEAIRNGARGIVAAGSTGEFYALTISER
ARLYKLTVDHVAGRIPVLAGVADLRVEDVVDACQAAVAAGCVGGMILPPIYAMPSPREIV
AFFEHVSRSSSLPLMLYNSPRRAGIDINPALVEQLSKLPTVVAIKDSSGLINQVTELVQR
VGGSLRVFVGYETMIVPARAVGAHGVIAMAHQIAGPLIRDYWDQALKGGESVDDMGRDVF
AFYRCFQSGAYYAAIKETMTQLGRDAGGPRLPLLPLTGDQKAAIAKIIGEAGLSRWAKT
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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