SitesBLAST
Comparing WP_007731008.1 NCBI__GCF_002893965.1:WP_007731008.1 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)
6rl5G The first crystal structure of the daba aminotransferase ectb in the ectoine biosynthesis pathway of the model organism chromohalobacter salexigens dsm 3034 (see paper)
53% identity, 99% coverage: 5:418/420 of query aligns to 1:418/422 of 6rl5G
- active site: S16 (≠ C20), F137 (= F141), D237 (= D240), K266 (= K269)
- binding pyridoxal-5'-phosphate: G110 (= G114), T111 (≠ S115), F137 (= F141), H138 (= H142), D237 (= D240), I239 (≠ V242), Q240 (= Q243), K266 (= K269), G294 (= G297), T295 (= T298)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
33% identity, 93% coverage: 24:413/420 of query aligns to 18:387/390 of 8ht4B
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
32% identity, 95% coverage: 16:413/420 of query aligns to 4:373/375 of 2eh6A
- active site: F127 (= F141), E179 (= E207), D212 (= D240), Q215 (= Q243), K241 (= K269), T270 (= T298), R352 (≠ K392)
- binding pyridoxal-5'-phosphate: G95 (= G114), T96 (≠ S115), F127 (= F141), H128 (= H142), E179 (= E207), D212 (= D240), V214 (= V242), K241 (= K269)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
32% identity, 95% coverage: 16:413/420 of query aligns to 5:374/376 of O66442
- GT 96:97 (≠ GS 114:115) binding pyridoxal 5'-phosphate
- K242 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T298) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 91% coverage: 26:406/420 of query aligns to 22:377/387 of 1wkhA
- active site: F132 (= F141), E184 (= E207), D217 (= D240), Q220 (= Q243), K246 (= K269), T275 (≠ F299), R363 (≠ K392)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ A50), S104 (≠ T113), G105 (= G114), T106 (≠ S115), F132 (= F141), S133 (≠ H142), E184 (= E207), E189 (= E212), D217 (= D240), I219 (≠ V242), K246 (= K269), R363 (≠ K392)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 91% coverage: 26:406/420 of query aligns to 22:377/387 of 1wkgA
- active site: F132 (= F141), E184 (= E207), D217 (= D240), Q220 (= Q243), K246 (= K269), T275 (≠ F299), R363 (≠ K392)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ A50), G105 (= G114), T106 (≠ S115), F132 (= F141), S133 (≠ H142), R135 (≠ M144), E184 (= E207), D217 (= D240), I219 (≠ V242), Q220 (= Q243), K246 (= K269), G273 (= G297), T274 (= T298), T275 (≠ F299)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 91% coverage: 26:406/420 of query aligns to 22:377/387 of 1vefA
- active site: F132 (= F141), D217 (= D240), K246 (= K269), T275 (≠ F299), R363 (≠ K392)
- binding pyridoxal-5'-phosphate: G105 (= G114), T106 (≠ S115), F132 (= F141), S133 (≠ H142), E184 (= E207), D217 (= D240), I219 (≠ V242), K246 (= K269)
Sites not aligning to the query:
P22256 4-aminobutyrate aminotransferase GabT; 5-aminovalerate transaminase; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; L-AIBAT; EC 2.6.1.19; EC 2.6.1.48 from Escherichia coli (strain K12) (see 2 papers)
30% identity, 98% coverage: 1:413/420 of query aligns to 1:419/426 of P22256
- I50 (≠ A50) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (= GS 114:115) binding pyridoxal 5'-phosphate
- E211 (= E212) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V242) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q243) binding pyridoxal 5'-phosphate
- K268 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T298) binding pyridoxal 5'-phosphate
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
34% identity, 91% coverage: 26:406/420 of query aligns to 30:385/395 of Q5SHH5
- GT 113:114 (≠ GS 114:115) binding pyridoxal 5'-phosphate
- K254 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T283 (≠ F299) binding pyridoxal 5'-phosphate
4ppmA Crystal structure of pige: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (map) from serratia sp. Fs14 (see paper)
31% identity, 90% coverage: 26:405/420 of query aligns to 47:444/464 of 4ppmA
- active site: Y159 (≠ F141), E212 (= E207), D245 (= D240), Q248 (= Q243), K274 (= K269), T309 (= T298), R431 (≠ K392)
- binding magnesium ion: A351 (≠ S341), Y354 (≠ F344), V357 (≠ E347)
- binding pyridoxal-5'-phosphate: G132 (= G114), T133 (≠ S115), Y159 (≠ F141), H160 (= H142), D245 (= D240), V247 (= V242), K274 (= K269)
Sites not aligning to the query:
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
31% identity, 93% coverage: 24:413/420 of query aligns to 23:418/425 of 1sffA
- active site: Y137 (≠ F141), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (≠ K392)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ S82), G110 (= G114), S111 (= S115), Y137 (≠ F141), H138 (= H142), R140 (≠ M144), E205 (= E207), D238 (= D240), V240 (= V242), Q241 (= Q243), K267 (= K269), T296 (= T298)
- binding sulfate ion: N152 (≠ S155), Y393 (≠ D388)
Sites not aligning to the query:
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
31% identity, 93% coverage: 24:413/420 of query aligns to 23:418/425 of 1sf2A
- active site: Y137 (≠ F141), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (≠ K392)
- binding pyridoxal-5'-phosphate: G110 (= G114), S111 (= S115), Y137 (≠ F141), H138 (= H142), E205 (= E207), D238 (= D240), V240 (= V242), Q241 (= Q243), K267 (= K269)
- binding sulfate ion: N152 (≠ S155), Y393 (≠ D388)
Sites not aligning to the query:
A0A0J9X1Q5 Aminotransferase PigE; EC 2.6.1.- from Serratia sp. (strain FS14) (see paper)
34% identity, 80% coverage: 26:363/420 of query aligns to 418:744/853 of A0A0J9X1Q5
- GT 503:504 (≠ GS 114:115) binding pyridoxal 5'-phosphate
- K645 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T680 (= T298) binding pyridoxal 5'-phosphate
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
31% identity, 93% coverage: 24:413/420 of query aligns to 23:418/425 of 1szkA
- active site: Y137 (≠ F141), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (≠ K392)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G114), S111 (= S115), Y137 (≠ F141), H138 (= H142), E205 (= E207), D238 (= D240), V240 (= V242), Q241 (= Q243), K267 (= K269)
Sites not aligning to the query:
P50457 4-aminobutyrate aminotransferase PuuE; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; EC 2.6.1.19 from Escherichia coli (strain K12) (see paper)
32% identity, 92% coverage: 29:414/420 of query aligns to 28:418/421 of P50457
- K267 (= K269) mutation to A: No GABA-AT activity.
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
29% identity, 98% coverage: 2:414/420 of query aligns to 19:424/429 of P73133
- Y39 (= Y19) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (≠ T113) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G114) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (≠ S115) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (≠ M144) mutation to A: 4100-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 9.5% of N-acetylornithine aminotransferase wild-type activity.
- E223 (= E212) mutation to A: 65-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 50% of N-acetylornithine aminotransferase wild-type activity.; mutation to S: 73-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Shows 160% of N-acetylornithine aminotransferase wild-type activity.
- D251 (= D240) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q243) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K269) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T298) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (≠ K392) mutation to A: 2080-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 18% of N-acetylornithine aminotransferase wild-type activity.
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
30% identity, 96% coverage: 16:417/420 of query aligns to 12:387/393 of 2ordA
- active site: F134 (= F141), E186 (= E207), D219 (= D240), Q222 (= Q243), K248 (= K269), T276 (= T298), R367 (≠ K392)
- binding pyridoxal-5'-phosphate: G102 (= G114), T103 (≠ S115), F134 (= F141), H135 (= H142), E186 (= E207), D219 (= D240), V221 (= V242), Q222 (= Q243), K248 (= K269)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
30% identity, 96% coverage: 16:417/420 of query aligns to 4:379/385 of Q9X2A5
- GT 94:95 (≠ GS 114:115) binding pyridoxal 5'-phosphate
- T268 (= T298) binding pyridoxal 5'-phosphate
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
32% identity, 91% coverage: 24:405/420 of query aligns to 19:373/390 of A0QYS9
- K304 (≠ A331) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Q9M8M7 Acetylornithine aminotransferase, chloroplastic/mitochondrial; ACOAT; Acetylornithine transaminase; AOTA; Protein HOPW1-1-INTERACTING 1; EC 2.6.1.11 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 98% coverage: 2:413/420 of query aligns to 56:451/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
Query Sequence
>WP_007731008.1 NCBI__GCF_002893965.1:WP_007731008.1
MNINEASIFETLESEVRSYCRDWPAVFTSASGSWIRDENGRDYLDFFAGAGALNYGHNNP
VLKSALVDYIMSDGITHGLDMSTVAKREFLETFQRNILEPRGLDYKVQFPGPTGSNTVEA
ALKLARKVTGRSAVINFTNAFHGMTLGALSVTGNSMKRAGAGVPLVHTTPMPFDNYFDGV
TEDFQWFSRVLDDSGSGINRPAAVIVETVQGEGGVNVARPEWLRALATLCSDRGILLIVD
DVQMGCGRTGPFFSFEEAGIVPDIVTLSKSISGYGMPMALTLFKRELDVWGPGEHNGTFR
GNNPAFVTSKVALDHYWSDDALTKTTLKKGARISECFANLSDQFPGEVSHRGRGLVQGLV
FEQPERAGKVCQLAFDEGLLAETSGPSDQVVKLLPALTITDDELEHGLSILAEATLKVCS
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory