SitesBLAST
Comparing WP_164924158.1 NCBI__GCF_000018545.1:WP_164924158.1 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)
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
48% identity, 92% coverage: 5:370/399 of query aligns to 1:358/375 of 2eh6A
- active site: F127 (= F131), E179 (= E183), D212 (= D216), Q215 (= Q219), K241 (= K245), T270 (= T274), R352 (= R364)
- binding pyridoxal-5'-phosphate: G95 (= G98), T96 (≠ A99), F127 (= F131), H128 (= H132), E179 (= E183), D212 (= D216), V214 (= V218), K241 (= K245)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
48% identity, 92% coverage: 5:370/399 of query aligns to 2:359/376 of O66442
- GT 96:97 (≠ GA 98:99) binding pyridoxal 5'-phosphate
- K242 (= K245) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T274) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
45% identity, 93% coverage: 20:392/399 of query aligns to 25:400/402 of 4jevB
- active site: F136 (= F131), E188 (= E183), D221 (= D216), Q224 (= Q219), K250 (= K245), T279 (= T274), R372 (= R364)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (≠ V41), S102 (= S97), G103 (= G98), T104 (≠ A99), F136 (= F131), H137 (= H132), E188 (= E183), E193 (= E188), D221 (= D216), V223 (= V218), Q224 (= Q219), K250 (= K245), R372 (= R364)
P40732 Acetylornithine/succinyldiaminopimelate aminotransferase; ACOAT; DapATase; Succinyldiaminopimelate transferase; EC 2.6.1.11; EC 2.6.1.17 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
45% identity, 93% coverage: 20:392/399 of query aligns to 30:405/405 of P40732
- GT 108:109 (≠ GA 98:99) binding pyridoxal 5'-phosphate
- K255 (= K245) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T274) binding pyridoxal 5'-phosphate
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
44% identity, 96% coverage: 7:390/399 of query aligns to 11:393/393 of 2ordA
- active site: F134 (= F131), E186 (= E183), D219 (= D216), Q222 (= Q219), K248 (= K245), T276 (= T274), R367 (= R364)
- binding pyridoxal-5'-phosphate: G102 (= G98), T103 (≠ A99), F134 (= F131), H135 (= H132), E186 (= E183), D219 (= D216), V221 (= V218), Q222 (= Q219), K248 (= K245)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
44% identity, 96% coverage: 7:390/399 of query aligns to 3:385/385 of Q9X2A5
- GT 94:95 (≠ GA 98:99) binding pyridoxal 5'-phosphate
- T268 (= T274) binding pyridoxal 5'-phosphate
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
45% identity, 93% coverage: 20:392/399 of query aligns to 25:395/397 of 4jewA
- active site: F136 (= F131), E188 (= E183), D221 (= D216), Q224 (= Q219), K250 (= K245), T274 (= T274), R367 (= R364)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G98), T104 (≠ A99), F136 (= F131), H137 (= H132), R139 (= R134), E188 (= E183), E193 (= E188), D221 (= D216), V223 (= V218), K250 (= K245)
- binding picric acid: K25 (≠ R20), K27 (≠ E22), W32 (≠ I27)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
45% identity, 93% coverage: 20:392/399 of query aligns to 19:389/389 of 2pb0A
- active site: F130 (= F131), E182 (= E183), D215 (= D216), Q218 (= Q219), K244 (= K245), T268 (= T274), R361 (= R364)
- binding pyridoxal-5'-phosphate: S96 (= S97), G97 (= G98), T98 (≠ A99), F130 (= F131), H131 (= H132), E182 (= E183), D215 (= D216), V217 (= V218), Q218 (= Q219), K244 (= K245)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
44% identity, 96% coverage: 5:386/399 of query aligns to 33:424/429 of P73133
- Y39 (= Y11) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S97) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G98) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A99) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R134) 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 (= E188) 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 (= D216) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q219) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K245) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T274) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R364) 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.
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
45% identity, 95% coverage: 11:388/399 of query aligns to 16:396/400 of 4addA
- active site: F136 (= F131), E188 (= E183), D221 (= D216), Q224 (= Q219), K250 (= K245), T279 (= T274), R372 (= R364)
- binding pyridoxal-5'-phosphate: G103 (= G98), A104 (= A99), F136 (= F131), H137 (= H132), D221 (= D216), V223 (= V218), K250 (= K245)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y11), F136 (= F131), R139 (= R134)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
45% identity, 95% coverage: 11:388/399 of query aligns to 16:396/401 of 4adbB
- active site: F136 (= F131), E188 (= E183), D221 (= D216), Q224 (= Q219), K250 (= K245), T279 (= T274), R372 (= R364)
- binding pyridoxal-5'-phosphate: S102 (= S97), G103 (= G98), A104 (= A99), F136 (= F131), H137 (= H132), D221 (= D216), V223 (= V218), Q224 (= Q219), K250 (= K245)
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)
44% identity, 95% coverage: 10:388/399 of query aligns to 72:447/457 of Q9M8M7