SitesBLAST
Comparing WP_047007017.1 NCBI__GCF_001010925.1:WP_047007017.1 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)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
44% identity, 95% coverage: 3:377/396 of query aligns to 1:366/376 of O66442
- GT 96:97 (≠ GA 97:98) binding pyridoxal 5'-phosphate
- K242 (= K244) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T273) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
45% identity, 94% coverage: 4:377/396 of query aligns to 1:365/375 of 2eh6A
- active site: F127 (= F130), E179 (= E182), D212 (= D215), Q215 (= Q218), K241 (= K244), T270 (= T273), R352 (= R364)
- binding pyridoxal-5'-phosphate: G95 (= G97), T96 (≠ A98), F127 (= F130), H128 (= H131), E179 (= E182), D212 (= D215), V214 (= V217), K241 (= K244)
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
46% identity, 96% coverage: 6:384/396 of query aligns to 11:387/393 of 2ordA
- active site: F134 (= F130), E186 (= E182), D219 (= D215), Q222 (= Q218), K248 (= K244), T276 (= T273), R367 (= R364)
- binding pyridoxal-5'-phosphate: G102 (= G97), T103 (≠ A98), F134 (= F130), H135 (= H131), E186 (= E182), D219 (= D215), V221 (= V217), Q222 (= Q218), K248 (= K244)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
46% identity, 96% coverage: 6:384/396 of query aligns to 3:379/385 of Q9X2A5
- GT 94:95 (≠ GA 97:98) binding pyridoxal 5'-phosphate
- T268 (= T273) binding pyridoxal 5'-phosphate
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
43% identity, 98% coverage: 4:390/396 of query aligns to 33:428/429 of P73133
- Y39 (= Y10) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S96) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G97) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A98) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R133) 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 (= E187) 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 (= D215) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q218) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K244) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T273) 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)
42% identity, 97% coverage: 6:390/396 of query aligns to 12:398/400 of 4addA
- active site: F136 (= F130), E188 (= E182), D221 (= D215), Q224 (= Q218), K250 (= K244), T279 (= T273), R372 (= R364)
- binding pyridoxal-5'-phosphate: G103 (= G97), A104 (= A98), F136 (= F130), H137 (= H131), D221 (= D215), V223 (= V217), K250 (= K244)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y10), F136 (= F130), R139 (= R133)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
42% identity, 97% coverage: 6:390/396 of query aligns to 12:398/401 of 4adbB
- active site: F136 (= F130), E188 (= E182), D221 (= D215), Q224 (= Q218), K250 (= K244), T279 (= T273), R372 (= R364)
- binding pyridoxal-5'-phosphate: S102 (= S96), G103 (= G97), A104 (= A98), F136 (= F130), H137 (= H131), D221 (= D215), V223 (= V217), Q224 (= Q218), K250 (= K244)
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)
42% identity, 96% coverage: 6:384/396 of query aligns to 17:397/405 of P40732
- GT 108:109 (≠ GA 97:98) binding pyridoxal 5'-phosphate
- K255 (= K244) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T273) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
42% identity, 96% coverage: 6:384/396 of query aligns to 12:392/402 of 4jevB
- active site: F136 (= F130), E188 (= E182), D221 (= D215), Q224 (= Q218), K250 (= K244), T279 (= T273), R372 (= R364)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I40), S102 (= S96), G103 (= G97), T104 (≠ A98), F136 (= F130), H137 (= H131), E188 (= E182), E193 (= E187), D221 (= D215), V223 (= V217), Q224 (= Q218), K250 (= K244), R372 (= R364)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
42% identity, 96% coverage: 6:384/396 of query aligns to 12:387/397 of 4jewA
- active site: F136 (= F130), E188 (= E182), D221 (= D215), Q224 (= Q218), K250 (= K244), T274 (= T273), R367 (= R364)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G97), T104 (≠ A98), F136 (= F130), H137 (= H131), R139 (= R133), E188 (= E182), E193 (= E187), D221 (= D215), V223 (= V217), K250 (= K244)
- binding picric acid: K25 (≠ E19), K27 (≠ D21), W32 (≠ I26)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
42% identity, 96% coverage: 6:384/396 of query aligns to 6:381/389 of 2pb0A
- active site: F130 (= F130), E182 (= E182), D215 (= D215), Q218 (= Q218), K244 (= K244), T268 (= T273), R361 (= R364)
- binding pyridoxal-5'-phosphate: S96 (= S96), G97 (= G97), T98 (≠ A98), F130 (= F130), H131 (= H131), E182 (= E182), D215 (= D215), V217 (= V217), Q218 (= Q218), K244 (= K244)
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)
42% identity, 96% coverage: 6:384/396 of query aligns to 69:450/457 of Q9M8M7