SitesBLAST
Comparing PP_0372 FitnessBrowser__Putida:PP_0372 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)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
41% identity, 86% coverage: 35:401/426 of query aligns to 3:372/385 of Q9X2A5
- GT 94:95 (≠ GA 126:127) binding pyridoxal 5'-phosphate
- T268 (≠ S299) 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
41% identity, 86% coverage: 35:401/426 of query aligns to 11:380/393 of 2ordA
- active site: F134 (≠ C158), E186 (= E209), D219 (= D242), Q222 (= Q245), K248 (= K271), T276 (≠ S299), R367 (= R388)
- binding pyridoxal-5'-phosphate: G102 (= G126), T103 (≠ A127), F134 (≠ C158), H135 (= H159), E186 (= E209), D219 (= D242), V221 (= V244), Q222 (= Q245), K248 (= K271)
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
39% identity, 86% coverage: 35:401/426 of query aligns to 3:365/375 of 2eh6A
- active site: F127 (≠ C158), E179 (= E209), D212 (= D242), Q215 (= Q245), K241 (= K271), T270 (≠ S299), R352 (= R388)
- binding pyridoxal-5'-phosphate: G95 (= G126), T96 (≠ A127), F127 (≠ C158), H128 (= H159), E179 (= E209), D212 (= D242), V214 (= V244), K241 (= K271)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
39% identity, 86% coverage: 35:401/426 of query aligns to 4:366/376 of O66442
- GT 96:97 (≠ GA 126:127) binding pyridoxal 5'-phosphate
- K242 (= K271) modified: N6-(pyridoxal phosphate)lysine
- T271 (≠ S299) binding pyridoxal 5'-phosphate
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
40% identity, 86% coverage: 48:414/426 of query aligns to 48:428/429 of P73133
- S125 (= S125) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G126) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A127) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R161) 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 (= E214) 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 (= D242) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q245) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K271) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (≠ S299) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R388) 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.
Sites not aligning to the query:
- 39 Y→F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
38% identity, 91% coverage: 25:410/426 of query aligns to 2:394/401 of 4adbB
- active site: F136 (≠ C158), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (≠ S299), R372 (= R388)
- binding pyridoxal-5'-phosphate: S102 (= S125), G103 (= G126), A104 (= A127), F136 (≠ C158), H137 (= H159), D221 (= D242), V223 (= V244), Q224 (= Q245), K250 (= K271)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
38% identity, 91% coverage: 25:410/426 of query aligns to 2:394/400 of 4addA
- active site: F136 (≠ C158), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (≠ S299), R372 (= R388)
- binding pyridoxal-5'-phosphate: G103 (= G126), A104 (= A127), F136 (≠ C158), H137 (= H159), D221 (= D242), V223 (= V244), K250 (= K271)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ T39), F136 (≠ C158), R139 (= R161)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
37% identity, 90% coverage: 33:414/426 of query aligns to 10:398/402 of 4jevB
- active site: F136 (≠ C158), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (≠ S299), R372 (= R388)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (≠ G69), S102 (= S125), G103 (= G126), T104 (≠ A127), F136 (≠ C158), H137 (= H159), E188 (= E209), E193 (= E214), D221 (= D242), V223 (= V244), Q224 (= Q245), K250 (= K271), R372 (= R388)
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)
37% identity, 90% coverage: 33:414/426 of query aligns to 15:403/405 of P40732
- GT 108:109 (≠ GA 126:127) binding pyridoxal 5'-phosphate
- K255 (= K271) modified: N6-(pyridoxal phosphate)lysine
- T284 (≠ S299) binding pyridoxal 5'-phosphate
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
37% identity, 90% coverage: 33:416/426 of query aligns to 10:395/397 of 4jewA
- active site: F136 (≠ C158), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T274 (≠ S299), R367 (= R388)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G126), T104 (≠ A127), F136 (≠ C158), H137 (= H159), R139 (= R161), E188 (= E209), E193 (= E214), D221 (= D242), V223 (= V244), K250 (= K271)
- binding picric acid: K25 (≠ R48), K27 (≠ Q50), W32 (= W55)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
37% identity, 90% coverage: 33:416/426 of query aligns to 4:389/389 of 2pb0A
- active site: F130 (≠ C158), E182 (= E209), D215 (= D242), Q218 (= Q245), K244 (= K271), T268 (≠ S299), R361 (= R388)
- binding pyridoxal-5'-phosphate: S96 (= S125), G97 (= G126), T98 (≠ A127), F130 (≠ C158), H131 (= H159), E182 (= E209), D215 (= D242), V217 (= V244), Q218 (= Q245), K244 (= K271)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
36% identity, 86% coverage: 46:412/426 of query aligns to 21:390/390 of 8ht4B