SitesBLAST
Comparing WP_008507916.1 NCBI__GCF_000182725.1:WP_008507916.1 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)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
43% identity, 95% coverage: 12:393/403 of query aligns to 37:428/429 of P73133
- Y39 (= Y14) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S100) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G101) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A102) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R137) 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 (= E191) 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 (= D219) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q222) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K248) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T277) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R367) 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.
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
43% identity, 95% coverage: 10:393/403 of query aligns to 3:371/375 of 2eh6A
- active site: F127 (= F134), E179 (= E186), D212 (= D219), Q215 (= Q222), K241 (= K248), T270 (= T277), R352 (= R367)
- binding pyridoxal-5'-phosphate: G95 (= G101), T96 (≠ A102), F127 (= F134), H128 (= H135), E179 (= E186), D212 (= D219), V214 (= V221), K241 (= K248)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
43% identity, 95% coverage: 10:393/403 of query aligns to 4:372/376 of O66442
- GT 96:97 (≠ GA 101:102) binding pyridoxal 5'-phosphate
- K242 (= K248) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T277) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
41% identity, 98% coverage: 1:393/403 of query aligns to 3:398/402 of 4jevB
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T277), R372 (= R367)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I44), S102 (= S100), G103 (= G101), T104 (≠ A102), F136 (= F134), H137 (= H135), E188 (= E186), E193 (= E191), D221 (= D219), V223 (= V221), Q224 (= Q222), K250 (= K248), R372 (= R367)
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)
41% identity, 98% coverage: 1:393/403 of query aligns to 8:403/405 of P40732
- GT 108:109 (≠ GA 101:102) binding pyridoxal 5'-phosphate
- K255 (= K248) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T277) binding pyridoxal 5'-phosphate
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
41% identity, 98% coverage: 1:393/403 of query aligns to 3:393/397 of 4jewA
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T274 (= T277), R367 (= R367)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G101), T104 (≠ A102), F136 (= F134), H137 (= H135), R139 (= R137), E188 (= E186), E193 (= E191), D221 (= D219), V223 (= V221), K250 (= K248)
- binding picric acid: K25 (≠ R23), K27 (≠ E25), W32 (≠ I30)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
42% identity, 92% coverage: 23:393/403 of query aligns to 19:387/389 of 2pb0A
- active site: F130 (= F134), E182 (= E186), D215 (= D219), Q218 (= Q222), K244 (= K248), T268 (= T277), R361 (= R367)
- binding pyridoxal-5'-phosphate: S96 (= S100), G97 (= G101), T98 (≠ A102), F130 (= F134), H131 (= H135), E182 (= E186), D215 (= D219), V217 (= V221), Q218 (= Q222), K244 (= K248)
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
43% identity, 94% coverage: 10:386/403 of query aligns to 11:389/393 of 2ordA
- active site: F134 (= F134), E186 (= E186), D219 (= D219), Q222 (= Q222), K248 (= K248), T276 (= T277), R367 (= R367)
- binding pyridoxal-5'-phosphate: G102 (= G101), T103 (≠ A102), F134 (= F134), H135 (= H135), E186 (= E186), D219 (= D219), V221 (= V221), Q222 (= Q222), K248 (= K248)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
43% identity, 94% coverage: 10:386/403 of query aligns to 3:381/385 of Q9X2A5
- GT 94:95 (≠ GA 101:102) binding pyridoxal 5'-phosphate
- T268 (= T277) binding pyridoxal 5'-phosphate
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
43% identity, 92% coverage: 23:393/403 of query aligns to 25:398/401 of 4adbB
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T277), R372 (= R367)
- binding pyridoxal-5'-phosphate: S102 (= S100), G103 (= G101), A104 (= A102), F136 (= F134), H137 (= H135), D221 (= D219), V223 (= V221), Q224 (= Q222), K250 (= K248)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
43% identity, 92% coverage: 23:393/403 of query aligns to 25:398/400 of 4addA
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T277), R372 (= R367)
- binding pyridoxal-5'-phosphate: G103 (= G101), A104 (= A102), F136 (= F134), H137 (= H135), D221 (= D219), V223 (= V221), K250 (= K248)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: F136 (= F134), R139 (= R137)
Sites not aligning to the query:
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
43% identity, 94% coverage: 10:386/403 of query aligns to 10:385/390 of 8ht4B