SitesBLAST
Comparing WP_053937056.1 NCBI__GCF_001294205.1:WP_053937056.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
60% identity, 99% coverage: 4:400/400 of query aligns to 9:405/405 of P40732
- GT 108:109 (≠ GA 103:104) binding pyridoxal 5'-phosphate
- K255 (= K250) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T279) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
59% identity, 99% coverage: 4:400/400 of query aligns to 4:400/402 of 4jevB
- active site: F136 (= F136), E188 (= E188), D221 (= D221), Q224 (= Q224), K250 (= K250), T279 (= T279), R372 (= R372)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I46), S102 (= S102), G103 (= G103), T104 (≠ A104), F136 (= F136), H137 (= H137), E188 (= E188), E193 (= E193), D221 (= D221), V223 (= V223), Q224 (= Q224), K250 (= K250), R372 (= R372)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
59% identity, 100% coverage: 1:400/400 of query aligns to 1:400/400 of 4addA
- active site: F136 (= F136), E188 (= E188), D221 (= D221), Q224 (= Q224), K250 (= K250), T279 (= T279), R372 (= R372)
- binding pyridoxal-5'-phosphate: G103 (= G103), A104 (= A104), F136 (= F136), H137 (= H137), D221 (= D221), V223 (= V223), K250 (= K250)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y16), F136 (= F136), R139 (= R139)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
59% identity, 100% coverage: 1:400/400 of query aligns to 1:400/401 of 4adbB
- active site: F136 (= F136), E188 (= E188), D221 (= D221), Q224 (= Q224), K250 (= K250), T279 (= T279), R372 (= R372)
- binding pyridoxal-5'-phosphate: S102 (= S102), G103 (= G103), A104 (= A104), F136 (= F136), H137 (= H137), D221 (= D221), V223 (= V223), Q224 (= Q224), K250 (= K250)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
59% identity, 99% coverage: 4:400/400 of query aligns to 4:395/397 of 4jewA
- active site: F136 (= F136), E188 (= E188), D221 (= D221), Q224 (= Q224), K250 (= K250), T274 (= T279), R367 (= R372)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G103), T104 (≠ A104), F136 (= F136), H137 (= H137), R139 (= R139), E188 (= E188), E193 (= E193), D221 (= D221), V223 (= V223), K250 (= K250)
- binding picric acid: K25 (≠ R25), K27 (≠ A27), W32 (= W32)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
59% identity, 98% coverage: 8:400/400 of query aligns to 2:389/389 of 2pb0A
- active site: F130 (= F136), E182 (= E188), D215 (= D221), Q218 (= Q224), K244 (= K250), T268 (= T279), R361 (= R372)
- binding pyridoxal-5'-phosphate: S96 (= S102), G97 (= G103), T98 (≠ A104), F130 (= F136), H131 (= H137), E182 (= E188), D215 (= D221), V217 (= V223), Q218 (= Q224), K244 (= K250)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
47% identity, 96% coverage: 11:395/400 of query aligns to 2:382/385 of Q9X2A5
- GT 94:95 (≠ GA 103:104) binding pyridoxal 5'-phosphate
- T268 (= T279) 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
47% identity, 96% coverage: 11:395/400 of query aligns to 10:390/393 of 2ordA
- active site: F134 (= F136), E186 (= E188), D219 (= D221), Q222 (= Q224), K248 (= K250), T276 (= T279), R367 (= R372)
- binding pyridoxal-5'-phosphate: G102 (= G103), T103 (≠ A104), F134 (= F136), H135 (= H137), E186 (= E188), D219 (= D221), V221 (= V223), Q222 (= Q224), K248 (= K250)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
44% identity, 99% coverage: 3:399/400 of query aligns to 26:429/429 of P73133
- Y39 (= Y16) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S102) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G103) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A104) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R139) 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 (= E193) 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 (= D221) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q224) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K250) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T279) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R372) 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.
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
44% identity, 95% coverage: 11:389/400 of query aligns to 3:370/376 of O66442
- GT 96:97 (≠ GA 103:104) binding pyridoxal 5'-phosphate
- K242 (= K250) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T279) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
44% identity, 95% coverage: 11:389/400 of query aligns to 2:369/375 of 2eh6A
- active site: F127 (= F136), E179 (= E188), D212 (= D221), Q215 (= Q224), K241 (= K250), T270 (= T279), R352 (= R372)
- binding pyridoxal-5'-phosphate: G95 (= G103), T96 (≠ A104), F127 (= F136), H128 (= H137), E179 (= E188), D212 (= D221), V214 (= V223), K241 (= K250)
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, 94% coverage: 10:385/400 of query aligns to 67:443/457 of Q9M8M7