SitesBLAST
Comparing WP_110806203.1 NCBI__GCF_003217355.1:WP_110806203.1 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)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
44% identity, 97% coverage: 5:384/393 of query aligns to 12:394/400 of 4addA
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T279 (= T272), R372 (= R362)
- binding pyridoxal-5'-phosphate: G103 (= G96), A104 (≠ T97), F136 (= F129), H137 (= H130), D221 (= D214), V223 (= V216), K250 (= K243)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y9), F136 (= F129), R139 (= R132)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
44% identity, 97% coverage: 5:384/393 of query aligns to 12:394/401 of 4adbB
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T279 (= T272), R372 (= R362)
- binding pyridoxal-5'-phosphate: S102 (= S95), G103 (= G96), A104 (≠ T97), F136 (= F129), H137 (= H130), D221 (= D214), V223 (= V216), Q224 (= Q217), K250 (= K243)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
45% identity, 98% coverage: 5:388/393 of query aligns to 35:428/429 of P73133
- Y39 (= Y9) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S95) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G96) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (≠ T97) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R132) 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 (= E186) 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 (= D214) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q217) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K243) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T272) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R362) 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.
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: 5:382/393 of query aligns to 3:379/385 of Q9X2A5
- GT 94:95 (= GT 96:97) binding pyridoxal 5'-phosphate
- T268 (= T272) 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: 5:382/393 of query aligns to 11:387/393 of 2ordA
- active site: F134 (= F129), E186 (= E181), D219 (= D214), Q222 (= Q217), K248 (= K243), T276 (= T272), R367 (= R362)
- binding pyridoxal-5'-phosphate: G102 (= G96), T103 (= T97), F134 (= F129), H135 (= H130), E186 (= E181), D219 (= D214), V221 (= V216), Q222 (= Q217), K248 (= K243)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
43% identity, 97% coverage: 5:384/393 of query aligns to 12:394/402 of 4jevB
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T279 (= T272), R372 (= R362)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I39), S102 (= S95), G103 (= G96), T104 (= T97), F136 (= F129), H137 (= H130), E188 (= E181), E193 (= E186), D221 (= D214), V223 (= V216), Q224 (= Q217), K250 (= K243), R372 (= R362)
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, 98% coverage: 5:389/393 of query aligns to 69:457/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
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)
43% identity, 97% coverage: 5:384/393 of query aligns to 17:399/405 of P40732
- GT 108:109 (= GT 96:97) binding pyridoxal 5'-phosphate
- K255 (= K243) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T272) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
43% identity, 96% coverage: 5:381/393 of query aligns to 3:371/375 of 2eh6A
- active site: F127 (= F129), E179 (= E181), D212 (= D214), Q215 (= Q217), K241 (= K243), T270 (= T272), R352 (= R362)
- binding pyridoxal-5'-phosphate: G95 (= G96), T96 (= T97), F127 (= F129), H128 (= H130), E179 (= E181), D212 (= D214), V214 (= V216), K241 (= K243)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
43% identity, 97% coverage: 2:381/393 of query aligns to 1:372/376 of O66442
- GT 96:97 (= GT 96:97) binding pyridoxal 5'-phosphate
- K242 (= K243) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T272) binding pyridoxal 5'-phosphate
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
42% identity, 97% coverage: 5:384/393 of query aligns to 12:389/397 of 4jewA
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T274 (= T272), R367 (= R362)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G96), T104 (= T97), F136 (= F129), H137 (= H130), R139 (= R132), E188 (= E181), E193 (= E186), D221 (= D214), V223 (= V216), K250 (= K243)
- binding picric acid: K25 (≠ R18), K27 (≠ E20), W32 (= W25)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
42% identity, 97% coverage: 5:384/393 of query aligns to 6:383/389 of 2pb0A