SitesBLAST
Comparing WP_027489558.1 NCBI__GCF_021560695.1:WP_027489558.1 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)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
48% identity, 97% coverage: 14:407/408 of query aligns to 10:400/400 of 4addA
- active site: F136 (= F142), E188 (= E195), D221 (= D228), Q224 (= Q231), K250 (= K257), T279 (= T286), R372 (= R379)
- binding pyridoxal-5'-phosphate: G103 (= G108), A104 (= A109), F136 (= F142), H137 (= H143), D221 (= D228), V223 (≠ I230), K250 (= K257)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y20), F136 (= F142), R139 (= R145)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
49% identity, 96% coverage: 15:407/408 of query aligns to 11:400/401 of 4adbB
- active site: F136 (= F142), E188 (= E195), D221 (= D228), Q224 (= Q231), K250 (= K257), T279 (= T286), R372 (= R379)
- binding pyridoxal-5'-phosphate: S102 (= S107), G103 (= G108), A104 (= A109), F136 (= F142), H137 (= H143), D221 (= D228), V223 (≠ I230), Q224 (= Q231), K250 (= K257)
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)
47% identity, 96% coverage: 17:407/408 of query aligns to 18:405/405 of P40732
- GT 108:109 (≠ GA 108:109) binding pyridoxal 5'-phosphate
- K255 (= K257) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T286) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
47% identity, 96% coverage: 17:407/408 of query aligns to 13:400/402 of 4jevB
- active site: F136 (= F142), E188 (= E195), D221 (= D228), Q224 (= Q231), K250 (= K257), T279 (= T286), R372 (= R379)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I50), S102 (= S107), G103 (= G108), T104 (≠ A109), F136 (= F142), H137 (= H143), E188 (= E195), E193 (= E200), D221 (= D228), V223 (≠ I230), Q224 (= Q231), K250 (= K257), R372 (= R379)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
47% identity, 96% coverage: 17:407/408 of query aligns to 7:389/389 of 2pb0A
- active site: F130 (= F142), E182 (= E195), D215 (= D228), Q218 (= Q231), K244 (= K257), T268 (= T286), R361 (= R379)
- binding pyridoxal-5'-phosphate: S96 (= S107), G97 (= G108), T98 (≠ A109), F130 (= F142), H131 (= H143), E182 (= E195), D215 (= D228), V217 (≠ I230), Q218 (= Q231), K244 (= K257)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
47% identity, 96% coverage: 17:407/408 of query aligns to 13:395/397 of 4jewA
- active site: F136 (= F142), E188 (= E195), D221 (= D228), Q224 (= Q231), K250 (= K257), T274 (= T286), R367 (= R379)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G108), T104 (≠ A109), F136 (= F142), H137 (= H143), R139 (= R145), E188 (= E195), E193 (= E200), D221 (= D228), V223 (≠ I230), K250 (= K257)
- binding picric acid: K25 (≠ H29), K27 (= K31), W32 (= W36)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
48% identity, 95% coverage: 15:403/408 of query aligns to 34:426/429 of P73133
- Y39 (= Y20) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S107) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G108) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A109) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R145) 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 (= E200) 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 (= D228) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q231) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K257) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T286) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R379) 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.
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
44% identity, 95% coverage: 15:403/408 of query aligns to 10:391/393 of 2ordA
- active site: F134 (= F142), E186 (= E195), D219 (= D228), Q222 (= Q231), K248 (= K257), T276 (= T286), R367 (= R379)
- binding pyridoxal-5'-phosphate: G102 (= G108), T103 (≠ A109), F134 (= F142), H135 (= H143), E186 (= E195), D219 (= D228), V221 (≠ I230), Q222 (= Q231), K248 (= K257)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
44% identity, 95% coverage: 15:403/408 of query aligns to 2:383/385 of Q9X2A5
- GT 94:95 (≠ GA 108:109) binding pyridoxal 5'-phosphate
- T268 (= T286) binding pyridoxal 5'-phosphate
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: 8:391/408 of query aligns to 61:442/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
45% identity, 92% coverage: 22:395/408 of query aligns to 18:382/390 of 8ht4B
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
42% identity, 95% coverage: 20:406/408 of query aligns to 15:387/390 of A0QYS9