SitesBLAST
Comparing WP_090273343.1 NCBI__GCF_900105005.1:WP_090273343.1 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)
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)
59% identity, 100% coverage: 2:403/404 of query aligns to 3:404/405 of P40732
- GT 108:109 (≠ GA 107:108) binding pyridoxal 5'-phosphate
- K255 (= K254) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T283) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
59% identity, 98% coverage: 7:403/404 of query aligns to 3:399/402 of 4jevB
- active site: F136 (= F140), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T279 (= T283), R372 (= R376)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I50), S102 (= S106), G103 (= G107), T104 (≠ A108), F136 (= F140), H137 (= H141), E188 (= E192), E193 (= E197), D221 (= D225), V223 (= V227), Q224 (= Q228), K250 (= K254), R372 (= R376)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
59% identity, 98% coverage: 7:403/404 of query aligns to 3:394/397 of 4jewA
- active site: F136 (= F140), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T274 (= T283), R367 (= R376)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G107), T104 (≠ A108), F136 (= F140), H137 (= H141), R139 (= R143), E188 (= E192), E193 (= E197), D221 (= D225), V223 (= V227), K250 (= K254)
- binding picric acid: K25 (≠ R29), K27 (≠ D31), W32 (= W36)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
59% identity, 99% coverage: 7:404/404 of query aligns to 3:400/400 of 4addA
- active site: F136 (= F140), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T279 (= T283), R372 (= R376)
- binding pyridoxal-5'-phosphate: G103 (= G107), A104 (= A108), F136 (= F140), H137 (= H141), D221 (= D225), V223 (= V227), K250 (= K254)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y20), F136 (= F140), R139 (= R143)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
59% identity, 99% coverage: 7:404/404 of query aligns to 3:400/401 of 4adbB
- active site: F136 (= F140), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T279 (= T283), R372 (= R376)
- binding pyridoxal-5'-phosphate: S102 (= S106), G103 (= G107), A104 (= A108), F136 (= F140), H137 (= H141), D221 (= D225), V223 (= V227), Q224 (= Q228), K250 (= K254)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
59% identity, 97% coverage: 12:403/404 of query aligns to 2:388/389 of 2pb0A
- active site: F130 (= F140), E182 (= E192), D215 (= D225), Q218 (= Q228), K244 (= K254), T268 (= T283), R361 (= R376)
- binding pyridoxal-5'-phosphate: S96 (= S106), G97 (= G107), T98 (≠ A108), F130 (= F140), H131 (= H141), E182 (= E192), D215 (= D225), V217 (= V227), Q218 (= Q228), K244 (= K254)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
44% identity, 100% coverage: 1:403/404 of query aligns to 20:429/429 of P73133
- Y39 (= Y20) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S106) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G107) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A108) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R143) 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 (= E197) 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 (= D225) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q228) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K254) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T283) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R376) 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
43% identity, 95% coverage: 16:399/404 of query aligns to 11:390/393 of 2ordA
- active site: F134 (= F140), E186 (= E192), D219 (= D225), Q222 (= Q228), K248 (= K254), T276 (= T283), R367 (= R376)
- binding pyridoxal-5'-phosphate: G102 (= G107), T103 (≠ A108), F134 (= F140), H135 (= H141), E186 (= E192), D219 (= D225), V221 (= V227), Q222 (= Q228), K248 (= K254)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
43% identity, 95% coverage: 16:399/404 of query aligns to 3:382/385 of Q9X2A5
- GT 94:95 (≠ GA 107:108) binding pyridoxal 5'-phosphate
- T268 (= T283) 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)
42% identity, 96% coverage: 14:402/404 of query aligns to 67:456/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
43% identity, 95% coverage: 16:399/404 of query aligns to 4:376/376 of O66442
- GT 96:97 (≠ GA 107:108) binding pyridoxal 5'-phosphate
- K242 (= K254) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T283) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
43% identity, 95% coverage: 16:399/404 of query aligns to 3:375/375 of 2eh6A