SitesBLAST
Comparing 207835 MicrobesOnline__882:207835 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)
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
39% identity, 96% coverage: 14:396/399 of query aligns to 1:375/375 of 2eh6A
- active site: F127 (= F140), E179 (= E192), D212 (= D225), Q215 (= Q228), K241 (= K254), T270 (= T283), R352 (= R373)
- binding pyridoxal-5'-phosphate: G95 (= G107), T96 (≠ A108), F127 (= F140), H128 (= H141), E179 (= E192), D212 (= D225), V214 (≠ I227), K241 (= K254)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
39% identity, 96% coverage: 14:396/399 of query aligns to 2:376/376 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
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
41% identity, 97% coverage: 13:398/399 of query aligns to 9:401/401 of 4adbB
- active site: F136 (= F140), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T279 (= T283), R372 (= R373)
- binding pyridoxal-5'-phosphate: S102 (= S106), G103 (= G107), A104 (= A108), F136 (= F140), H137 (= H141), D221 (= D225), V223 (≠ I227), Q224 (= Q228), K250 (= K254)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
40% identity, 96% coverage: 13:397/399 of query aligns to 32:426/429 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 (= R373) 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.
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
41% identity, 95% coverage: 13:390/399 of query aligns to 9:389/400 of 4addA
- active site: F136 (= F140), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T279 (= T283), R372 (= R373)
- binding pyridoxal-5'-phosphate: G103 (= G107), A104 (= A108), F136 (= F140), H137 (= H141), D221 (= D225), V223 (≠ I227), K250 (= K254)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y20), F136 (= F140), R139 (= R143)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
40% identity, 89% coverage: 29:385/399 of query aligns to 25:384/402 of 4jevB
- active site: F136 (= F140), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T279 (= T283), R372 (= R373)
- 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 (≠ I227), Q224 (= Q228), K250 (= K254), R372 (= R373)
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)
40% identity, 89% coverage: 29:385/399 of query aligns to 30:389/405 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
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
41% identity, 99% coverage: 2:398/399 of query aligns to 5:395/400 of P9WPZ7
- K314 (≠ G315) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine; partial
7nncC Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal-5'-phosphate and 6-methoxyquinoline-3-carboxylic acid
42% identity, 98% coverage: 8:398/399 of query aligns to 5:389/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
42% identity, 98% coverage: 8:398/399 of query aligns to 5:389/391 of 7nn4A
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
39% identity, 89% coverage: 29:385/399 of query aligns to 25:379/397 of 4jewA
- active site: F136 (= F140), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T274 (= T283), R367 (= R373)
- 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 (≠ I227), K250 (= K254)
- binding picric acid: K25 (≠ R29), K27 (≠ E31), W32 (= W36)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
39% identity, 89% coverage: 29:385/399 of query aligns to 19:373/389 of 2pb0A