SitesBLAST
Comparing 7023380 Shewana3_0610 bifunctional N-succinyldiaminopimelate-aminotransferase/acetylornithine transaminase protein (RefSeq) 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)
62% identity, 98% coverage: 7:404/405 of query aligns to 8:405/405 of P40732
- GT 108:109 (≠ GA 107:108) binding
- K255 (= K254) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T283) binding
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
62% identity, 98% coverage: 7:404/405 of query aligns to 3:400/402 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), N107 (= N111), F136 (= F140), H137 (= H141), G138 (= G142), E188 (= E192), E193 (= E197), D221 (= D225), V223 (= V227), Q224 (= Q228), K250 (= K254), S278 (= S282), T279 (= T283), R372 (= R376)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
61% identity, 98% coverage: 7:404/405 of query aligns to 3:395/397 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: I46 (= I50), S102 (= S106), G103 (= G107), T104 (≠ A108), N107 (= N111), F136 (= F140), H137 (= H141), G138 (= G142), R139 (= R143), E188 (= E192), E193 (= E197), D221 (= D225), V223 (= V227), Q224 (= Q228), K250 (= K254)
- binding picric acid: K25 (≠ R29), K27 (≠ E31), W32 (= W36), G36 (= G40), E38 (= E42)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
61% identity, 97% coverage: 12:404/405 of query aligns to 2:389/389 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), N101 (= N111), F130 (= F140), H131 (= H141), G132 (= G142), E182 (= E192), D215 (= D225), V217 (= V227), Q218 (= Q228), K244 (= K254)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
59% identity, 97% coverage: 7:399/405 of query aligns to 3:395/401 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), N107 (= N111), F136 (= F140), H137 (= H141), G138 (= G142), E188 (= E192), D221 (= D225), V223 (= V227), Q224 (= Q228), K250 (= K254), T278 (≠ S282), T279 (= T283)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
59% identity, 97% coverage: 7:399/405 of query aligns to 3:395/400 of 4addA
- 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), N107 (= N111), F136 (= F140), H137 (= H141), G138 (= G142), E188 (= E192), D221 (= D225), V223 (= V227), Q224 (= Q228), K250 (= K254), T278 (≠ S282), T279 (= T283)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y20), I46 (= I50), G75 (≠ V79), F136 (= F140), R139 (= R143), E193 (= E197), K250 (= K254), G277 (= G281), T278 (≠ S282), T279 (= T283)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
41% identity, 93% coverage: 28:402/405 of query aligns to 15:385/385 of Q9X2A5
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
41% identity, 93% coverage: 28:402/405 of query aligns to 23:393/393 of 2ordA
- active site: F134 (= F140), E186 (= E192), D219 (= D225), Q222 (= Q228), K248 (= K254), T276 (= T283), R367 (= R376)
- binding pyridoxal-5'-phosphate: T101 (≠ S106), G102 (= G107), T103 (≠ A108), N106 (= N111), F134 (= F140), H135 (= H141), G136 (= G142), E186 (= E192), E191 (= E197), D219 (= D225), V221 (= V227), Q222 (= Q228), K248 (= K254), T275 (≠ S282), T276 (= T283)
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
42% identity, 94% coverage: 9:388/405 of query aligns to 4:372/390 of A0QYS9
- K304 (≠ Q315) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
40% identity, 93% coverage: 16:393/405 of query aligns to 4:370/376 of O66442
- GT 96:97 (≠ GA 107:108) binding
- K242 (= K254) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T283) binding
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
40% identity, 93% coverage: 16:393/405 of query aligns to 3:369/375 of 2eh6A
- active site: F127 (= F140), E179 (= E192), D212 (= D225), Q215 (= Q228), K241 (= K254), T270 (= T283), R352 (= R376)
- binding pyridoxal-5'-phosphate: S94 (= S106), G95 (= G107), T96 (≠ A108), F127 (= F140), H128 (= H141), G129 (= G142), E179 (= E192), D212 (= D225), V214 (= V227), Q215 (= Q228), K241 (= K254), S269 (= S282), T270 (= T283), F271 (≠ Y284)
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, 95% coverage: 15:399/405 of query aligns to 68:446/457 of Q9M8M7