SitesBLAST
Comparing WP_043529620.1 NCBI__GCF_000759345.1:WP_043529620.1 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)
63% identity, 98% coverage: 6:401/404 of query aligns to 9:404/405 of P40732
- GT 108:109 (≠ GG 105:106) binding pyridoxal 5'-phosphate
- K255 (= K252) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T281) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
62% identity, 98% coverage: 6:401/404 of query aligns to 4:399/402 of 4jevB
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T281), R372 (= R374)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I48), S102 (= S104), G103 (= G105), T104 (≠ G106), F136 (= F138), H137 (= H139), E188 (= E190), E193 (= E195), D221 (= D223), V223 (= V225), Q224 (= Q226), K250 (= K252), R372 (= R374)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
60% identity, 99% coverage: 6:403/404 of query aligns to 4:401/401 of 4adbB
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T281), R372 (= R374)
- binding pyridoxal-5'-phosphate: S102 (= S104), G103 (= G105), A104 (≠ G106), F136 (= F138), H137 (= H139), D221 (= D223), V223 (= V225), Q224 (= Q226), K250 (= K252)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
61% identity, 98% coverage: 6:401/404 of query aligns to 4:399/400 of 4addA
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T281), R372 (= R374)
- binding pyridoxal-5'-phosphate: G103 (= G105), A104 (≠ G106), F136 (= F138), H137 (= H139), D221 (= D223), V223 (= V225), K250 (= K252)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y18), F136 (= F138), R139 (= R141)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
62% identity, 98% coverage: 6:401/404 of query aligns to 4:394/397 of 4jewA
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T274 (= T281), R367 (= R374)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G105), T104 (≠ G106), F136 (= F138), H137 (= H139), R139 (= R141), E188 (= E190), E193 (= E195), D221 (= D223), V223 (= V225), K250 (= K252)
- binding picric acid: K25 (≠ R27), K27 (= K29), W32 (= W34)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
62% identity, 97% coverage: 10:401/404 of query aligns to 2:388/389 of 2pb0A
- active site: F130 (= F138), E182 (= E190), D215 (= D223), Q218 (= Q226), K244 (= K252), T268 (= T281), R361 (= R374)
- binding pyridoxal-5'-phosphate: S96 (= S104), G97 (= G105), T98 (≠ G106), F130 (= F138), H131 (= H139), E182 (= E190), D215 (= D223), V217 (= V225), Q218 (= Q226), K244 (= K252)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
44% identity, 98% coverage: 8:401/404 of query aligns to 29:429/429 of P73133
- Y39 (= Y18) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S104) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G105) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (≠ G106) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R141) 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 (= E195) 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 (= D223) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q226) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K252) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T281) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R374) 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)
42% identity, 95% coverage: 13:397/404 of query aligns to 2:382/385 of Q9X2A5
- GT 94:95 (≠ GG 105:106) binding pyridoxal 5'-phosphate
- T268 (= T281) 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
42% identity, 95% coverage: 13:397/404 of query aligns to 10:390/393 of 2ordA
- active site: F134 (= F138), E186 (= E190), D219 (= D223), Q222 (= Q226), K248 (= K252), T276 (= T281), R367 (= R374)
- binding pyridoxal-5'-phosphate: G102 (= G105), T103 (≠ G106), F134 (= F138), H135 (= H139), E186 (= E190), D219 (= D223), V221 (= V225), Q222 (= Q226), K248 (= K252)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
44% identity, 94% coverage: 13:393/404 of query aligns to 3:372/376 of O66442
- GT 96:97 (≠ GG 105:106) binding pyridoxal 5'-phosphate
- K242 (= K252) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T281) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
44% identity, 94% coverage: 13:393/404 of query aligns to 2:371/375 of 2eh6A
- active site: F127 (= F138), E179 (= E190), D212 (= D223), Q215 (= Q226), K241 (= K252), T270 (= T281), R352 (= R374)
- binding pyridoxal-5'-phosphate: G95 (= G105), T96 (≠ G106), F127 (= F138), H128 (= H139), E179 (= E190), D212 (= D223), V214 (= V225), K241 (= K252)
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)
41% identity, 95% coverage: 17:400/404 of query aligns to 72:456/457 of Q9M8M7