SitesBLAST
Comparing WP_011388902.1 NCBI__GCF_000013085.1:WP_011388902.1 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)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
44% identity, 95% coverage: 1:376/394 of query aligns to 8:385/402 of 4jevB
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T279 (= T272), R372 (= R363)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I39), S102 (= S95), G103 (= G96), T104 (≠ A97), F136 (= F129), H137 (= H130), E188 (= E181), E193 (= E186), D221 (= D214), V223 (≠ I216), Q224 (= Q217), K250 (= K243), R372 (= R363)
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)
44% identity, 95% coverage: 1:376/394 of query aligns to 13:390/405 of P40732
- GT 108:109 (≠ GA 96:97) binding pyridoxal 5'-phosphate
- K255 (= K243) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T272) binding pyridoxal 5'-phosphate
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
42% identity, 98% coverage: 5:389/394 of query aligns to 3:385/385 of Q9X2A5
- GT 94:95 (≠ GA 96:97) binding pyridoxal 5'-phosphate
- T268 (= T272) 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, 98% coverage: 5:389/394 of query aligns to 11:393/393 of 2ordA
- active site: F134 (= F129), E186 (= E181), D219 (= D214), Q222 (= Q217), K248 (= K243), T276 (= T272), R367 (= R363)
- binding pyridoxal-5'-phosphate: G102 (= G96), T103 (≠ A97), F134 (= F129), H135 (= H130), E186 (= E181), D219 (= D214), V221 (≠ I216), Q222 (= Q217), K248 (= K243)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
43% identity, 95% coverage: 1:376/394 of query aligns to 8:380/397 of 4jewA
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T274 (= T272), R367 (= R363)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G96), T104 (≠ A97), F136 (= F129), H137 (= H130), R139 (= R132), E188 (= E181), E193 (= E186), D221 (= D214), V223 (≠ I216), K250 (= K243)
- binding picric acid: K25 (≠ H18), K27 (≠ E20), W32 (≠ V25)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
43% identity, 95% coverage: 1:376/394 of query aligns to 2:374/389 of 2pb0A
- active site: F130 (= F129), E182 (= E181), D215 (= D214), Q218 (= Q217), K244 (= K243), T268 (= T272), R361 (= R363)
- binding pyridoxal-5'-phosphate: S96 (= S95), G97 (= G96), T98 (≠ A97), F130 (= F129), H131 (= H130), E182 (= E181), D215 (= D214), V217 (≠ I216), Q218 (= Q217), K244 (= K243)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
42% identity, 97% coverage: 1:383/394 of query aligns to 8:396/400 of 4addA
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T279 (= T272), R372 (= R363)
- binding pyridoxal-5'-phosphate: G103 (= G96), A104 (= A97), F136 (= F129), H137 (= H130), D221 (= D214), V223 (≠ I216), K250 (= K243)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ F9), F136 (= F129), R139 (= R132)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
42% identity, 97% coverage: 1:383/394 of query aligns to 8:396/401 of 4adbB
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T279 (= T272), R372 (= R363)
- binding pyridoxal-5'-phosphate: S102 (= S95), G103 (= G96), A104 (= A97), F136 (= F129), H137 (= H130), D221 (= D214), V223 (≠ I216), Q224 (= Q217), K250 (= K243)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
43% identity, 94% coverage: 19:389/394 of query aligns to 49:428/429 of P73133
- S125 (= S95) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G96) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A97) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R132) 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 (= E186) 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 (= D214) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q217) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K243) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T272) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R363) 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.
Sites not aligning to the query:
- 39 Y→F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
41% identity, 94% coverage: 5:375/394 of query aligns to 4:365/376 of O66442
- GT 96:97 (≠ GA 96:97) binding pyridoxal 5'-phosphate
- K242 (= K243) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T272) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
41% identity, 94% coverage: 5:375/394 of query aligns to 3:364/375 of 2eh6A
- active site: F127 (= F129), E179 (= E181), D212 (= D214), Q215 (= Q217), K241 (= K243), T270 (= T272), R352 (= R363)
- binding pyridoxal-5'-phosphate: G95 (= G96), T96 (≠ A97), F127 (= F129), H128 (= H130), E179 (= E181), D212 (= D214), V214 (≠ I216), K241 (= K243)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
43% identity, 97% coverage: 5:387/394 of query aligns to 10:390/390 of 8ht4B