SitesBLAST
Comparing WP_047216038.1 NCBI__GCF_001931675.1:WP_047216038.1 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)
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
44% identity, 96% coverage: 11:395/399 of query aligns to 11:390/393 of 2ordA
- active site: F134 (= F138), E186 (= E190), D219 (= D223), Q222 (= Q226), K248 (= K252), T276 (= T280), R367 (= R372)
- binding pyridoxal-5'-phosphate: G102 (= G102), T103 (≠ A103), F134 (= F138), H135 (= H139), E186 (= E190), D219 (= D223), V221 (= V225), Q222 (= Q226), K248 (= K252)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
44% identity, 96% coverage: 11:395/399 of query aligns to 3:382/385 of Q9X2A5
- GT 94:95 (≠ GA 102:103) binding pyridoxal 5'-phosphate
- T268 (= T280) binding pyridoxal 5'-phosphate
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
46% identity, 90% coverage: 25:384/399 of query aligns to 26:384/400 of 4addA
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T280), R372 (= R372)
- binding pyridoxal-5'-phosphate: G103 (= G102), A104 (= A103), F136 (= F138), H137 (= H139), D221 (= D223), V223 (= V225), K250 (= K252)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: F136 (= F138), R139 (= R141)
Sites not aligning to the query:
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
46% identity, 90% coverage: 25:384/399 of query aligns to 26:384/401 of 4adbB
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T280), R372 (= R372)
- binding pyridoxal-5'-phosphate: S102 (= S101), G103 (= G102), A104 (= A103), F136 (= F138), H137 (= H139), D221 (= D223), V223 (= V225), Q224 (= Q226), K250 (= K252)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
41% identity, 96% coverage: 11:395/399 of query aligns to 1:376/376 of O66442
- GT 96:97 (≠ GA 102:103) binding pyridoxal 5'-phosphate
- K242 (= K252) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T280) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
41% identity, 96% coverage: 11:395/399 of query aligns to 3:375/375 of 2eh6A
- active site: F127 (= F138), E179 (= E190), D212 (= D223), Q215 (= Q226), K241 (= K252), T270 (= T280), R352 (= R372)
- binding pyridoxal-5'-phosphate: G95 (= G102), T96 (≠ A103), F127 (= F138), H128 (= H139), E179 (= E190), D212 (= D223), V214 (= V225), K241 (= K252)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
40% identity, 97% coverage: 11:396/399 of query aligns to 35:426/429 of P73133
- Y39 (≠ T15) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S101) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G102) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A103) 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 (= T280) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R372) 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.
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
41% identity, 95% coverage: 17:395/399 of query aligns to 10:385/388 of 3nx3A
- active site: F127 (= F138), E179 (= E190), D212 (= D223), Q215 (= Q226), K241 (= K252), T271 (= T280), R362 (= R372)
- binding magnesium ion: N191 (≠ T202), F194 (= F205), I313 (≠ C322), F316 (≠ Y325), D317 (≠ G326), C319 (≠ E328), Q370 (≠ T380), K371 (≠ R381)
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, 94% coverage: 17:391/399 of query aligns to 75:449/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
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)
38% identity, 94% coverage: 25:398/399 of query aligns to 31:403/405 of P40732
- GT 108:109 (≠ GA 102:103) binding pyridoxal 5'-phosphate
- K255 (= K252) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T280) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
38% identity, 94% coverage: 25:398/399 of query aligns to 26:398/402 of 4jevB
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T280), R372 (= R372)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (≠ W45), S102 (= S101), G103 (= G102), T104 (≠ A103), F136 (= F138), H137 (= H139), E188 (= E190), E193 (= E195), D221 (= D223), V223 (= V225), Q224 (= Q226), K250 (= K252), R372 (= R372)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
37% identity, 94% coverage: 25:398/399 of query aligns to 26:393/397 of 4jewA