SitesBLAST
Comparing WP_034272173.1 NCBI__GCF_000504245.1:WP_034272173.1 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)
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
63% identity, 98% coverage: 1:384/393 of query aligns to 1:384/390 of A0QYS9
- K304 (= K304) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
60% identity, 97% coverage: 2:384/393 of query aligns to 10:394/400 of P9WPZ7
- K314 (= K304) 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
60% identity, 97% coverage: 2:384/393 of query aligns to 4:388/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
60% identity, 97% coverage: 2:384/393 of query aligns to 4:388/391 of 7nn4A
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
50% identity, 95% coverage: 5:379/393 of query aligns to 4:385/390 of 8ht4B
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
45% identity, 91% coverage: 11:367/393 of query aligns to 11:374/393 of 2ordA
- active site: F134 (= F129), E186 (= E181), D219 (= D214), Q222 (= Q217), K248 (= K243), T276 (= T272), R367 (= R360)
- binding pyridoxal-5'-phosphate: G102 (= G103), T103 (≠ A104), F134 (= F129), H135 (= H130), E186 (= E181), D219 (= D214), V221 (= V216), Q222 (= Q217), K248 (= K243)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
45% identity, 91% coverage: 11:367/393 of query aligns to 3:366/385 of Q9X2A5
- GT 94:95 (≠ GA 103:104) binding pyridoxal 5'-phosphate
- T268 (= T272) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
42% identity, 95% coverage: 11:383/393 of query aligns to 3:375/375 of 2eh6A
- active site: F127 (= F129), E179 (= E181), D212 (= D214), Q215 (= Q217), K241 (= K243), T270 (= T272), R352 (= R360)
- binding pyridoxal-5'-phosphate: G95 (= G103), T96 (≠ A104), F127 (= F129), H128 (= H130), E179 (= E181), D212 (= D214), V214 (= V216), K241 (= K243)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
42% identity, 95% coverage: 11:383/393 of query aligns to 4:376/376 of O66442
- GT 96:97 (≠ GA 103:104) binding pyridoxal 5'-phosphate
- K242 (= K243) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T272) binding pyridoxal 5'-phosphate
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
41% identity, 95% coverage: 11:383/393 of query aligns to 35:425/429 of P73133
- Y39 (= Y15) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S102) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G103) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A104) 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 (= R360) 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.
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
47% identity, 94% coverage: 15:383/393 of query aligns to 24:394/395 of Q5SHH5
- GT 113:114 (≠ GA 103:104) binding pyridoxal 5'-phosphate
- K254 (= K243) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T272) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
47% identity, 94% coverage: 15:383/393 of query aligns to 16:386/387 of 1wkhA
- active site: F132 (= F129), E184 (= E181), D217 (= D214), Q220 (= Q217), K246 (= K243), T275 (= T272), R363 (= R360)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I45), S104 (= S102), G105 (= G103), T106 (≠ A104), F132 (= F129), S133 (≠ H130), E184 (= E181), E189 (= E186), D217 (= D214), I219 (≠ V216), K246 (= K243), R363 (= R360)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
47% identity, 94% coverage: 15:383/393 of query aligns to 16:386/387 of 1wkgA