SitesBLAST
Comparing WP_109969430.1 NCBI__GCF_003173355.1:WP_109969430.1 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)
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
40% identity, 92% coverage: 20:385/400 of query aligns to 25:384/395 of Q5SHH5
- GT 113:114 (≠ GA 110:111) binding pyridoxal 5'-phosphate
- K254 (= K251) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T280) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
39% identity, 92% coverage: 20:385/400 of query aligns to 17:376/387 of 1wkhA
- active site: F132 (= F137), E184 (= E189), D217 (= D222), Q220 (= Q225), K246 (= K251), T275 (= T280), R363 (= R372)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ W49), S104 (= S109), G105 (= G110), T106 (≠ A111), F132 (= F137), S133 (≠ H138), E184 (= E189), E189 (= E194), D217 (= D222), I219 (= I224), K246 (= K251), R363 (= R372)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
39% identity, 92% coverage: 20:385/400 of query aligns to 17:376/387 of 1wkgA
- active site: F132 (= F137), E184 (= E189), D217 (= D222), Q220 (= Q225), K246 (= K251), T275 (= T280), R363 (= R372)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ W49), G105 (= G110), T106 (≠ A111), F132 (= F137), S133 (≠ H138), R135 (= R140), E184 (= E189), D217 (= D222), I219 (= I224), Q220 (= Q225), K246 (= K251), G273 (= G278), T274 (≠ G279), T275 (= T280)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
39% identity, 92% coverage: 20:385/400 of query aligns to 17:376/387 of 1vefA
- active site: F132 (= F137), D217 (= D222), K246 (= K251), T275 (= T280), R363 (= R372)
- binding pyridoxal-5'-phosphate: G105 (= G110), T106 (≠ A111), F132 (= F137), S133 (≠ H138), E184 (= E189), D217 (= D222), I219 (= I224), K246 (= K251)
Sites not aligning to the query:
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
40% identity, 92% coverage: 28:396/400 of query aligns to 16:375/375 of 2eh6A
- active site: F127 (= F137), E179 (= E189), D212 (= D222), Q215 (= Q225), K241 (= K251), T270 (= T280), R352 (= R372)
- binding pyridoxal-5'-phosphate: G95 (= G110), T96 (≠ A111), F127 (= F137), H128 (= H138), E179 (= E189), D212 (= D222), V214 (≠ I224), K241 (= K251)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
40% identity, 92% coverage: 28:396/400 of query aligns to 17:376/376 of O66442
- GT 96:97 (≠ GA 110:111) binding pyridoxal 5'-phosphate
- K242 (= K251) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T280) 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
37% identity, 91% coverage: 29:393/400 of query aligns to 25:388/393 of 2ordA
- active site: F134 (= F137), E186 (= E189), D219 (= D222), Q222 (= Q225), K248 (= K251), T276 (= T280), R367 (= R372)
- binding pyridoxal-5'-phosphate: G102 (= G110), T103 (≠ A111), F134 (= F137), H135 (= H138), E186 (= E189), D219 (= D222), V221 (≠ I224), Q222 (= Q225), K248 (= K251)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
37% identity, 91% coverage: 29:393/400 of query aligns to 17:380/385 of Q9X2A5
- GT 94:95 (≠ GA 110:111) binding pyridoxal 5'-phosphate
- T268 (= T280) binding pyridoxal 5'-phosphate
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
38% identity, 95% coverage: 12:389/400 of query aligns to 9:389/400 of 4addA
- active site: F136 (= F137), E188 (= E189), D221 (= D222), Q224 (= Q225), K250 (= K251), T279 (= T280), R372 (= R372)
- binding pyridoxal-5'-phosphate: G103 (= G110), A104 (= A111), F136 (= F137), H137 (= H138), D221 (= D222), V223 (≠ I224), K250 (= K251)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ A19), F136 (= F137), R139 (= R140)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
38% identity, 95% coverage: 12:389/400 of query aligns to 9:389/401 of 4adbB
- active site: F136 (= F137), E188 (= E189), D221 (= D222), Q224 (= Q225), K250 (= K251), T279 (= T280), R372 (= R372)
- binding pyridoxal-5'-phosphate: S102 (= S109), G103 (= G110), A104 (= A111), F136 (= F137), H137 (= H138), D221 (= D222), V223 (≠ I224), Q224 (= Q225), K250 (= K251)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
36% identity, 97% coverage: 12:397/400 of query aligns to 32:427/429 of P73133
- Y39 (≠ A19) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S109) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G110) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A111) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R140) 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 (= E194) 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 (= D222) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q225) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K251) 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.
P04181 Ornithine aminotransferase, mitochondrial; Ornithine delta-aminotransferase; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Homo sapiens (Human) (see 8 papers)
37% identity, 94% coverage: 24:397/400 of query aligns to 60:438/439 of P04181