SitesBLAST
Comparing WP_053767489.1 NCBI__GCF_001280255.1:WP_053767489.1 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)
92% identity, 99% coverage: 1:394/396 of query aligns to 1:394/395 of Q5SHH5
- GT 113:114 (= GT 113:114) binding pyridoxal 5'-phosphate
- K254 (= K254) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T283) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
92% identity, 97% coverage: 9:394/396 of query aligns to 1:386/387 of 1wkhA
- active site: S13 (≠ T21), F132 (= F140), E184 (= E192), D217 (= D225), Q220 (= Q228), K246 (= K254), T275 (= T283), R363 (= R371)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (= Y54), S104 (= S112), G105 (= G113), T106 (= T114), F132 (= F140), S133 (= S141), E184 (= E192), E189 (= E197), D217 (= D225), I219 (= I227), K246 (= K254), R363 (= R371)
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
92% identity, 97% coverage: 9:394/396 of query aligns to 1:386/387 of 1wkgA
- active site: S13 (≠ T21), F132 (= F140), E184 (= E192), D217 (= D225), Q220 (= Q228), K246 (= K254), T275 (= T283), R363 (= R371)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (= Y24), Y46 (= Y54), G105 (= G113), T106 (= T114), F132 (= F140), S133 (= S141), R135 (= R143), E184 (= E192), D217 (= D225), I219 (= I227), Q220 (= Q228), K246 (= K254), G273 (= G281), T274 (= T282), T275 (= T283)
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
92% identity, 97% coverage: 9:394/396 of query aligns to 1:386/387 of 1vefA
- active site: S13 (≠ T21), F132 (= F140), D217 (= D225), K246 (= K254), T275 (= T283), R363 (= R371)
- binding pyridoxal-5'-phosphate: G105 (= G113), T106 (= T114), F132 (= F140), S133 (= S141), E184 (= E192), D217 (= D225), I219 (= I227), K246 (= K254)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
43% identity, 94% coverage: 24:394/396 of query aligns to 8:376/376 of O66442
- GT 96:97 (= GT 113:114) binding pyridoxal 5'-phosphate
- K242 (= K254) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T283) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
43% identity, 94% coverage: 24:394/396 of query aligns to 7:375/375 of 2eh6A
- active site: F127 (= F140), E179 (= E192), D212 (= D225), Q215 (= Q228), K241 (= K254), T270 (= T283), R352 (= R371)
- binding pyridoxal-5'-phosphate: G95 (= G113), T96 (= T114), F127 (= F140), H128 (≠ S141), E179 (= E192), D212 (= D225), V214 (≠ I227), K241 (= K254)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
44% identity, 94% coverage: 24:394/396 of query aligns to 7:382/385 of Q9X2A5
- GT 94:95 (= GT 113:114) binding pyridoxal 5'-phosphate
- T268 (= T283) 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
44% identity, 94% coverage: 24:394/396 of query aligns to 15:390/393 of 2ordA
- active site: F134 (= F140), E186 (= E192), D219 (= D225), Q222 (= Q228), K248 (= K254), T276 (= T283), R367 (= R371)
- binding pyridoxal-5'-phosphate: G102 (= G113), T103 (= T114), F134 (= F140), H135 (≠ S141), E186 (= E192), D219 (= D225), V221 (≠ I227), Q222 (= Q228), K248 (= K254)
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
46% identity, 94% coverage: 24:394/396 of query aligns to 15:383/390 of A0QYS9
- K304 (≠ P315) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
40% identity, 94% coverage: 23:394/396 of query aligns to 20:404/405 of P40732
- GT 108:109 (= GT 113:114) binding pyridoxal 5'-phosphate
- K255 (= K254) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T283) binding pyridoxal 5'-phosphate
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
44% identity, 98% coverage: 5:394/396 of query aligns to 11:393/400 of P9WPZ7
- K314 (≠ P315) 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
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
40% identity, 94% coverage: 23:394/396 of query aligns to 15:399/402 of 4jevB
- active site: F136 (= F140), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T279 (= T283), R372 (= R371)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (≠ Y54), S102 (= S112), G103 (= G113), T104 (= T114), F136 (= F140), H137 (≠ S141), E188 (= E192), E193 (= E197), D221 (= D225), V223 (≠ I227), Q224 (= Q228), K250 (= K254), R372 (= R371)
7nncC Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal-5'-phosphate and 6-methoxyquinoline-3-carboxylic acid
44% identity, 98% coverage: 5:394/396 of query aligns to 5:387/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
44% identity, 98% coverage: 5:394/396 of query aligns to 5:387/391 of 7nn4A
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
38% identity, 94% coverage: 23:394/396 of query aligns to 7:385/388 of 3nx3A
- active site: F127 (= F140), E179 (= E192), D212 (= D225), Q215 (= Q228), K241 (= K254), T271 (= T283), R362 (= R371)
- binding magnesium ion: N191 (≠ K204), F194 (= F207), I313 (≠ P325), F316 (vs. gap), D317 (≠ P327), C319 (≠ I329), Q370 (≠ D379), K371 (≠ R380)
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)
39% identity, 97% coverage: 12:395/396 of query aligns to 61:454/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
40% identity, 94% coverage: 24:394/396 of query aligns to 39:425/429 of P73133
- Y39 (= Y24) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S112) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G113) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (≠ T114) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R143) 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 (= E197) 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 (= D225) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q228) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K254) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T283) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R371) 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.
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
40% identity, 94% coverage: 23:394/396 of query aligns to 9:388/389 of 2pb0A
- active site: F130 (= F140), E182 (= E192), D215 (= D225), Q218 (= Q228), K244 (= K254), T268 (= T283), R361 (= R371)
- binding pyridoxal-5'-phosphate: S96 (= S112), G97 (= G113), T98 (= T114), F130 (= F140), H131 (≠ S141), E182 (= E192), D215 (= D225), V217 (≠ I227), Q218 (= Q228), K244 (= K254)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
44% identity, 91% coverage: 31:390/396 of query aligns to 21:385/390 of 8ht4B
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
40% identity, 94% coverage: 23:394/396 of query aligns to 15:394/397 of 4jewA
- active site: F136 (= F140), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T274 (= T283), R367 (= R371)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G113), T104 (= T114), F136 (= F140), H137 (≠ S141), R139 (= R143), E188 (= E192), E193 (= E197), D221 (= D225), V223 (≠ I227), K250 (= K254)
- binding picric acid: K25 (≠ R33), K27 (≠ Q35), W32 (= W40)
Query Sequence
>WP_053767489.1 NCBI__GCF_001280255.1:WP_053767489.1
MERAVKEDWRALLEAEKTLDTGVYTKHDLLIVRGQGARVWDAEGNEYIDCVGGYGVANLG
HGNPEVVEAVKRQAETLMVMPQTLPTPARGEFYRTLVSLLPPELNRVFPVNSGTEANEAA
LKFARAHTGRKKFVAAMRGFSGRTMGSLSVTWEPKYREPFLPLVGPVEFIPYNDVEALRR
AVDEETAAVILEPVQGEGGVRPAKPEFLQAAREITREKGALLILDEIQTGMGRTGRRFAF
EHYGVVPDILTLAKALGGGVPIGAVVMRKEVAESMPKGGHGTTFGGNPLAMAAGVAAIRY
LERTRLWERAAELGPWFMEKLREIPSPKIREVRGLGLMVGLELKEKSAPYIQKLEKEHRI
LTLQAGPTVIRFLPPLVIDREDLERVVEAVRAVLTE
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory