SitesBLAST
Comparing WP_025274361.1 NCBI__GCF_000527155.1:WP_025274361.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
51% identity, 96% coverage: 9:392/401 of query aligns to 3:384/390 of A0QYS9
- K304 (≠ R314) 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)
50% identity, 98% coverage: 1:393/401 of query aligns to 1:395/400 of P9WPZ7
- M1 (= M1) modified: Initiator methionine, Removed
- T2 (= T2) modified: N-acetylthreonine; partial
- K314 (≠ R314) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7nncC Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal-5'-phosphate and 6-methoxyquinoline-3-carboxylic acid
50% identity, 97% coverage: 5:393/401 of query aligns to 1:389/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
50% identity, 97% coverage: 5:393/401 of query aligns to 1:389/391 of 7nn4A
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
43% identity, 95% coverage: 13:391/401 of query aligns to 6:389/390 of 8ht4B
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
41% identity, 94% coverage: 17:392/401 of query aligns to 11:391/393 of 2ordA
- active site: F134 (= F139), E186 (= E191), D219 (= D224), Q222 (= Q227), K248 (= K253), T276 (= T282), R367 (= R368)
- binding pyridoxal-5'-phosphate: G102 (= G109), T103 (= T110), F134 (= F139), H135 (= H140), E186 (= E191), D219 (= D224), V221 (≠ I226), Q222 (= Q227), K248 (= K253)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
41% identity, 94% coverage: 17:392/401 of query aligns to 3:383/385 of Q9X2A5
- GT 94:95 (= GT 109:110) binding pyridoxal 5'-phosphate
- T268 (= T282) binding pyridoxal 5'-phosphate
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)
42% identity, 94% coverage: 14:391/401 of query aligns to 66:453/457 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, 95% coverage: 2:382/401 of query aligns to 17:416/429 of P73133
- Y39 (= Y21) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S108) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G109) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (≠ T110) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R142) 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 (= E196) 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 (= D224) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q227) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K253) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T282) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R368) 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)
42% identity, 94% coverage: 14:391/401 of query aligns to 15:394/395 of Q5SHH5
- GT 113:114 (= GT 109:110) binding pyridoxal 5'-phosphate
- K254 (= K253) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T282) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
42% identity, 94% coverage: 14:391/401 of query aligns to 7:386/387 of 1wkhA
- active site: S13 (≠ T20), F132 (= F139), E184 (= E191), D217 (= D224), Q220 (= Q227), K246 (= K253), T275 (= T282), R363 (= R368)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I51), S104 (= S108), G105 (= G109), T106 (= T110), F132 (= F139), S133 (≠ H140), E184 (= E191), E189 (= E196), D217 (= D224), I219 (= I226), K246 (= K253), R363 (= R368)
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
42% identity, 94% coverage: 14:391/401 of query aligns to 7:386/387 of 1wkgA
- active site: S13 (≠ T20), F132 (= F139), E184 (= E191), D217 (= D224), Q220 (= Q227), K246 (= K253), T275 (= T282), R363 (= R368)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (= Y21), Y46 (≠ I51), G105 (= G109), T106 (= T110), F132 (= F139), S133 (≠ H140), R135 (= R142), E184 (= E191), D217 (= D224), I219 (= I226), Q220 (= Q227), K246 (= K253), G273 (= G280), T274 (≠ S281), T275 (= T282)
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
42% identity, 94% coverage: 14:391/401 of query aligns to 7:386/387 of 1vefA
- active site: S13 (≠ T20), F132 (= F139), D217 (= D224), K246 (= K253), T275 (= T282), R363 (= R368)
- binding pyridoxal-5'-phosphate: G105 (= G109), T106 (= T110), F132 (= F139), S133 (≠ H140), E184 (= E191), D217 (= D224), I219 (= I226), K246 (= K253)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
38% identity, 94% coverage: 17:391/401 of query aligns to 4:376/376 of O66442
- GT 96:97 (= GT 109:110) binding pyridoxal 5'-phosphate
- K242 (= K253) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T282) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
38% identity, 94% coverage: 17:391/401 of query aligns to 3:375/375 of 2eh6A
- active site: F127 (= F139), E179 (= E191), D212 (= D224), Q215 (= Q227), K241 (= K253), T270 (= T282), R352 (= R368)
- binding pyridoxal-5'-phosphate: G95 (= G109), T96 (= T110), F127 (= F139), H128 (= H140), E179 (= E191), D212 (= D224), V214 (≠ I226), K241 (= K253)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
39% identity, 94% coverage: 10:387/401 of query aligns to 5:395/400 of 4addA
- active site: F136 (= F139), E188 (= E191), D221 (= D224), Q224 (= Q227), K250 (= K253), T279 (= T282), R372 (= R368)
- binding pyridoxal-5'-phosphate: G103 (= G109), A104 (≠ T110), F136 (= F139), H137 (= H140), D221 (= D224), V223 (≠ I226), K250 (= K253)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y21), F136 (= F139), R139 (= R142)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
38% identity, 96% coverage: 10:393/401 of query aligns to 5:401/401 of 4adbB
- active site: F136 (= F139), E188 (= E191), D221 (= D224), Q224 (= Q227), K250 (= K253), T279 (= T282), R372 (= R368)
- binding pyridoxal-5'-phosphate: S102 (= S108), G103 (= G109), A104 (≠ T110), F136 (= F139), H137 (= H140), D221 (= D224), V223 (≠ I226), Q224 (= Q227), K250 (= K253)
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)
36% identity, 98% coverage: 1:391/401 of query aligns to 1:404/405 of P40732
- GT 108:109 (= GT 109:110) binding pyridoxal 5'-phosphate
- K255 (= K253) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T282) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
36% identity, 95% coverage: 13:391/401 of query aligns to 8:399/402 of 4jevB
- active site: F136 (= F139), E188 (= E191), D221 (= D224), Q224 (= Q227), K250 (= K253), T279 (= T282), R372 (= R368)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I51), S102 (= S108), G103 (= G109), T104 (= T110), F136 (= F139), H137 (= H140), E188 (= E191), E193 (= E196), D221 (= D224), V223 (≠ I226), Q224 (= Q227), K250 (= K253), R372 (= R368)
2byjA Ornithine aminotransferase mutant y85i (see paper)
38% identity, 95% coverage: 2:382/401 of query aligns to 4:392/404 of 2byjA
- active site: F142 (= F139), E195 (= E191), D228 (= D224), Q231 (= Q227), K257 (= K253), T287 (= T282), R378 (= R368)
- binding pyridoxal-5'-phosphate: G107 (= G109), V108 (≠ T110), F142 (= F139), W143 (≠ H140), D228 (= D224), I230 (= I226), Q231 (= Q227), K257 (= K253)
Query Sequence
>WP_025274361.1 NCBI__GCF_000527155.1:WP_025274361.1
MTTDSTTALQNRYADALMDTYGQPPVALASGNGRHVTDVDGRTYLDMIGGIAVSTVGHRH
PDYVEAVVRQTATIAHTSNLFFHPTEVELAETLVKLTGADGRVFFSNSGTEANEAALKLA
LKAGKPHGKTRIVAAENSFHGRTLGTLAVTGKASIREPFAPFGIEATFVPYGDTAALTAA
VDDTVAAVILEPTQGEAGVVPASTDFLHTARALTHEHGSALILDEIQAGFGRTGRWFAHH
AADITPDIITLAKGLAGGIPMGATIGVGDWGNVFQAGDHGSTFGGNPIAGAAALAVIDII
EREDLFDNVNTLGRKLENRLHNHPAVIAVRGEALWRGIVLDTDIAADVCGQLRNAGILAN
PVRPNVIRIAPPLSITAAELEQFTSALTDVLDQYPAQGKTP
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