SitesBLAST
Comparing WP_024850655.1 NCBI__GCF_000526715.1:WP_024850655.1 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)
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
49% identity, 95% coverage: 8:380/394 of query aligns to 3:368/375 of 2eh6A
- active site: F127 (= F131), E179 (= E184), D212 (= D217), Q215 (= Q220), K241 (= K246), T270 (= T275), R352 (= R364)
- binding pyridoxal-5'-phosphate: G95 (= G99), T96 (≠ A100), F127 (= F131), H128 (= H132), E179 (= E184), D212 (= D217), V214 (≠ I219), K241 (= K246)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
49% identity, 95% coverage: 8:380/394 of query aligns to 4:369/376 of O66442
- GT 96:97 (≠ GA 99:100) binding pyridoxal 5'-phosphate
- K242 (= K246) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T275) binding pyridoxal 5'-phosphate
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
45% identity, 95% coverage: 8:381/394 of query aligns to 35:419/429 of P73133
- Y39 (= Y12) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S98) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G99) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A100) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R134) 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 (= E189) 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 (= D217) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q220) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K246) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T275) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R364) 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.
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
44% identity, 96% coverage: 8:387/394 of query aligns to 10:389/390 of 8ht4B
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
44% identity, 97% coverage: 8:388/394 of query aligns to 3:383/385 of Q9X2A5
- GT 94:95 (≠ GA 99:100) binding pyridoxal 5'-phosphate
- T268 (= T275) 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, 97% coverage: 8:388/394 of query aligns to 11:391/393 of 2ordA
- active site: F134 (= F131), E186 (= E184), D219 (= D217), Q222 (= Q220), K248 (= K246), T276 (= T275), R367 (= R364)
- binding pyridoxal-5'-phosphate: G102 (= G99), T103 (≠ A100), F134 (= F131), H135 (= H132), E186 (= E184), D219 (= D217), V221 (≠ I219), Q222 (= Q220), K248 (= K246)
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
45% identity, 97% coverage: 8:391/394 of query aligns to 11:387/390 of A0QYS9
- K304 (≠ Q307) 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)
45% identity, 96% coverage: 8:387/394 of query aligns to 19:393/400 of P9WPZ7
- K314 (≠ Q307) 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
45% identity, 96% coverage: 8:387/394 of query aligns to 13:387/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
45% identity, 96% coverage: 8:387/394 of query aligns to 13:387/391 of 7nn4A
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, 95% coverage: 8:381/394 of query aligns to 69:447/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
38% identity, 97% coverage: 8:389/394 of query aligns to 4:387/388 of 3nx3A
- active site: F127 (= F131), E179 (= E184), D212 (= D217), Q215 (= Q220), K241 (= K246), T271 (= T275), R362 (= R364)
- binding magnesium ion: N191 (≠ K196), F194 (≠ Y199), I313 (≠ L317), F316 (≠ Q320), D317 (≠ S321), C319 (≠ V323), Q370 (= Q372), K371 (≠ N373)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
39% identity, 96% coverage: 8:386/394 of query aligns to 12:401/402 of 4jevB
- active site: F136 (= F131), E188 (= E184), D221 (= D217), Q224 (= Q220), K250 (= K246), T279 (= T275), R372 (= R364)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I42), S102 (= S98), G103 (= G99), T104 (≠ A100), F136 (= F131), H137 (= H132), E188 (= E184), E193 (= E189), D221 (= D217), V223 (≠ I219), Q224 (= Q220), K250 (= K246), R372 (= R364)
5e3kA Crystal structure of the ornithine aminotransferase from toxoplasma gondii me49 in a complex with (s)-4-amino-5-fluoropentanoic acid
38% identity, 96% coverage: 8:384/394 of query aligns to 28:412/422 of 5e3kA
- active site: Y154 (≠ F131), E207 (= E184), D240 (= D217), Q243 (= Q220), K269 (= K246), T299 (= T275), R392 (= R364)
- binding 4-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]pent-4-enoic acid: Y32 (= Y12), V62 (≠ I42), G119 (= G99), A120 (= A100), Y154 (≠ F131), W155 (≠ H132), E212 (= E189), D240 (= D217), I242 (= I219), Q243 (= Q220), K269 (= K246), S298 (≠ T274), T299 (= T275)
5eqcA Structure of the ornithine aminotransferase from toxoplasma gondii crystallized in presence of oxidized glutathione reveals partial occupancy of plp at the protein active site
38% identity, 96% coverage: 8:384/394 of query aligns to 30:414/426 of 5eqcA
- active site: Y156 (≠ F131), E209 (= E184), D242 (= D217), Q245 (= Q220), K271 (= K246), T301 (= T275), R394 (= R364)
- binding beta-D-glucopyranose: R354 (= R327), G355 (= G328), R356 (≠ K329)
- binding alpha-D-glucopyranose: R48 (≠ V26), E404 (≠ Q374), D408 (≠ E378)
- binding pyridoxal-5'-phosphate: G121 (= G99), A122 (= A100), W157 (≠ H132), D242 (= D217), I244 (= I219), Q245 (= Q220), K271 (= K246)
5e3kB Crystal structure of the ornithine aminotransferase from toxoplasma gondii me49 in a complex with (s)-4-amino-5-fluoropentanoic acid
38% identity, 96% coverage: 8:384/394 of query aligns to 29:413/424 of 5e3kB
- active site: Y155 (≠ F131), E208 (= E184), D241 (= D217), Q244 (= Q220), K270 (= K246), T300 (= T275), R393 (= R364)
- binding 4-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]pent-4-enoic acid: Y33 (= Y12), V63 (≠ I42), G120 (= G99), A121 (= A100), Y155 (≠ F131), W156 (≠ H132), E213 (= E189), D241 (= D217), I243 (= I219), Q244 (= Q220), K270 (= K246), S299 (≠ T274), T300 (= T275)
- binding carbonate ion: P180 (≠ E156), G181 (= G157)
5e5iA Structure of the ornithine aminotransferase from toxoplasma gondii in complex with inactivator
38% identity, 96% coverage: 8:384/394 of query aligns to 27:411/421 of 5e5iA
- active site: Y153 (≠ F131), E206 (= E184), D239 (= D217), Q242 (= Q220), K268 (= K246), T298 (= T275), R391 (= R364)
- binding 4-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]pent-4-enoic acid: S297 (≠ T274), T298 (= T275)
- binding 6-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]-4-oxidanylidene-hexanoic acid: Y31 (= Y12), V61 (≠ I42), G118 (= G99), A119 (= A100), W154 (≠ H132), E211 (= E189), D239 (= D217), I241 (= I219), Q242 (= Q220), K268 (= K246)
5dj9A Crystal structure of the ornithine aminotransferase from toxoplasma gondii me49 in a complex with gabaculine
38% identity, 96% coverage: 8:384/394 of query aligns to 27:411/421 of 5dj9A
- active site: Y153 (≠ F131), E206 (= E184), D239 (= D217), Q242 (= Q220), K268 (= K246), T298 (= T275), R391 (= R364)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: Y31 (= Y12), V61 (≠ I42), G118 (= G99), A119 (= A100), Y153 (≠ F131), W154 (≠ H132), E211 (= E189), D239 (= D217), I241 (= I219), Q242 (= Q220), K268 (= K246), S297 (≠ T274), T298 (= T275)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
38% identity, 98% coverage: 8:392/394 of query aligns to 12:400/400 of 4addA
- active site: F136 (= F131), E188 (= E184), D221 (= D217), Q224 (= Q220), K250 (= K246), T279 (= T275), R372 (= R364)
- binding pyridoxal-5'-phosphate: G103 (= G99), A104 (= A100), F136 (= F131), H137 (= H132), D221 (= D217), V223 (≠ I219), K250 (= K246)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y12), F136 (= F131), R139 (= R134)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
38% identity, 98% coverage: 8:392/394 of query aligns to 12:400/401 of 4adbB
- active site: F136 (= F131), E188 (= E184), D221 (= D217), Q224 (= Q220), K250 (= K246), T279 (= T275), R372 (= R364)
- binding pyridoxal-5'-phosphate: S102 (= S98), G103 (= G99), A104 (= A100), F136 (= F131), H137 (= H132), D221 (= D217), V223 (≠ I219), Q224 (= Q220), K250 (= K246)
Query Sequence
>WP_024850655.1 NCBI__GCF_000526715.1:WP_024850655.1
MTTTVDPIMNTYARLPITFISGDGAVLRDENHQEYLDAVSGIAVCSLGHTHPAVTEAICH
QAGQLIHTSNLYQVEKQNLLAEKLIELSQMDRVFFSNSGAEANEATLKIARKYGHQKNID
RAKIIVMENSFHGRTLATLSATGNEKVHEGFYPLVEGFVRVPFDDVQAVKELSNDPDIVA
ILVEPIQGEGGVHVPKPGYLKQLKEICEQNDWLLMLDEIQTGIGRTGKWFAHQHDDIVPD
VMTLAKALGNGVPIGACLAKGKAAEVLVPGNHGTTFGGNPLACAAGLATLNVMETHSLID
QVHTKGQMIVERFQEALKNQSNVVNVRGKGFMIGIQLDSPCGELVKQALEQKLLINVTRG
DTIRLLPPFVIQNQQIDELIEKVVALIKNHSSAE
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