SitesBLAST
Comparing WP_028487133.1 NCBI__GCF_000483485.1:WP_028487133.1 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)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
46% identity, 98% coverage: 4:384/390 of query aligns to 3:376/376 of O66442
- GT 96:97 (≠ GA 96:97) binding pyridoxal 5'-phosphate
- K242 (= K243) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T272) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
46% identity, 98% coverage: 4:384/390 of query aligns to 2:375/375 of 2eh6A
- active site: F127 (= F128), E179 (= E181), D212 (= D214), Q215 (= Q217), K241 (= K243), T270 (= T272), R352 (= R361)
- binding pyridoxal-5'-phosphate: G95 (= G96), T96 (≠ A97), F127 (= F128), H128 (= H129), E179 (= E181), D212 (= D214), V214 (≠ I216), K241 (= K243)
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
42% identity, 98% coverage: 4:385/390 of query aligns to 10:391/393 of 2ordA
- active site: F134 (= F128), E186 (= E181), D219 (= D214), Q222 (= Q217), K248 (= K243), T276 (= T272), R367 (= R361)
- binding pyridoxal-5'-phosphate: G102 (= G96), T103 (≠ A97), F134 (= F128), H135 (= H129), E186 (= E181), D219 (= D214), V221 (≠ I216), 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)
42% identity, 98% coverage: 4:385/390 of query aligns to 2:383/385 of Q9X2A5
- GT 94:95 (≠ GA 96:97) binding pyridoxal 5'-phosphate
- T268 (= T272) binding pyridoxal 5'-phosphate
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
43% identity, 97% coverage: 5:384/390 of query aligns to 11:383/390 of A0QYS9
- K304 (≠ Q304) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
39% identity, 97% coverage: 5:384/390 of query aligns to 10:389/390 of 8ht4B
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: 5:382/390 of query aligns to 69:451/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
41% identity, 97% coverage: 5:384/390 of query aligns to 19:393/400 of P9WPZ7
- K314 (≠ Q304) 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
41% identity, 97% coverage: 5:384/390 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.
41% identity, 97% coverage: 5:384/390 of query aligns to 13:387/391 of 7nn4A
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, 99% coverage: 4:389/390 of query aligns to 29:419/426 of 5eqcA
- active site: Y156 (≠ F128), E209 (= E181), D242 (= D214), Q245 (= Q217), K271 (= K243), T301 (= T272), R394 (= R361)
- binding beta-D-glucopyranose: R354 (= R324), G355 (= G325), R356 (≠ K326)
- binding alpha-D-glucopyranose: R48 (≠ I23), E404 (= E371), D408 (≠ Q375)
- binding pyridoxal-5'-phosphate: G121 (= G96), A122 (= A97), W157 (≠ H129), D242 (= D214), I244 (= I216), Q245 (= Q217), K271 (= K243)
5e3kB Crystal structure of the ornithine aminotransferase from toxoplasma gondii me49 in a complex with (s)-4-amino-5-fluoropentanoic acid
38% identity, 99% coverage: 4:389/390 of query aligns to 28:418/424 of 5e3kB
- active site: Y155 (≠ F128), E208 (= E181), D241 (= D214), Q244 (= Q217), K270 (= K243), T300 (= T272), R393 (= R361)
- binding 4-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]pent-4-enoic acid: Y33 (= Y9), V63 (≠ I39), G120 (= G96), A121 (= A97), Y155 (≠ F128), W156 (≠ H129), E213 (= E186), D241 (= D214), I243 (= I216), Q244 (= Q217), K270 (= K243), S299 (≠ T271), T300 (= T272)
- binding carbonate ion: P180 (≠ E153), G181 (= G154)
5e5iA Structure of the ornithine aminotransferase from toxoplasma gondii in complex with inactivator
38% identity, 99% coverage: 4:389/390 of query aligns to 26:416/421 of 5e5iA
- active site: Y153 (≠ F128), E206 (= E181), D239 (= D214), Q242 (= Q217), K268 (= K243), T298 (= T272), R391 (= R361)
- binding 4-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]pent-4-enoic acid: S297 (≠ T271), T298 (= T272)
- binding 6-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]-4-oxidanylidene-hexanoic acid: Y31 (= Y9), V61 (≠ I39), G118 (= G96), A119 (= A97), W154 (≠ H129), E211 (= E186), D239 (= D214), I241 (= I216), Q242 (= Q217), K268 (= K243)
5dj9A Crystal structure of the ornithine aminotransferase from toxoplasma gondii me49 in a complex with gabaculine
38% identity, 99% coverage: 4:389/390 of query aligns to 26:416/421 of 5dj9A
- active site: Y153 (≠ F128), E206 (= E181), D239 (= D214), Q242 (= Q217), K268 (= K243), T298 (= T272), R391 (= R361)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: Y31 (= Y9), V61 (≠ I39), G118 (= G96), A119 (= A97), Y153 (≠ F128), W154 (≠ H129), E211 (= E186), D239 (= D214), I241 (= I216), Q242 (= Q217), K268 (= K243), S297 (≠ T271), T298 (= T272)
5e3kA Crystal structure of the ornithine aminotransferase from toxoplasma gondii me49 in a complex with (s)-4-amino-5-fluoropentanoic acid
38% identity, 99% coverage: 4:389/390 of query aligns to 27:417/422 of 5e3kA
- active site: Y154 (≠ F128), E207 (= E181), D240 (= D214), Q243 (= Q217), K269 (= K243), T299 (= T272), R392 (= R361)
- binding 4-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]pent-4-enoic acid: Y32 (= Y9), V62 (≠ I39), G119 (= G96), A120 (= A97), Y154 (≠ F128), W155 (≠ H129), E212 (= E186), D240 (= D214), I242 (= I216), Q243 (= Q217), K269 (= K243), S298 (≠ T271), T299 (= T272)
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
37% identity, 98% coverage: 4:387/390 of query aligns to 3:388/388 of 3nx3A
- active site: F127 (= F128), E179 (= E181), D212 (= D214), Q215 (= Q217), K241 (= K243), T271 (= T272), R362 (= R361)
- binding magnesium ion: N191 (≠ K193), F194 (≠ Y196), I313 (≠ L314), F316 (≠ Q317), D317 (≠ S318), C319 (≠ V320), Q370 (≠ D369), K371 (≠ T370)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
36% identity, 100% coverage: 1:389/390 of query aligns to 8:400/400 of 4addA
- active site: F136 (= F128), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T279 (= T272), R372 (= R361)
- binding pyridoxal-5'-phosphate: G103 (= G96), A104 (= A97), F136 (= F128), H137 (= H129), D221 (= D214), V223 (≠ I216), K250 (= K243)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y9), F136 (= F128), R139 (= R131)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
36% identity, 100% coverage: 1:389/390 of query aligns to 8:400/401 of 4adbB
- active site: F136 (= F128), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T279 (= T272), R372 (= R361)
- binding pyridoxal-5'-phosphate: S102 (= S95), G103 (= G96), A104 (= A97), F136 (= F128), H137 (= H129), D221 (= D214), V223 (≠ I216), Q224 (= Q217), K250 (= K243)
Q6LFH8 Ornithine aminotransferase; PfOAT; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Plasmodium falciparum (isolate 3D7) (see paper)
36% identity, 97% coverage: 8:387/390 of query aligns to 24:410/414 of Q6LFH8
- C154 (≠ T135) modified: Disulfide link with 163, Reversible; mutation to S: Severe reduction in catalytic activity. Does not affect TRX1-mediated activation. Severe reduction in catalytic activity and loss of TRX1-mediated activation; when associated with S-163.
- C163 (≠ V144) modified: Disulfide link with 154, Reversible; mutation to S: No effect on catalytic activity. Requires higher concentrations of TRX1 for activation. Severe reduction in catalytic activity and loss of TRX1-mediated activation; when associated with S-154.
- C316 (≠ I296) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C350 (≠ I330) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C390 (≠ V367) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
39% identity, 92% coverage: 18:377/390 of query aligns to 25:379/387 of 1wkhA
- active site: F132 (= F128), E184 (= E181), D217 (= D214), Q220 (= Q217), K246 (= K243), T275 (= T272), R363 (= R361)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I39), S104 (= S95), G105 (= G96), T106 (≠ A97), F132 (= F128), S133 (≠ H129), E184 (= E181), E189 (= E186), D217 (= D214), I219 (= I216), K246 (= K243), R363 (= R361)
Sites not aligning to the query:
Query Sequence
>WP_028487133.1 NCBI__GCF_000483485.1:WP_028487133.1
MSDHLMTTYARLPVTFEKGAGAILQDTNGKSYLDAVSGIAVCSLGHAHPAVAEAICEQSH
QLIHTSNLYNVANQQKLSDRLTELSGMDRAFFCNSGAEANETALKIAKKFGHQKGIDNPA
VIVMENSFHGRTMATLSATGNAKVHEGFTPLVEGFVRVPYDNVEAVKQHSDNANIVAILV
EPVQGEGGVHVPKAGYLTELKAICEQNDWLLMLDEIQTGIGRTGKWFAFQHESVTPDVLT
LAKALGNGVPIGCCLAKGKAADVLVPGNHGTTFGGNPLACAAGLAVLNIMEMHNYIPHVA
KKGQTLLERFREELKDQSSVIEIRGKGYMIGIQLDRPCGELVTKALENGLLINVTRGDTV
RLLPPFVMDTEQKEQLITQLTQLIREFLAT
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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