SitesBLAST
Comparing N515DRAFT_3308 FitnessBrowser__Dyella79:N515DRAFT_3308 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)
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)
47% identity, 95% coverage: 19:408/411 of query aligns to 18:404/405 of P40732
- GT 108:109 (= GT 110:111) binding pyridoxal 5'-phosphate
- K255 (= K259) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T288) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
47% identity, 95% coverage: 19:408/411 of query aligns to 13:399/402 of 4jevB
- active site: F136 (= F144), E188 (= E197), D221 (= D230), Q224 (= Q233), K250 (= K259), T279 (= T288), R372 (= R381)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I52), S102 (= S109), G103 (= G110), T104 (= T111), F136 (= F144), H137 (= H145), E188 (= E197), E193 (= E202), D221 (= D230), V223 (≠ I232), Q224 (= Q233), K250 (= K259), R372 (= R381)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
47% identity, 96% coverage: 17:410/411 of query aligns to 11:401/401 of 4adbB
- active site: F136 (= F144), E188 (= E197), D221 (= D230), Q224 (= Q233), K250 (= K259), T279 (= T288), R372 (= R381)
- binding pyridoxal-5'-phosphate: S102 (= S109), G103 (= G110), A104 (≠ T111), F136 (= F144), H137 (= H145), D221 (= D230), V223 (≠ I232), Q224 (= Q233), K250 (= K259)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
47% identity, 96% coverage: 16:408/411 of query aligns to 10:399/400 of 4addA
- active site: F136 (= F144), E188 (= E197), D221 (= D230), Q224 (= Q233), K250 (= K259), T279 (= T288), R372 (= R381)
- binding pyridoxal-5'-phosphate: G103 (= G110), A104 (≠ T111), F136 (= F144), H137 (= H145), D221 (= D230), V223 (≠ I232), K250 (= K259)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y22), F136 (= F144), R139 (= R147)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
47% identity, 95% coverage: 19:408/411 of query aligns to 7:388/389 of 2pb0A
- active site: F130 (= F144), E182 (= E197), D215 (= D230), Q218 (= Q233), K244 (= K259), T268 (= T288), R361 (= R381)
- binding pyridoxal-5'-phosphate: S96 (= S109), G97 (= G110), T98 (= T111), F130 (= F144), H131 (= H145), E182 (= E197), D215 (= D230), V217 (≠ I232), Q218 (= Q233), K244 (= K259)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
47% identity, 95% coverage: 19:408/411 of query aligns to 13:394/397 of 4jewA
- active site: F136 (= F144), E188 (= E197), D221 (= D230), Q224 (= Q233), K250 (= K259), T274 (= T288), R367 (= R381)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G110), T104 (= T111), F136 (= F144), H137 (= H145), R139 (= R147), E188 (= E197), E193 (= E202), D221 (= D230), V223 (≠ I232), K250 (= K259)
- binding picric acid: K25 (≠ H31), K27 (= K33), W32 (= W38)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
47% identity, 95% coverage: 17:408/411 of query aligns to 34:429/429 of P73133
- Y39 (= Y22) 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 (≠ T111) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R147) 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 (= E202) 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 (= D230) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q233) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K259) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T288) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R381) 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.
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: 17:404/411 of query aligns to 10:390/393 of 2ordA
- active site: F134 (= F144), E186 (= E197), D219 (= D230), Q222 (= Q233), K248 (= K259), T276 (= T288), R367 (= R381)
- binding pyridoxal-5'-phosphate: G102 (= G110), T103 (= T111), F134 (= F144), H135 (= H145), E186 (= E197), D219 (= D230), V221 (≠ I232), Q222 (= Q233), K248 (= K259)
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: 17:404/411 of query aligns to 2:382/385 of Q9X2A5
- GT 94:95 (= GT 110:111) binding pyridoxal 5'-phosphate
- T268 (= T288) 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)
43% identity, 94% coverage: 7:393/411 of query aligns to 58:442/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
42% identity, 97% coverage: 9:405/411 of query aligns to 1:390/390 of 8ht4B
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
44% identity, 93% coverage: 22:404/411 of query aligns to 15:383/390 of A0QYS9
- K304 (≠ Q320) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
37% identity, 96% coverage: 15:407/411 of query aligns to 1:388/388 of 3nx3A
- active site: F127 (= F144), E179 (= E197), D212 (= D230), Q215 (= Q233), K241 (= K259), T271 (= T288), R362 (= R381)
- binding magnesium ion: N191 (≠ S209), F194 (= F212), I313 (≠ D330), F316 (≠ L333), D317 (≠ K334), C319 (≠ F336), Q370 (≠ T389), K371 (≠ D390)
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
45% identity, 94% coverage: 22:409/411 of query aligns to 23:398/400 of P9WPZ7
- K314 (≠ Q320) 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
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
44% identity, 94% coverage: 21:405/411 of query aligns to 23:395/395 of Q5SHH5
- GT 113:114 (= GT 110:111) binding pyridoxal 5'-phosphate
- K254 (= K259) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T288) binding pyridoxal 5'-phosphate
7nncC Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal-5'-phosphate and 6-methoxyquinoline-3-carboxylic acid
45% identity, 93% coverage: 22:404/411 of query aligns to 17:387/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
45% identity, 93% coverage: 22:404/411 of query aligns to 17:387/391 of 7nn4A
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
43% identity, 94% coverage: 21:405/411 of query aligns to 15:387/387 of 1wkhA
- active site: F132 (= F144), E184 (= E197), D217 (= D230), Q220 (= Q233), K246 (= K259), T275 (= T288), R363 (= R381)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I52), S104 (= S109), G105 (= G110), T106 (= T111), F132 (= F144), S133 (≠ H145), E184 (= E197), E189 (= E202), D217 (= D230), I219 (= I232), K246 (= K259), R363 (= R381)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
43% identity, 94% coverage: 21:405/411 of query aligns to 15:387/387 of 1wkgA
- active site: F132 (= F144), E184 (= E197), D217 (= D230), Q220 (= Q233), K246 (= K259), T275 (= T288), R363 (= R381)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (= Y22), Y46 (≠ I52), G105 (= G110), T106 (= T111), F132 (= F144), S133 (≠ H145), R135 (= R147), E184 (= E197), D217 (= D230), I219 (= I232), Q220 (= Q233), K246 (= K259), G273 (= G286), T274 (= T287), T275 (= T288)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
43% identity, 94% coverage: 21:405/411 of query aligns to 15:387/387 of 1vefA
- active site: F132 (= F144), D217 (= D230), K246 (= K259), T275 (= T288), R363 (= R381)
- binding pyridoxal-5'-phosphate: G105 (= G110), T106 (= T111), F132 (= F144), S133 (≠ H145), E184 (= E197), D217 (= D230), I219 (= I232), K246 (= K259)
Sites not aligning to the query:
Query Sequence
>N515DRAFT_3308 FitnessBrowser__Dyella79:N515DRAFT_3308
MHAQDSSSSLIDLGKRYWLPVYRPREVVLDHGKGARVWDTEGRDYVDLGAGIAVNALGHQ
DPDLVDALVTQARKLWHSSNVFYTEPPLHLAEELVQASGFAERVFLCNSGTEANEAAIKL
VRKWAASKGRAPEQRVILTFRGSFHGRTLAAVTATAQPKYQENYEPLPGGFRYLDFNDVA
GLEAAFAQGDVAAVMLEPVQGEGGVLPASPAFIRRARELCDTHEALLVLDEIQCGMGRTG
TLFAHAQDGVTPDIVTLAKALGCGFPIGAMLAGPKVAEVMQYGAHGTTFGGNPMAAAVAR
VALRKLASAELMANVAKQAQALRDGLAAIDGELKLFAEVRGRGLMLGAVLAEAYKGRAGE
VLDHAAAHGLLVLQAGPDVLRFVPPLNITDADLAEGLARLRAALADFVGKR
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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