SitesBLAST
Comparing WP_011736998.1 NCBI__GCF_000015045.1:WP_011736998.1 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)
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
48% identity, 96% coverage: 13:393/398 of query aligns to 2:375/375 of 2eh6A
- active site: F127 (= F138), E179 (= E190), D212 (= D223), Q215 (= Q226), K241 (= K252), T270 (= T281), R352 (= R370)
- binding pyridoxal-5'-phosphate: G95 (= G105), T96 (≠ A106), F127 (= F138), H128 (= H139), E179 (= E190), D212 (= D223), V214 (= V225), K241 (= K252)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
48% identity, 96% coverage: 13:393/398 of query aligns to 3:376/376 of O66442
- GT 96:97 (≠ GA 105:106) binding pyridoxal 5'-phosphate
- K242 (= K252) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T281) binding pyridoxal 5'-phosphate
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
48% identity, 96% coverage: 11:394/398 of query aligns to 32:426/429 of P73133
- Y39 (= Y18) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S104) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G105) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A106) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R141) 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 (= E195) 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 (= D223) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q226) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K252) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T281) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R370) 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
45% identity, 96% coverage: 13:393/398 of query aligns to 10:390/393 of 2ordA
- active site: F134 (= F138), E186 (= E190), D219 (= D223), Q222 (= Q226), K248 (= K252), T276 (= T281), R367 (= R370)
- binding pyridoxal-5'-phosphate: G102 (= G105), T103 (≠ A106), F134 (= F138), H135 (= H139), E186 (= E190), D219 (= D223), V221 (= V225), Q222 (= Q226), K248 (= K252)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
45% identity, 96% coverage: 13:393/398 of query aligns to 2:382/385 of Q9X2A5
- GT 94:95 (≠ GA 105:106) binding pyridoxal 5'-phosphate
- T268 (= T281) binding pyridoxal 5'-phosphate
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
44% identity, 94% coverage: 8:382/398 of query aligns to 6:384/400 of 4addA
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T281), R372 (= R370)
- binding pyridoxal-5'-phosphate: G103 (= G105), A104 (= A106), F136 (= F138), H137 (= H139), D221 (= D223), V223 (= V225), K250 (= K252)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y18), F136 (= F138), R139 (= R141)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
44% identity, 94% coverage: 8:382/398 of query aligns to 6:384/401 of 4adbB
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T281), R372 (= R370)
- binding pyridoxal-5'-phosphate: S102 (= S104), G103 (= G105), A104 (= A106), F136 (= F138), H137 (= H139), D221 (= D223), V223 (= V225), Q224 (= Q226), K250 (= K252)
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, 97% coverage: 3:390/398 of query aligns to 58:450/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
43% identity, 94% coverage: 11:384/398 of query aligns to 9:386/402 of 4jevB
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T279 (= T281), R372 (= R370)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I48), S102 (= S104), G103 (= G105), T104 (≠ A106), F136 (= F138), H137 (= H139), E188 (= E190), E193 (= E195), D221 (= D223), V223 (= V225), Q224 (= Q226), K250 (= K252), R372 (= R370)
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)
43% identity, 94% coverage: 11:384/398 of query aligns to 14:391/405 of P40732
- GT 108:109 (≠ GA 105:106) binding pyridoxal 5'-phosphate
- K255 (= K252) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T281) 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)
44% identity, 97% coverage: 8:393/398 of query aligns to 5:383/390 of A0QYS9
- K304 (≠ A313) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
42% identity, 94% coverage: 11:384/398 of query aligns to 9:381/397 of 4jewA
- active site: F136 (= F138), E188 (= E190), D221 (= D223), Q224 (= Q226), K250 (= K252), T274 (= T281), R367 (= R370)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G105), T104 (≠ A106), F136 (= F138), H137 (= H139), R139 (= R141), E188 (= E190), E193 (= E195), D221 (= D223), V223 (= V225), K250 (= K252)
- binding picric acid: K25 (≠ R27), K27 (≠ E29), W32 (= W34)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
42% identity, 94% coverage: 11:384/398 of query aligns to 3:375/389 of 2pb0A
- active site: F130 (= F138), E182 (= E190), D215 (= D223), Q218 (= Q226), K244 (= K252), T268 (= T281), R361 (= R370)
- binding pyridoxal-5'-phosphate: S96 (= S104), G97 (= G105), T98 (≠ A106), F130 (= F138), H131 (= H139), E182 (= E190), D215 (= D223), V217 (= V225), Q218 (= Q226), K244 (= K252)
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
45% identity, 97% coverage: 8:393/398 of query aligns to 13:393/400 of P9WPZ7
- K314 (≠ A313) 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, 97% coverage: 8:393/398 of query aligns to 7:387/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
45% identity, 97% coverage: 8:393/398 of query aligns to 7:387/391 of 7nn4A
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
40% identity, 94% coverage: 13:385/398 of query aligns to 3:377/388 of 3nx3A
- active site: F127 (= F138), E179 (= E190), D212 (= D223), Q215 (= Q226), K241 (= K252), T271 (= T281), R362 (= R370)
- binding magnesium ion: N191 (≠ S202), F194 (≠ Y205), I313 (≠ A323), F316 (≠ Y326), D317 (≠ P327), C319 (≠ A329), Q370 (≠ T378), K371 (= K379)
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
41% identity, 95% coverage: 18:394/398 of query aligns to 24:395/395 of Q5SHH5
- GT 113:114 (≠ GA 105:106) binding pyridoxal 5'-phosphate
- K254 (= K252) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T281) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
41% identity, 95% coverage: 18:394/398 of query aligns to 16:387/387 of 1wkhA
- active site: F132 (= F138), E184 (= E190), D217 (= D223), Q220 (= Q226), K246 (= K252), T275 (= T281), R363 (= R370)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I48), S104 (= S104), G105 (= G105), T106 (≠ A106), F132 (= F138), S133 (≠ H139), E184 (= E190), E189 (= E195), D217 (= D223), I219 (≠ V225), K246 (= K252), R363 (= R370)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
41% identity, 95% coverage: 18:394/398 of query aligns to 16:387/387 of 1wkgA
- active site: F132 (= F138), E184 (= E190), D217 (= D223), Q220 (= Q226), K246 (= K252), T275 (= T281), R363 (= R370)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (= Y18), Y46 (≠ I48), G105 (= G105), T106 (≠ A106), F132 (= F138), S133 (≠ H139), R135 (= R141), E184 (= E190), D217 (= D223), I219 (≠ V225), Q220 (= Q226), K246 (= K252), G273 (= G279), T274 (≠ S280), T275 (= T281)
Sites not aligning to the query:
Query Sequence
>WP_011736998.1 NCBI__GCF_000015045.1:WP_011736998.1
MNSEQWIEKSDRYIMKNYGRFPLVPLRGEGCRLWDADGREYLDFLGGIAVNNLGHCPPKV
VEALRRQAGEMIHCSNLYQIPRQIELAELLCQNSFADKAFFCNSGAEANEAAIKLARKYS
RDNFGPERFAIITATDSFHGRTMATVSATGQEKVQRFFDPLLHGFSHVPFNDPAALEAAI
TPATCAIMLEPIQGESGVNIPSSDYFREVRRICDEYNLLLIFDEVQVGMGRTGRLFAYEN
FDCTPDIMTLAKALAGGAPIGAMLAKDEIAASFTPGTHGSTFGGNPLVCAAAVATLRVML
DEDILARTRETGAYLMAELEKLAQTYPFAGPVRGIGLMVGMPLSIPAGDIVRKGHERGVL
LNAVHDTVLRFVPPLIVTKQEVDQMIFILDGILAEVEA
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