SitesBLAST
Comparing WP_013258689.1 NCBI__GCF_000143965.1:WP_013258689.1 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)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
46% identity, 97% coverage: 7:391/398 of query aligns to 31:426/429 of P73133
- Y39 (= Y15) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S101) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G102) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A103) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R137) 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 (= E191) 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 (= D219) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q222) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K248) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T277) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R367) 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, 96% coverage: 10:390/398 of query aligns to 10:390/393 of 2ordA
- active site: F134 (= F134), E186 (= E186), D219 (= D219), Q222 (= Q222), K248 (= K248), T276 (= T277), R367 (= R367)
- binding pyridoxal-5'-phosphate: G102 (= G102), T103 (≠ A103), F134 (= F134), H135 (= H135), E186 (= E186), D219 (= D219), V221 (≠ I221), Q222 (= Q222), K248 (= K248)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
44% identity, 96% coverage: 10:390/398 of query aligns to 2:382/385 of Q9X2A5
- GT 94:95 (≠ GA 102:103) binding pyridoxal 5'-phosphate
- T268 (= T277) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
44% identity, 96% coverage: 10:390/398 of query aligns to 2:375/375 of 2eh6A
- active site: F127 (= F134), E179 (= E186), D212 (= D219), Q215 (= Q222), K241 (= K248), T270 (= T277), R352 (= R367)
- binding pyridoxal-5'-phosphate: G95 (= G102), T96 (≠ A103), F127 (= F134), H128 (= H135), E179 (= E186), D212 (= D219), V214 (≠ I221), K241 (= K248)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
44% identity, 96% coverage: 10:390/398 of query aligns to 3:376/376 of O66442
- GT 96:97 (≠ GA 102:103) binding pyridoxal 5'-phosphate
- K242 (= K248) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T277) 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)
45% identity, 98% coverage: 1:390/398 of query aligns to 1:383/390 of A0QYS9
- K304 (= K309) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
42% identity, 98% coverage: 3:394/398 of query aligns to 4:396/401 of 4adbB
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T277), R372 (= R367)
- binding pyridoxal-5'-phosphate: S102 (= S101), G103 (= G102), A104 (= A103), F136 (= F134), H137 (= H135), D221 (= D219), V223 (≠ I221), Q224 (= Q222), K250 (= K248)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
42% identity, 98% coverage: 3:394/398 of query aligns to 4:396/400 of 4addA
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T277), R372 (= R367)
- binding pyridoxal-5'-phosphate: G103 (= G102), A104 (= A103), F136 (= F134), H137 (= H135), D221 (= D219), V223 (≠ I221), K250 (= K248)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y15), F136 (= F134), R139 (= R137)
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
45% identity, 98% coverage: 2:390/398 of query aligns to 10:393/400 of P9WPZ7
- K314 (= K309) 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, 98% coverage: 2:390/398 of query aligns to 4:387/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
45% identity, 98% coverage: 2:390/398 of query aligns to 4:387/391 of 7nn4A
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
44% identity, 98% coverage: 2:391/398 of query aligns to 1:390/390 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)
40% identity, 98% coverage: 3:392/398 of query aligns to 58:455/457 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
39% identity, 96% coverage: 10:392/398 of query aligns to 3:387/388 of 3nx3A
- active site: F127 (= F134), E179 (= E186), D212 (= D219), Q215 (= Q222), K241 (= K248), T271 (= T277), R362 (= R367)
- binding magnesium ion: N191 (≠ P198), F194 (≠ Y201), I313 (≠ C319), F316 (≠ Y322), D317 (≠ P323), C319 (≠ H325), Q370 (≠ E375), K371 (≠ D376)
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)
37% identity, 95% coverage: 3:379/398 of query aligns to 9:389/405 of P40732
- GT 108:109 (≠ GA 102:103) binding pyridoxal 5'-phosphate
- K255 (= K248) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T277) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
37% identity, 95% coverage: 3:379/398 of query aligns to 4:384/402 of 4jevB
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T279 (= T277), R372 (= R367)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I45), S102 (= S101), G103 (= G102), T104 (≠ A103), F136 (= F134), H137 (= H135), E188 (= E186), E193 (= E191), D221 (= D219), V223 (≠ I221), Q224 (= Q222), K250 (= K248), R372 (= R367)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
37% identity, 95% coverage: 3:379/398 of query aligns to 4:379/397 of 4jewA
- active site: F136 (= F134), E188 (= E186), D221 (= D219), Q224 (= Q222), K250 (= K248), T274 (= T277), R367 (= R367)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G102), T104 (≠ A103), F136 (= F134), H137 (= H135), R139 (= R137), E188 (= E186), E193 (= E191), D221 (= D219), V223 (≠ I221), K250 (= K248)
- binding picric acid: K25 (≠ R24), K27 (≠ E26), W32 (= W31)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
37% identity, 94% coverage: 7:379/398 of query aligns to 2:373/389 of 2pb0A
- active site: F130 (= F134), E182 (= E186), D215 (= D219), Q218 (= Q222), K244 (= K248), T268 (= T277), R361 (= R367)
- binding pyridoxal-5'-phosphate: S96 (= S101), G97 (= G102), T98 (≠ A103), F130 (= F134), H131 (= H135), E182 (= E186), D215 (= D219), V217 (≠ I221), Q218 (= Q222), K244 (= K248)
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
39% identity, 95% coverage: 15:391/398 of query aligns to 24:395/395 of Q5SHH5
- GT 113:114 (≠ GA 102:103) binding pyridoxal 5'-phosphate
- K254 (= K248) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T277) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
39% identity, 95% coverage: 15:391/398 of query aligns to 16:387/387 of 1wkhA
- active site: F132 (= F134), E184 (= E186), D217 (= D219), Q220 (= Q222), K246 (= K248), T275 (= T277), R363 (= R367)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I45), S104 (= S101), G105 (= G102), T106 (≠ A103), F132 (= F134), S133 (≠ H135), E184 (= E186), E189 (= E191), D217 (= D219), I219 (= I221), K246 (= K248), R363 (= R367)
Sites not aligning to the query:
Query Sequence
>WP_013258689.1 NCBI__GCF_000143965.1:WP_013258689.1
MTSQEKIDQYVMQTYGRFPVTFVRGEGCLLWDDQGKSYIDFLAGIAVCGLGHANPEVAEA
VCAQAKKLLHVSNLFYTEPQARVAELLVQNSFADRVFFCNSGAEANEGALKLSRLWGKAF
KDGAHEVVTIQGSFHGRTIATLSATGQEKIQKGYDPLVSRFKYAPWGDLEAITAAVDEKV
CAVMLEPILGEGGVVPPPEGYLPAVRRLCDKTGTMLIFDEIQTGLGRTGKLFAHEHFGVK
PDVMTLAKGLGNGLPVGAVCATSEAAALFQPGSHATTFGAGPLIMEAARVVLETLLRPGF
LERVQQAGKKLRKGLEGLCQKYPGHKLEARGLGLMRALILPTPGATVVKKMLQRGFVINC
TQDKILRFVPPLIIEDAHIDALIGALDEMLAAGEIAAG
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