SitesBLAST
Comparing WP_037570915.1 NCBI__GCF_000744815.1:WP_037570915.1 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)
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
61% identity, 98% coverage: 7:392/395 of query aligns to 3:388/390 of A0QYS9
- K304 (≠ E308) 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)
62% identity, 98% coverage: 2:387/395 of query aligns to 6:393/400 of P9WPZ7
- K314 (≠ E308) 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
63% identity, 96% coverage: 7:387/395 of query aligns to 5:387/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
63% identity, 96% coverage: 7:387/395 of query aligns to 5:387/391 of 7nn4A
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
53% identity, 95% coverage: 9:382/395 of query aligns to 4:385/390 of 8ht4B
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
41% identity, 94% coverage: 15:387/395 of query aligns to 4:376/376 of O66442
- GT 96:97 (≠ GA 107:108) binding pyridoxal 5'-phosphate
- K242 (= K247) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T276) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
41% identity, 94% coverage: 15:387/395 of query aligns to 3:375/375 of 2eh6A
- active site: F127 (= F133), E179 (= E185), D212 (= D218), Q215 (= Q221), K241 (= K247), T270 (= T276), R352 (= R364)
- binding pyridoxal-5'-phosphate: G95 (= G107), T96 (≠ A108), F127 (= F133), H128 (= H134), E179 (= E185), D212 (= D218), V214 (= V220), K241 (= K247)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
42% identity, 93% coverage: 8:375/395 of query aligns to 28:413/429 of P73133
- Y39 (= Y19) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S106) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G107) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A108) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R136) 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 (= E190) 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 (= D218) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q221) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K247) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T276) 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.
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
41% identity, 95% coverage: 15:390/395 of query aligns to 3:385/385 of Q9X2A5
- GT 94:95 (≠ GA 107:108) binding pyridoxal 5'-phosphate
- T268 (= T276) 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
41% identity, 95% coverage: 15:390/395 of query aligns to 11:393/393 of 2ordA
- active site: F134 (= F133), E186 (= E185), D219 (= D218), Q222 (= Q221), K248 (= K247), T276 (= T276), R367 (= R364)
- binding pyridoxal-5'-phosphate: G102 (= G107), T103 (≠ A108), F134 (= F133), H135 (= H134), E186 (= E185), D219 (= D218), V221 (= V220), Q222 (= Q221), K248 (= K247)
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
45% identity, 93% coverage: 19:387/395 of query aligns to 24:394/395 of Q5SHH5
- GT 113:114 (≠ GA 107:108) binding pyridoxal 5'-phosphate
- K254 (= K247) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T276) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
45% identity, 93% coverage: 19:387/395 of query aligns to 16:386/387 of 1wkhA
- active site: F132 (= F133), E184 (= E185), D217 (= D218), Q220 (= Q221), K246 (= K247), T275 (= T276), R363 (= R364)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I49), S104 (= S106), G105 (= G107), T106 (≠ A108), F132 (= F133), S133 (≠ H134), E184 (= E185), E189 (= E190), D217 (= D218), I219 (≠ V220), K246 (= K247), R363 (= R364)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
45% identity, 93% coverage: 19:387/395 of query aligns to 16:386/387 of 1wkgA
- active site: F132 (= F133), E184 (= E185), D217 (= D218), Q220 (= Q221), K246 (= K247), T275 (= T276), R363 (= R364)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (= Y19), Y46 (≠ I49), G105 (= G107), T106 (≠ A108), F132 (= F133), S133 (≠ H134), R135 (= R136), E184 (= E185), D217 (= D218), I219 (≠ V220), Q220 (= Q221), K246 (= K247), G273 (= G274), T274 (= T275), T275 (= T276)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
45% identity, 93% coverage: 19:387/395 of query aligns to 16:386/387 of 1vefA
- active site: F132 (= F133), D217 (= D218), K246 (= K247), T275 (= T276), R363 (= R364)
- binding pyridoxal-5'-phosphate: G105 (= G107), T106 (≠ A108), F132 (= F133), S133 (≠ H134), E184 (= E185), D217 (= D218), I219 (≠ V220), K246 (= K247)
Sites not aligning to the query:
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
42% identity, 89% coverage: 22:373/395 of query aligns to 20:381/401 of 4adbB
- active site: F136 (= F133), E188 (= E185), D221 (= D218), Q224 (= Q221), K250 (= K247), T279 (= T276), R372 (= R364)
- binding pyridoxal-5'-phosphate: S102 (= S106), G103 (= G107), A104 (= A108), F136 (= F133), H137 (= H134), D221 (= D218), V223 (= V220), Q224 (= Q221), K250 (= K247)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
42% identity, 89% coverage: 22:373/395 of query aligns to 20:381/400 of 4addA
- active site: F136 (= F133), E188 (= E185), D221 (= D218), Q224 (= Q221), K250 (= K247), T279 (= T276), R372 (= R364)
- binding pyridoxal-5'-phosphate: G103 (= G107), A104 (= A108), F136 (= F133), H137 (= H134), D221 (= D218), V223 (= V220), K250 (= K247)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: F136 (= F133), R139 (= R136)
Sites not aligning to the query:
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)
38% identity, 96% coverage: 4:383/395 of query aligns to 58:449/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
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)
40% identity, 89% coverage: 24:375/395 of query aligns to 27:388/405 of P40732
- GT 108:109 (≠ GA 107:108) binding pyridoxal 5'-phosphate
- K255 (= K247) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T276) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
40% identity, 89% coverage: 24:375/395 of query aligns to 22:383/402 of 4jevB
- active site: F136 (= F133), E188 (= E185), D221 (= D218), Q224 (= Q221), K250 (= K247), T279 (= T276), R372 (= R364)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I49), S102 (= S106), G103 (= G107), T104 (≠ A108), F136 (= F133), H137 (= H134), E188 (= E185), E193 (= E190), D221 (= D218), V223 (= V220), Q224 (= Q221), K250 (= K247), R372 (= R364)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
39% identity, 89% coverage: 24:375/395 of query aligns to 16:372/389 of 2pb0A
- active site: F130 (= F133), E182 (= E185), D215 (= D218), Q218 (= Q221), K244 (= K247), T268 (= T276), R361 (= R364)
- binding pyridoxal-5'-phosphate: S96 (= S106), G97 (= G107), T98 (≠ A108), F130 (= F133), H131 (= H134), E182 (= E185), D215 (= D218), V217 (= V220), Q218 (= Q221), K244 (= K247)
Query Sequence
>WP_037570915.1 NCBI__GCF_000744815.1:WP_037570915.1
MTGNQELTQRWQQSLMNNYGTPRIPLARGEGAHVWDADGKRYTDLVAGIAVNALGHGHPA
VVGAVTEQINTLGHVSNLFIAEPPVRLSERLLELFGRPGRVFFCNSGAEANEGAFKIGRL
TGRRHMVATTGGFHGRTMGALSLTGQPGKQDGFAPLPGDVEFVPYGDVEALRAAVTEETA
FFIVEPVQGENGAVPAPDGYLEAAREITRAKGALLVVDEVQTGIGRTGHWFAHQAAGIEP
DVVTLAKGLGGGLPIGATVAFGAAAELLQPGQHGTTFGGNPVCCAAGLAVLDTIAQDGLL
DHVKRVGERLRSGIESIGDPLVARVRGTGLLLGIVLTEPLAPQVQAAAQRAGFLVNATGP
DLVRLVPPLTLPEVDADAFLAVLPGILRSVREAGA
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