SitesBLAST
Comparing WP_012383166.1 NCBI__GCF_000019845.1:WP_012383166.1 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)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
43% identity, 95% coverage: 5:390/405 of query aligns to 12:400/402 of 4jevB
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T279 (= T272), R372 (= R362)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I39), S102 (= S95), G103 (= G96), T104 (≠ A97), F136 (= F129), H137 (= H130), E188 (= E181), E193 (= E186), D221 (= D214), V223 (= V216), Q224 (= Q217), K250 (= K243), R372 (= R362)
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, 95% coverage: 5:390/405 of query aligns to 17:405/405 of P40732
- GT 108:109 (≠ GA 96:97) binding pyridoxal 5'-phosphate
- K255 (= K243) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T272) binding pyridoxal 5'-phosphate
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
44% identity, 96% coverage: 5:391/405 of query aligns to 12:401/401 of 4adbB
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T279 (= T272), R372 (= R362)
- binding pyridoxal-5'-phosphate: S102 (= S95), G103 (= G96), A104 (= A97), F136 (= F129), H137 (= H130), D221 (= D214), V223 (= V216), Q224 (= Q217), K250 (= K243)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
44% identity, 94% coverage: 5:385/405 of query aligns to 12:395/400 of 4addA
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T279 (= T272), R372 (= R362)
- binding pyridoxal-5'-phosphate: G103 (= G96), A104 (= A97), F136 (= F129), H137 (= H130), D221 (= D214), V223 (= V216), K250 (= K243)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y9), F136 (= F129), R139 (= R132)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
43% identity, 95% coverage: 3:388/405 of query aligns to 33:428/429 of P73133
- Y39 (= Y9) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S95) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G96) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A97) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R132) 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 (= E186) 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 (= D214) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q217) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K243) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T272) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R362) 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)
45% identity, 93% coverage: 5:381/405 of query aligns to 3:378/385 of Q9X2A5
- GT 94:95 (≠ GA 96:97) binding pyridoxal 5'-phosphate
- T268 (= T272) 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
45% identity, 93% coverage: 5:381/405 of query aligns to 11:386/393 of 2ordA
- active site: F134 (= F129), E186 (= E181), D219 (= D214), Q222 (= Q217), K248 (= K243), T276 (= T272), R367 (= R362)
- binding pyridoxal-5'-phosphate: G102 (= G96), T103 (≠ A97), F134 (= F129), H135 (= H130), E186 (= E181), D219 (= D214), V221 (= V216), Q222 (= Q217), K248 (= K243)
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
42% identity, 94% coverage: 3:381/405 of query aligns to 1:371/375 of 2eh6A
- active site: F127 (= F129), E179 (= E181), D212 (= D214), Q215 (= Q217), K241 (= K243), T270 (= T272), R352 (= R362)
- binding pyridoxal-5'-phosphate: G95 (= G96), T96 (≠ A97), F127 (= F129), H128 (= H130), E179 (= E181), D212 (= D214), V214 (= V216), K241 (= K243)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
42% identity, 94% coverage: 3:381/405 of query aligns to 2:372/376 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
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
42% identity, 95% coverage: 5:390/405 of query aligns to 12:395/397 of 4jewA
- active site: F136 (= F129), E188 (= E181), D221 (= D214), Q224 (= Q217), K250 (= K243), T274 (= T272), R367 (= R362)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G96), T104 (≠ A97), F136 (= F129), H137 (= H130), R139 (= R132), E188 (= E181), E193 (= E186), D221 (= D214), V223 (= V216), K250 (= K243)
- binding picric acid: K25 (≠ R18), K27 (≠ E20), W32 (≠ T25)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
42% identity, 95% coverage: 5:390/405 of query aligns to 6:389/389 of 2pb0A
- active site: F130 (= F129), E182 (= E181), D215 (= D214), Q218 (= Q217), K244 (= K243), T268 (= T272), R361 (= R362)
- binding pyridoxal-5'-phosphate: S96 (= S95), G97 (= G96), T98 (≠ A97), F130 (= F129), H131 (= H130), E182 (= E181), D215 (= D214), V217 (= V216), Q218 (= Q217), K244 (= K243)
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)
44% identity, 94% coverage: 8:388/405 of query aligns to 72:456/457 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
41% identity, 94% coverage: 3:384/405 of query aligns to 2:384/388 of 3nx3A
- active site: F127 (= F129), E179 (= E181), D212 (= D214), Q215 (= Q217), K241 (= K243), T271 (= T272), R362 (= R362)
- binding magnesium ion: N191 (≠ S193), F194 (= F196), I313 (≠ R314), F316 (≠ H317), D317 (≠ E319), C319 (≠ I321), Q370 (≠ G370), K371 (≠ E371)
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
41% identity, 94% coverage: 5:383/405 of query aligns to 11:381/390 of A0QYS9
- K304 (≠ V304) 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)
38% identity, 93% coverage: 5:381/405 of query aligns to 10:385/390 of 8ht4B
P9WPZ7 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
41% identity, 94% coverage: 5:383/405 of query aligns to 19:391/400 of P9WPZ7
- K314 (≠ V304) 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, 94% coverage: 5:383/405 of query aligns to 13:385/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
41% identity, 94% coverage: 5:383/405 of query aligns to 13:385/391 of 7nn4A
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
35% identity, 94% coverage: 8:386/405 of query aligns to 23:395/395 of Q5SHH5
- GT 113:114 (≠ GA 96:97) binding pyridoxal 5'-phosphate
- K254 (= K243) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T272) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
35% identity, 94% coverage: 8:386/405 of query aligns to 15:387/387 of 1wkhA
- active site: F132 (= F129), E184 (= E181), D217 (= D214), Q220 (= Q217), K246 (= K243), T275 (= T272), R363 (= R362)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I39), S104 (= S95), G105 (= G96), T106 (≠ A97), F132 (= F129), S133 (≠ H130), E184 (= E181), E189 (= E186), D217 (= D214), I219 (≠ V216), K246 (= K243), R363 (= R362)
Sites not aligning to the query:
Query Sequence
>WP_012383166.1 NCBI__GCF_000019845.1:WP_012383166.1
MTSSLLPTYARAPIAFERGEGAWLTSTTGERFLDFGGGIAVASLGYSHPHLIKALHEQGD
KLWHTSNLFQIPQAERLAERLTAVSFADFVFFTNSGAEAMEGVIKTARKYHAACGHPEKN
RIITFQGAFHGRTLATIAAAGNEKYLDGFEPRLPGFDNVPFGDLEAVKAAIKPETGAILI
EPIQGEGGIRVVSPDFLQALRKLCDEQGLLLLLDEVQSGVGRSGKLFAYEWAGVEPDVMA
IAKGIGGGFPLGAFMATREAAKGMVVGTHGSTYGGNPLATSIGNAVLDIVLEPSFLAHVE
ATGVLLQQRLVALRERHPEVIAELRGAGLMRGIKVTLPVADFAAAARAEKLLVIPAGDNV
VRLLPPLIIGEEEVDGAIERLDAACAALKARINANSSSLLSGAAE
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