SitesBLAST
Comparing WP_052293610.1 NCBI__GCF_000010725.1:WP_052293610.1 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)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
44% identity, 99% coverage: 1:383/385 of query aligns to 13:395/401 of 4adbB
- active site: F136 (= F124), E188 (= E176), D221 (= D209), Q224 (= Q212), K250 (= K238), T279 (= T267), R372 (= R357)
- binding pyridoxal-5'-phosphate: S102 (= S90), G103 (= G91), A104 (= A92), F136 (= F124), H137 (= H125), D221 (= D209), V223 (≠ I211), Q224 (= Q212), K250 (= K238)
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
44% identity, 99% coverage: 1:381/385 of query aligns to 12:391/393 of 2ordA
- active site: F134 (= F124), E186 (= E176), D219 (= D209), Q222 (= Q212), K248 (= K238), T276 (= T267), R367 (= R357)
- binding pyridoxal-5'-phosphate: G102 (= G91), T103 (≠ A92), F134 (= F124), H135 (= H125), E186 (= E176), D219 (= D209), V221 (≠ I211), Q222 (= Q212), K248 (= K238)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
44% identity, 99% coverage: 1:383/385 of query aligns to 13:395/400 of 4addA
- active site: F136 (= F124), E188 (= E176), D221 (= D209), Q224 (= Q212), K250 (= K238), T279 (= T267), R372 (= R357)
- binding pyridoxal-5'-phosphate: G103 (= G91), A104 (= A92), F136 (= F124), H137 (= H125), D221 (= D209), V223 (≠ I211), K250 (= K238)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y4), F136 (= F124), R139 (= R127)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
44% identity, 99% coverage: 1:381/385 of query aligns to 4:383/385 of Q9X2A5
- GT 94:95 (≠ GA 91:92) binding pyridoxal 5'-phosphate
- T268 (= T267) binding pyridoxal 5'-phosphate
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)
44% identity, 99% coverage: 1:381/385 of query aligns to 18:398/405 of P40732
- GT 108:109 (≠ GA 91:92) binding pyridoxal 5'-phosphate
- K255 (= K238) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T267) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
44% identity, 99% coverage: 1:381/385 of query aligns to 13:393/402 of 4jevB
- active site: F136 (= F124), E188 (= E176), D221 (= D209), Q224 (= Q212), K250 (= K238), T279 (= T267), R372 (= R357)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (≠ V34), S102 (= S90), G103 (= G91), T104 (≠ A92), F136 (= F124), H137 (= H125), E188 (= E176), E193 (= E181), D221 (= D209), V223 (≠ I211), Q224 (= Q212), K250 (= K238), R372 (= R357)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
43% identity, 98% coverage: 1:376/385 of query aligns to 5:372/376 of O66442
- GT 96:97 (≠ GA 91:92) binding pyridoxal 5'-phosphate
- K242 (= K238) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T267) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
43% identity, 98% coverage: 1:376/385 of query aligns to 4:371/375 of 2eh6A
- active site: F127 (= F124), E179 (= E176), D212 (= D209), Q215 (= Q212), K241 (= K238), T270 (= T267), R352 (= R357)
- binding pyridoxal-5'-phosphate: G95 (= G91), T96 (≠ A92), F127 (= F124), H128 (= H125), E179 (= E176), D212 (= D209), V214 (≠ I211), K241 (= K238)
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, 98% coverage: 3:379/385 of query aligns to 72:452/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
44% identity, 99% coverage: 1:381/385 of query aligns to 7:382/389 of 2pb0A
- active site: F130 (= F124), E182 (= E176), D215 (= D209), Q218 (= Q212), K244 (= K238), T268 (= T267), R361 (= R357)
- binding pyridoxal-5'-phosphate: S96 (= S90), G97 (= G91), T98 (≠ A92), F130 (= F124), H131 (= H125), E182 (= E176), D215 (= D209), V217 (≠ I211), Q218 (= Q212), K244 (= K238)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
44% identity, 99% coverage: 1:381/385 of query aligns to 13:388/397 of 4jewA
- active site: F136 (= F124), E188 (= E176), D221 (= D209), Q224 (= Q212), K250 (= K238), T274 (= T267), R367 (= R357)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G91), T104 (≠ A92), F136 (= F124), H137 (= H125), R139 (= R127), E188 (= E176), E193 (= E181), D221 (= D209), V223 (≠ I211), K250 (= K238)
- binding picric acid: K25 (≠ R13), K27 (≠ E15), W32 (≠ Y20)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
42% identity, 98% coverage: 1:376/385 of query aligns to 36:421/429 of P73133
- Y39 (= Y4) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S90) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G91) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A92) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R127) 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 (= E181) 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 (= D209) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q212) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K238) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T267) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R357) 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.
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
41% identity, 96% coverage: 1:371/385 of query aligns to 5:376/388 of 3nx3A
- active site: F127 (= F124), E179 (= E176), D212 (= D209), Q215 (= Q212), K241 (= K238), T271 (= T267), R362 (= R357)
- binding magnesium ion: N191 (≠ S188), F194 (= F191), I313 (= I309), F316 (≠ H312), D317 (≠ P313), C319 (≠ L317), Q370 (≠ G365), K371 (≠ E366)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
42% identity, 98% coverage: 3:379/385 of query aligns to 13:388/390 of 8ht4B
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
39% identity, 99% coverage: 1:383/385 of query aligns to 12:390/390 of A0QYS9
- K304 (≠ G299) 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)
39% identity, 100% coverage: 1:385/385 of query aligns to 20:398/400 of P9WPZ7
- K314 (≠ G299) 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
40% identity, 98% coverage: 1:378/385 of query aligns to 14:389/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
40% identity, 98% coverage: 1:378/385 of query aligns to 14:389/391 of 7nn4A
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
36% identity, 96% coverage: 3:373/385 of query aligns to 23:387/395 of Q5SHH5
- GT 113:114 (≠ GA 91:92) binding pyridoxal 5'-phosphate
- K254 (= K238) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T267) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
35% identity, 96% coverage: 3:373/385 of query aligns to 15:379/387 of 1wkhA
- active site: F132 (= F124), E184 (= E176), D217 (= D209), Q220 (= Q212), K246 (= K238), T275 (= T267), R363 (= R357)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ V34), S104 (= S90), G105 (= G91), T106 (≠ A92), F132 (= F124), S133 (≠ H125), E184 (= E176), E189 (= E181), D217 (= D209), I219 (= I211), K246 (= K238), R363 (= R357)
Sites not aligning to the query:
Query Sequence
>WP_052293610.1 NCBI__GCF_000010725.1:WP_052293610.1
MPTYARADVVFERGEGPYLYATDGRRFLDFAAGVAVNALGHAHPYLVEKLTEQAGKLWHT
SNLFRVAGQESLGKRLTEVTFADTVFFTNSGAEAWECGAKTVRKYHYDSGNPQKNRIITF
EQAFHGRTLGAISAAKQEKLVHGFDPLLDGFDQVPFGDLDAVRAAITPATGGICVEPIQG
EGGIRAGSVEFLRGLRALCDEHGLLLFLDEIQCGMGRTGKLFAHEWAGITPDVMCVAKGI
GGGFPLGACLATERAAAGMTAGTHGSTYGGNPLATAVGNAVLDVMLAPGFLDEVRKTAGY
ARARLEELIAKHPAMFLDLRGQGLMLGLKLGQPVGEVVAKLRANGLLAVPAGDNVVRLLP
PLTIGEAEVNEAVGILDRTAQECVG
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