SitesBLAST
Comparing WP_011606299.1 NCBI__GCF_000058485.1:WP_011606299.1 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)
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
60% identity, 96% coverage: 5:400/413 of query aligns to 3:388/390 of A0QYS9
- K304 (≠ D316) 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)
59% identity, 95% coverage: 2:395/413 of query aligns to 8:393/400 of P9WPZ7
- K314 (≠ D316) 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
59% identity, 95% coverage: 2:395/413 of query aligns to 2:387/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
59% identity, 95% coverage: 2:395/413 of query aligns to 2:387/391 of 7nn4A
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
50% identity, 92% coverage: 12:389/413 of query aligns to 9:384/390 of 8ht4B
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
43% identity, 93% coverage: 13:395/413 of query aligns to 11:390/393 of 2ordA
- active site: F134 (= F141), E186 (= E193), D219 (= D226), Q222 (= Q229), K248 (= K255), T276 (= T284), R367 (= R372)
- binding pyridoxal-5'-phosphate: G102 (= G115), T103 (≠ A116), F134 (= F141), H135 (= H142), E186 (= E193), D219 (= D226), V221 (= V228), Q222 (= Q229), K248 (= K255)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
43% identity, 93% coverage: 13:395/413 of query aligns to 3:382/385 of Q9X2A5
- GT 94:95 (≠ GA 115:116) binding pyridoxal 5'-phosphate
- T268 (= T284) binding pyridoxal 5'-phosphate
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
44% identity, 92% coverage: 2:383/413 of query aligns to 28:413/429 of P73133
- Y39 (= Y17) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S114) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G115) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A116) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R144) 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 (= E198) 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 (= D226) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q229) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K255) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T284) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R372) 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.
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, 93% coverage: 1:385/413 of query aligns to 57:443/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
39% identity, 93% coverage: 13:395/413 of query aligns to 4:376/376 of O66442
- GT 96:97 (≠ GA 115:116) binding pyridoxal 5'-phosphate
- K242 (= K255) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T284) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
39% identity, 93% coverage: 13:395/413 of query aligns to 3:375/375 of 2eh6A
- active site: F127 (= F141), E179 (= E193), D212 (= D226), Q215 (= Q229), K241 (= K255), T270 (= T284), R352 (= R372)
- binding pyridoxal-5'-phosphate: G95 (= G115), T96 (≠ A116), F127 (= F141), H128 (= H142), E179 (= E193), D212 (= D226), V214 (= V228), K241 (= K255)
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
40% identity, 92% coverage: 17:395/413 of query aligns to 24:394/395 of Q5SHH5
- GT 113:114 (≠ GA 115:116) binding pyridoxal 5'-phosphate
- K254 (= K255) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T284) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
40% identity, 92% coverage: 17:395/413 of query aligns to 16:386/387 of 1wkhA
- active site: F132 (= F141), E184 (= E193), D217 (= D226), Q220 (= Q229), K246 (= K255), T275 (= T284), R363 (= R372)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I47), S104 (= S114), G105 (= G115), T106 (≠ A116), F132 (= F141), S133 (≠ H142), E184 (= E193), E189 (= E198), D217 (= D226), I219 (≠ V228), K246 (= K255), R363 (= R372)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
40% identity, 92% coverage: 17:395/413 of query aligns to 16:386/387 of 1wkgA
- active site: F132 (= F141), E184 (= E193), D217 (= D226), Q220 (= Q229), K246 (= K255), T275 (= T284), R363 (= R372)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (= Y17), Y46 (≠ I47), G105 (= G115), T106 (≠ A116), F132 (= F141), S133 (≠ H142), R135 (= R144), E184 (= E193), D217 (= D226), I219 (≠ V228), Q220 (= Q229), K246 (= K255), G273 (= G282), T274 (≠ S283), T275 (= T284)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
40% identity, 92% coverage: 17:395/413 of query aligns to 16:386/387 of 1vefA
- active site: F132 (= F141), D217 (= D226), K246 (= K255), T275 (= T284), R363 (= R372)
- binding pyridoxal-5'-phosphate: G105 (= G115), T106 (≠ A116), F132 (= F141), S133 (≠ H142), E184 (= E193), D217 (= D226), I219 (≠ V228), K246 (= K255)
Sites not aligning to the query:
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
39% identity, 90% coverage: 25:395/413 of query aligns to 24:399/400 of 4addA
- active site: F136 (= F141), E188 (= E193), D221 (= D226), Q224 (= Q229), K250 (= K255), T279 (= T284), R372 (= R372)
- binding pyridoxal-5'-phosphate: G103 (= G115), A104 (= A116), F136 (= F141), H137 (= H142), D221 (= D226), V223 (= V228), K250 (= K255)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: F136 (= F141), R139 (= R144)
Sites not aligning to the query:
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
39% identity, 90% coverage: 25:395/413 of query aligns to 24:399/401 of 4adbB
- active site: F136 (= F141), E188 (= E193), D221 (= D226), Q224 (= Q229), K250 (= K255), T279 (= T284), R372 (= R372)
- binding pyridoxal-5'-phosphate: S102 (= S114), G103 (= G115), A104 (= A116), F136 (= F141), H137 (= H142), D221 (= D226), V223 (= V228), Q224 (= Q229), K250 (= K255)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
39% identity, 92% coverage: 2:383/413 of query aligns to 1:383/402 of 4jevB
- active site: F136 (= F141), E188 (= E193), D221 (= D226), Q224 (= Q229), K250 (= K255), T279 (= T284), R372 (= R372)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I47), S102 (= S114), G103 (= G115), T104 (≠ A116), F136 (= F141), H137 (= H142), E188 (= E193), E193 (= E198), D221 (= D226), V223 (= V228), Q224 (= Q229), K250 (= K255), R372 (= R372)
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)
39% identity, 92% coverage: 2:383/413 of query aligns to 6:388/405 of P40732
- GT 108:109 (≠ GA 115:116) binding pyridoxal 5'-phosphate
- K255 (= K255) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T284) binding pyridoxal 5'-phosphate
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
36% identity, 92% coverage: 13:391/413 of query aligns to 4:381/388 of 3nx3A
- active site: F127 (= F141), E179 (= E193), D212 (= D226), Q215 (= Q229), K241 (= K255), T271 (= T284), R362 (= R372)
- binding magnesium ion: N191 (≠ P205), F194 (≠ Y208), I313 (≠ A324), F316 (≠ I327), D317 (≠ P328), C319 (≠ V330), Q370 (≠ T380), K371 (≠ D381)
Query Sequence
>WP_011606299.1 NCBI__GCF_000058485.1:WP_011606299.1
MTADLLARRDAVVMATYGRPTISLVRGQGTRVWDDAGREYLDLLGGIAVSVLGHGHPAIR
AAVVDQFDTLGHVSNLYANEPQVRLAERLVELLAAGAPAPGLPAGGAKTFFANSGAEANE
AAIKIARRTGRPEIIAAEGAFHGRTLGALSITGQPAKRAPFEPLLPGVRFVPYGDAAALR
AAVGERTAAVFLEPTLGEAGVVPPPPGYLAQARAACDDAGALLVFDEVQSGIGRTGSWFA
HQAAGVQPDIVTLAKGLGGGLPIGACIGIGAAADLLRPGDHGSTFGGGPIVCAAALAVLD
TIAAEGLLDHATRLGDRLAAQIVAAGIPGVIGVRGVGLWRAIELDGPFAPAVETAARAAG
YLVNAVAPDAVRLAPPLILTDAEADAFAAALPAIVGAARDGASLSERASKVTA
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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