SitesBLAST
Comparing WP_009141315.1 NCBI__GCF_000225705.1:WP_009141315.1 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)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
40% identity, 97% coverage: 12:426/427 of query aligns to 2:376/376 of O66442
- GT 96:97 (≠ GA 137:138) binding pyridoxal 5'-phosphate
- K242 (= K286) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T315) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
40% identity, 97% coverage: 12:426/427 of query aligns to 1:375/375 of 2eh6A
- active site: F127 (= F169), E179 (= E224), D212 (= D257), Q215 (= Q260), K241 (= K286), T270 (= T315), R352 (= R403)
- binding pyridoxal-5'-phosphate: G95 (= G137), T96 (≠ A138), F127 (= F169), H128 (= H170), E179 (= E224), D212 (= D257), V214 (= V259), K241 (= K286)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
39% identity, 97% coverage: 13:426/427 of query aligns to 2:382/385 of Q9X2A5
- GT 94:95 (≠ GA 137:138) binding pyridoxal 5'-phosphate
- T268 (= T315) 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
39% identity, 97% coverage: 13:426/427 of query aligns to 10:390/393 of 2ordA
- active site: F134 (= F169), E186 (= E224), D219 (= D257), Q222 (= Q260), K248 (= K286), T276 (= T315), R367 (= R403)
- binding pyridoxal-5'-phosphate: G102 (= G137), T103 (≠ A138), F134 (= F169), H135 (= H170), E186 (= E224), D219 (= D257), V221 (= V259), Q222 (= Q260), K248 (= K286)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
37% identity, 97% coverage: 12:427/427 of query aligns to 33:426/429 of P73133
- Y39 (≠ F18) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S136) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G137) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A138) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R172) 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 (= E229) 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 (= D257) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q260) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K286) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T315) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R403) 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.
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
37% identity, 94% coverage: 25:427/427 of query aligns to 31:395/395 of Q5SHH5
- GT 113:114 (≠ GA 137:138) binding pyridoxal 5'-phosphate
- K254 (= K286) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T315) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 94% coverage: 25:427/427 of query aligns to 23:387/387 of 1wkhA
- active site: F132 (= F169), E184 (= E224), D217 (= D257), Q220 (= Q260), K246 (= K286), T275 (= T315), R363 (= R403)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I48), S104 (= S136), G105 (= G137), T106 (≠ A138), F132 (= F169), S133 (≠ H170), E184 (= E224), E189 (= E229), D217 (= D257), I219 (≠ V259), K246 (= K286), R363 (= R403)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 94% coverage: 25:427/427 of query aligns to 23:387/387 of 1wkgA
- active site: F132 (= F169), E184 (= E224), D217 (= D257), Q220 (= Q260), K246 (= K286), T275 (= T315), R363 (= R403)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ I48), G105 (= G137), T106 (≠ A138), F132 (= F169), S133 (≠ H170), R135 (= R172), E184 (= E224), D217 (= D257), I219 (≠ V259), Q220 (= Q260), K246 (= K286), G273 (= G313), T274 (= T314), T275 (= T315)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 94% coverage: 25:427/427 of query aligns to 23:387/387 of 1vefA
- active site: F132 (= F169), D217 (= D257), K246 (= K286), T275 (= T315), R363 (= R403)
- binding pyridoxal-5'-phosphate: G105 (= G137), T106 (≠ A138), F132 (= F169), S133 (≠ H170), E184 (= E224), D217 (= D257), I219 (≠ V259), K246 (= K286)
Sites not aligning to the query:
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
38% identity, 97% coverage: 14:427/427 of query aligns to 10:390/390 of 8ht4B
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
37% identity, 96% coverage: 13:424/427 of query aligns to 11:393/400 of 4addA
- active site: F136 (= F169), E188 (= E224), D221 (= D257), Q224 (= Q260), K250 (= K286), T279 (= T315), R372 (= R403)
- binding pyridoxal-5'-phosphate: G103 (= G137), A104 (= A138), F136 (= F169), H137 (= H170), D221 (= D257), V223 (= V259), K250 (= K286)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ F18), F136 (= F169), R139 (= R172)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
37% identity, 96% coverage: 13:424/427 of query aligns to 11:393/401 of 4adbB
- active site: F136 (= F169), E188 (= E224), D221 (= D257), Q224 (= Q260), K250 (= K286), T279 (= T315), R372 (= R403)
- binding pyridoxal-5'-phosphate: S102 (= S136), G103 (= G137), A104 (= A138), F136 (= F169), H137 (= H170), D221 (= D257), V223 (= V259), Q224 (= Q260), K250 (= K286)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
37% identity, 92% coverage: 22:415/427 of query aligns to 18:384/402 of 4jevB
- active site: F136 (= F169), E188 (= E224), D221 (= D257), Q224 (= Q260), K250 (= K286), T279 (= T315), R372 (= R403)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I48), S102 (= S136), G103 (= G137), T104 (≠ A138), F136 (= F169), H137 (= H170), E188 (= E224), E193 (= E229), D221 (= D257), V223 (= V259), Q224 (= Q260), K250 (= K286), R372 (= R403)
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, 92% coverage: 22:415/427 of query aligns to 23:389/405 of P40732
- GT 108:109 (≠ GA 137:138) binding pyridoxal 5'-phosphate
- K255 (= K286) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T315) 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)
38% identity, 99% coverage: 5:426/427 of query aligns to 3:383/390 of A0QYS9
- K304 (≠ D347) 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, 97% coverage: 11:426/427 of query aligns to 16:393/400 of P9WPZ7
- K314 (≠ D347) 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
39% identity, 97% coverage: 11:426/427 of query aligns to 10:387/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
39% identity, 97% coverage: 11:426/427 of query aligns to 10:387/391 of 7nn4A
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)
34% identity, 98% coverage: 10:426/427 of query aligns to 65:453/457 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
33% identity, 97% coverage: 11:426/427 of query aligns to 1:385/388 of 3nx3A
- active site: F127 (= F169), E179 (= E224), D212 (= D257), Q215 (= Q260), K241 (= K286), T271 (= T315), R362 (= R403)
- binding magnesium ion: N191 (≠ T236), F194 (= F239), I313 (≠ P357), F316 (≠ I360), D317 (= D361), C319 (vs. gap), Q370 (≠ E411), K371 (≠ R412)
Query Sequence
>WP_009141315.1 NCBI__GCF_000225705.1:WP_009141315.1
MSLGLQKALESSYVMNTFARMPVEFVEGHGMTLVGDDGTEYQDFLAGIGVCSLGHCHPVL
VEAIQRQAERLLHVSNYYYIERRGELAAILSKLASGDMDGALMIADAVRAGDEAAAVALG
SPTESDQIWKTFFANSGAEANEGAMKLARLYAKRSGNGGNTIVALRGSFHGRTLETIAAT
MQDRLQDAFKPLPQDFLACTPNDVDELTALFEEHGSEICAVMVEPIQGESGVHPLTPEFF
KAAHDLAHAHGALLIADEVQTGVFRSGKPFAFQTYGIEPDIMSLAKGIAGGVPMGAVMAK
ASVADAFNPGDHGTTFGGSALAVAASCAVLCELVRGEYDKHAREVGDYMAARLAGLPHVI
DVRGCGLMLGCDLDDAAGDAHDVVSAALASGFVINATGAHTLRFLPPLICERQDVDALID
ALSAILA
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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