SitesBLAST
Comparing WP_012468162.1 NCBI__GCF_000020385.1:WP_012468162.1 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)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
43% identity, 95% coverage: 10:386/397 of query aligns to 3:381/385 of Q9X2A5
- GT 94:95 (≠ GA 101:102) binding pyridoxal 5'-phosphate
- T268 (= T275) 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
43% identity, 95% coverage: 10:386/397 of query aligns to 11:389/393 of 2ordA
- active site: F134 (= F133), E186 (= E185), D219 (= D218), Q222 (= Q221), K248 (= K247), T276 (= T275), R367 (= R364)
- binding pyridoxal-5'-phosphate: G102 (= G101), T103 (≠ A102), F134 (= F133), H135 (= H134), E186 (= E185), D219 (= D218), V221 (= V220), Q222 (= Q221), K248 (= K247)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
44% identity, 94% coverage: 7:380/397 of query aligns to 8:388/401 of 4adbB
- active site: F136 (= F133), E188 (= E185), D221 (= D218), Q224 (= Q221), K250 (= K247), T279 (= T275), R372 (= R364)
- binding pyridoxal-5'-phosphate: S102 (= S100), G103 (= G101), A104 (= A102), 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)
44% identity, 94% coverage: 7:380/397 of query aligns to 8:388/400 of 4addA
- active site: F136 (= F133), E188 (= E185), D221 (= D218), Q224 (= Q221), K250 (= K247), T279 (= T275), R372 (= R364)
- binding pyridoxal-5'-phosphate: G103 (= G101), A104 (= A102), F136 (= F133), H137 (= H134), D221 (= D218), V223 (= V220), K250 (= K247)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ K15), F136 (= F133), R139 (= R136)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
41% identity, 96% coverage: 3:385/397 of query aligns to 27:423/429 of P73133
- Y39 (≠ T14) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S100) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G101) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A102) 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 (= T275) 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.
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
41% identity, 95% coverage: 10:387/397 of query aligns to 3:375/375 of 2eh6A
- active site: F127 (= F133), E179 (= E185), D212 (= D218), Q215 (= Q221), K241 (= K247), T270 (= T275), R352 (= R364)
- binding pyridoxal-5'-phosphate: G95 (= G101), T96 (≠ A102), F127 (= F133), H128 (= H134), E179 (= E185), D212 (= D218), V214 (= V220), K241 (= K247)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
41% identity, 95% coverage: 10:387/397 of query aligns to 4:376/376 of O66442
- GT 96:97 (≠ GA 101:102) binding pyridoxal 5'-phosphate
- K242 (= K247) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T275) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
40% identity, 96% coverage: 5:385/397 of query aligns to 6:393/402 of 4jevB
- active site: F136 (= F133), E188 (= E185), D221 (= D218), Q224 (= Q221), K250 (= K247), T279 (= T275), R372 (= R364)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (≠ W44), S102 (= S100), G103 (= G101), T104 (≠ A102), F136 (= F133), H137 (= H134), E188 (= E185), E193 (= E190), D221 (= D218), V223 (= V220), Q224 (= Q221), K250 (= K247), R372 (= R364)
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, 96% coverage: 5:385/397 of query aligns to 11:398/405 of P40732
- GT 108:109 (≠ GA 101:102) binding pyridoxal 5'-phosphate
- K255 (= K247) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T275) binding pyridoxal 5'-phosphate
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
40% identity, 96% coverage: 5:385/397 of query aligns to 6:388/397 of 4jewA
- active site: F136 (= F133), E188 (= E185), D221 (= D218), Q224 (= Q221), K250 (= K247), T274 (= T275), R367 (= R364)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G101), T104 (≠ A102), F136 (= F133), H137 (= H134), R139 (= R136), E188 (= E185), E193 (= E190), D221 (= D218), V223 (= V220), K250 (= K247)
- binding picric acid: K25 (≠ A23), K27 (≠ Q25), W32 (≠ T30)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
40% identity, 95% coverage: 7:385/397 of query aligns to 2:382/389 of 2pb0A
- active site: F130 (= F133), E182 (= E185), D215 (= D218), Q218 (= Q221), K244 (= K247), T268 (= T275), R361 (= R364)
- binding pyridoxal-5'-phosphate: S96 (= S100), G97 (= G101), T98 (≠ A102), F130 (= F133), H131 (= H134), E182 (= E185), D215 (= D218), V217 (= V220), Q218 (= Q221), K244 (= K247)
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)
39% identity, 94% coverage: 16:389/397 of query aligns to 75:455/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
37% identity, 96% coverage: 10:392/397 of query aligns to 11:388/390 of A0QYS9
- K304 (≠ V307) 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)
38% identity, 93% coverage: 10:377/397 of query aligns to 19:383/400 of P9WPZ7
- K314 (≠ V307) 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
38% identity, 93% coverage: 10:377/397 of query aligns to 13:377/391 of 7nncC
7nn4A Crystal structure of mycobacterium tuberculosis argd with prosthetic group pyridoxal 5'-phosphate and 3-hydroxy-2-naphthoic acid.
38% identity, 93% coverage: 10:377/397 of query aligns to 13:377/391 of 7nn4A
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
36% identity, 92% coverage: 17:383/397 of query aligns to 17:385/390 of 8ht4B
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
37% identity, 93% coverage: 10:377/397 of query aligns to 4:375/388 of 3nx3A
- active site: F127 (= F133), E179 (= E185), D212 (= D218), Q215 (= Q221), K241 (= K247), T271 (= T275), R362 (= R364)
- binding magnesium ion: N191 (≠ S197), F194 (= F200), I313 (≠ S317), F316 (≠ H320), D317 (≠ G321), C319 (≠ G323), Q370 (≠ S372), K371 (≠ A373)
P04181 Ornithine aminotransferase, mitochondrial; Ornithine delta-aminotransferase; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Homo sapiens (Human) (see 8 papers)
35% identity, 94% coverage: 18:389/397 of query aligns to 59:438/439 of P04181
- N89 (≠ C48) to K: in HOGA; no effect on protein abundance; dbSNP:rs386833602
- Q90 (≠ L49) to E: in HOGA; mistargeted, accumulates in cytoplasm; dbSNP:rs121965060
- C93 (≠ A52) to F: in HOGA; no effect on protein abundance; dbSNP:rs121965038
- Q104 (= Q63) to R: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833604
- R154 (= R113) to L: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965039
- R180 (= R136) to T: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965040
- A184 (≠ T140) natural variant: Missing (in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965035)
- P199 (= P155) to Q: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs267606925
- A226 (vs. gap) to V: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965059
- P241 (≠ A196) to L: in HOGA; no effect on protein abundance; dbSNP:rs121965051
- Y245 (≠ F200) to C: in HOGA; no effect on protein abundance; dbSNP:rs121965046
- R250 (= R205) to P: in HOGA; no effect on protein abundance; dbSNP:rs121965052
- T267 (= T222) to I: in HOGA; decreased protein abundance; dbSNP:rs386833618
- A270 (≠ G225) to P: decreased protein abundance; dbSNP:rs121965041
- R271 (= R226) to K: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965042
- K292 (= K247) modified: N6-(pyridoxal phosphate)lysine
- E318 (≠ D271) to K: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833621
- V332 (= V285) to M: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965047
- G353 (= G306) to D: in HOGA; decreased protein abundance; dbSNP:rs121965053
- G375 (= G329) to A: in HOGA; decreased protein abundance; dbSNP:rs121965045
- C394 (≠ T345) to R: in HOGA; no effect on protein abundance; dbSNP:rs121965054; to Y: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833597
- L402 (= L353) to P: in HOGA; may affect protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965043
- P417 (≠ A368) to L: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965044
- I436 (≠ F387) to N: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833598
- L437 (≠ V388) to F: in HOGA; likely benign; no effect on protein stability; no effect on ornithine aminotransferase activity; dbSNP:rs1800456
Sites not aligning to the query:
- 1:35 modified: transit peptide, Mitochondrion; in renal form
- 51 G → D: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs11553554
- 55 Y → H: in HOGA; decreased protein abundance; dbSNP:rs121965037
8ez1B Human ornithine aminotransferase (hoat) co-crystallized with its inactivator 3-amino-4-fluorocyclopentenecarboxylic acid (see paper)
35% identity, 94% coverage: 18:389/397 of query aligns to 22:401/402 of 8ez1B
- binding (1R,3S,4Z)-3-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-4-iminocyclopentane-1-carboxylic acid: Y48 (≠ W44), T104 (≠ S100), G105 (= G101), V106 (≠ A102), F140 (= F133), W141 (≠ H134), E198 (= E190), D226 (= D218), I228 (≠ V220), Q229 (= Q221), K255 (= K247), R376 (= R364)
Query Sequence
>WP_012468162.1 NCBI__GCF_000020385.1:WP_012468162.1
MSESSAFDSLMTITKRPPIVMVAGQGSWLTDSNGKRYLDFIQGWAVNCLGHAPAVITQAL
SQQAAQLISPSPAFYNQPAIRLADLLTANSCFERVFFANSGAEANEGAIKLARKWGSLHK
QGAYEIITMVNGFHGRTLATMSASGKPHWQGLFEPKVPGFIKVGLNDLEAVTAAISERTV
AIMLEPVQGEAGVIPASQLFLQGLRQLADQHQLLLIFDEVQTGMGRLGSLFAYQQAGVEP
DIMSLGKGIGGGVPLAALLAKEAVCCFEPGDQGGTYNGNPLMAAVGCAVLEAMLQPGFLE
QVRERGVQLANGLRKLSTRHGLGEVRGSGLLQALALPANNGDAVTEAARELGLIINAARP
DTLRFMPALNVSADEVDTCLRLLDQVFVAGAEMGCPA
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