SitesBLAST
Comparing Synpcc7942_0943 Synpcc7942_0943 acetylornithine aminotransferase 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)
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
46% identity, 93% coverage: 27:419/422 of query aligns to 11:393/393 of 2ordA
- active site: F134 (= F151), E186 (= E209), D219 (= D242), Q222 (= Q245), K248 (= K271), T276 (= T299), R367 (= R393)
- binding pyridoxal-5'-phosphate: G102 (= G118), T103 (≠ A119), F134 (= F151), H135 (= H152), E186 (= E209), D219 (= D242), V221 (= V244), Q222 (= Q245), K248 (= K271)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
46% identity, 93% coverage: 27:419/422 of query aligns to 3:385/385 of Q9X2A5
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
42% identity, 92% coverage: 27:416/422 of query aligns to 3:375/375 of 2eh6A
- active site: F127 (= F151), E179 (= E209), D212 (= D242), Q215 (= Q245), K241 (= K271), T270 (= T299), R352 (= R393)
- binding pyridoxal-5'-phosphate: G95 (= G118), T96 (≠ A119), F127 (= F151), H128 (= H152), E179 (= E209), D212 (= D242), V214 (= V244), K241 (= K271)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
42% identity, 92% coverage: 27:416/422 of query aligns to 4:376/376 of O66442
- GT 96:97 (≠ GA 118:119) binding
- K242 (= K271) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T299) binding
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
41% identity, 93% coverage: 17:409/422 of query aligns to 2:388/401 of 4adbB
- active site: F136 (= F151), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (= T299), R372 (= R393)
- binding pyridoxal-5'-phosphate: S102 (= S117), G103 (= G118), A104 (= A119), F136 (= F151), H137 (= H152), D221 (= D242), V223 (= V244), Q224 (= Q245), K250 (= K271)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
41% identity, 93% coverage: 17:409/422 of query aligns to 2:388/400 of 4addA
- active site: F136 (= F151), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (= T299), R372 (= R393)
- binding pyridoxal-5'-phosphate: G103 (= G118), A104 (= A119), F136 (= F151), H137 (= H152), D221 (= D242), V223 (= V244), K250 (= K271)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y31), F136 (= F151), R139 (= R154)
3nx3A Crystal structure of acetylornithine aminotransferase (argd) from campylobacter jejuni
39% identity, 92% coverage: 27:416/422 of query aligns to 4:385/388 of 3nx3A
- active site: F127 (= F151), E179 (= E209), D212 (= D242), Q215 (= Q245), K241 (= K271), T271 (= T299), R362 (= R393)
- binding magnesium ion: N191 (≠ D221), F194 (≠ Y224), I313 (≠ V341), F316 (≠ Y344), D317 (≠ N346), C319 (≠ L348), Q370 (≠ S401), K371 (≠ A402)
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)
40% identity, 93% coverage: 27:419/422 of query aligns to 69:456/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
43% identity, 95% coverage: 23:422/422 of query aligns to 7:388/390 of A0QYS9
- K304 (≠ E331) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
38% identity, 92% coverage: 23:409/422 of query aligns to 8:388/402 of 4jevB
- active site: F136 (= F151), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (= T299), R372 (= R393)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I61), S102 (= S117), G103 (= G118), T104 (≠ A119), F136 (= F151), H137 (= H152), E188 (= E209), E193 (= E214), D221 (= D242), V223 (= V244), Q224 (= Q245), K250 (= K271), R372 (= R393)
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)
38% identity, 92% coverage: 23:409/422 of query aligns to 13:393/405 of P40732
- GT 108:109 (≠ GA 118:119) binding
- K255 (= K271) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T299) binding
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum
41% identity, 91% coverage: 27:409/422 of query aligns to 10:382/390 of 8ht4B
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
37% identity, 92% coverage: 23:409/422 of query aligns to 8:383/397 of 4jewA
- active site: F136 (= F151), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T274 (= T299), R367 (= R393)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G118), T104 (≠ A119), F136 (= F151), H137 (= H152), R139 (= R154), E188 (= E209), E193 (= E214), D221 (= D242), V223 (= V244), K250 (= K271)
- binding picric acid: K25 (≠ R40), K27 (≠ E42), W32 (= W47)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
37% identity, 93% coverage: 23:416/422 of query aligns to 2:384/389 of 2pb0A
- active site: F130 (= F151), E182 (= E209), D215 (= D242), Q218 (= Q245), K244 (= K271), T268 (= T299), R361 (= R393)
- binding pyridoxal-5'-phosphate: S96 (= S117), G97 (= G118), T98 (≠ A119), F130 (= F151), H131 (= H152), E182 (= E209), D215 (= D242), V217 (= V244), Q218 (= Q245), K244 (= K271)
2byjA Ornithine aminotransferase mutant y85i (see paper)
35% identity, 95% coverage: 17:419/422 of query aligns to 3:404/404 of 2byjA
- active site: F142 (= F151), E195 (= E209), D228 (= D242), Q231 (= Q245), K257 (= K271), T287 (= T299), R378 (= R393)
- binding pyridoxal-5'-phosphate: G107 (= G118), V108 (≠ A119), F142 (= F151), W143 (≠ H152), D228 (= D242), I230 (≠ V244), Q231 (= Q245), K257 (= K271)
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, 99% coverage: 1:419/422 of query aligns to 22:439/439 of P04181
- G51 (vs. gap) to D: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs11553554
- Y55 (= Y31) to H: in HOGA; decreased protein abundance; dbSNP:rs121965037
- N89 (≠ T65) to K: in HOGA; no effect on protein abundance; dbSNP:rs386833602
- Q90 (≠ L66) to E: in HOGA; mistargeted, accumulates in cytoplasm; dbSNP:rs121965060
- C93 (≠ A69) to F: in HOGA; no effect on protein abundance; dbSNP:rs121965038
- Q104 (= Q80) to R: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833604
- R154 (= R130) to L: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965039
- R180 (= R154) to T: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965040
- A184 (= A158) natural variant: Missing (in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965035)
- P199 (= P173) to Q: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs267606925
- A226 (= A205) to V: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965059
- P241 (≠ G220) to L: in HOGA; no effect on protein abundance; dbSNP:rs121965051
- Y245 (= Y224) to C: in HOGA; no effect on protein abundance; dbSNP:rs121965046
- R250 (= R229) to P: in HOGA; no effect on protein abundance; dbSNP:rs121965052
- T267 (≠ V246) to I: in HOGA; decreased protein abundance; dbSNP:rs386833618
- A270 (≠ G249) to P: decreased protein abundance; dbSNP:rs121965041
- R271 (= R250) to K: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965042
- K292 (= K271) modified: N6-(pyridoxal phosphate)lysine
- E318 (= E295) to K: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833621
- V332 (≠ A309) to M: in HOGA; loss of protein stability; loss of ornithine aminotransferase activityx; dbSNP:rs121965047
- G353 (= G330) to D: in HOGA; decreased protein abundance; dbSNP:rs121965053
- G375 (= G355) to A: in HOGA; decreased protein abundance; dbSNP:rs121965045
- C394 (≠ V374) 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 (= L382) to P: in HOGA; may affect protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965043
- P417 (= P397) to L: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965044
- I436 (≠ L416) to N: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833598
- L437 (= L417) to F: in HOGA; no effect on protein stability; increased ornithine aminotransferase activity; dbSNP:rs1800456
Sites not aligning to the query:
- 1:35 modified: transit peptide, Mitochondrion; in renal form
8ez1B Human ornithine aminotransferase (hoat) co-crystallized with its inactivator 3-amino-4-fluorocyclopentenecarboxylic acid (see paper)
35% identity, 95% coverage: 17:419/422 of query aligns to 1:402/402 of 8ez1B
- binding (1R,3S,4Z)-3-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-4-iminocyclopentane-1-carboxylic acid: Y48 (≠ I61), T104 (≠ S117), G105 (= G118), V106 (≠ A119), F140 (= F151), W141 (≠ H152), E198 (= E214), D226 (= D242), I228 (≠ V244), Q229 (= Q245), K255 (= K271), R376 (= R393)
8ez1A Human ornithine aminotransferase (hoat) co-crystallized with its inactivator 3-amino-4-fluorocyclopentenecarboxylic acid (see paper)
35% identity, 95% coverage: 17:419/422 of query aligns to 1:402/402 of 8ez1A
- binding (3E,4E)-4-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-3-iminocyclopent-1-ene-1-carboxylic acid: Y48 (≠ I61), G105 (= G118), V106 (≠ A119), F140 (= F151), W141 (≠ H152), E198 (= E214), D226 (= D242), I228 (≠ V244), Q229 (= Q245), K255 (= K271), R376 (= R393)
7tfpC Human ornithine aminotransferase cocrystallized with its inhibitor, (1s,3s)-3-amino-4-(difluoromethylene)cyclopentane-1-carboxylic acid. (see paper)
35% identity, 95% coverage: 17:419/422 of query aligns to 1:402/402 of 7tfpC
- binding (1S,3S,4S)-3-amino-4-(fluoromethyl)cyclopentane-1-carboxylic acid: Y18 (= Y31), Y48 (≠ I61), F140 (= F151), E198 (= E214), K255 (= K271), R376 (= R393)
- binding pyridoxal-5'-phosphate: G105 (= G118), V106 (≠ A119), F140 (= F151), W141 (≠ H152), D226 (= D242), I228 (≠ V244), Q229 (= Q245), K255 (= K271)
7lk0A Ornithine aminotransferase (oat) cocrystallized with its potent inhibitor - (s)-3-amino-4,4-difluorocyclopent-1-enecarboxylic acid (ss-1-148) (see paper)
35% identity, 95% coverage: 17:419/422 of query aligns to 1:402/402 of 7lk0A
- binding (1R,3S)-3-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-4-oxocyclopentane-1-carboxylic acid: Y18 (= Y31), Y48 (≠ I61), G105 (= G118), V106 (≠ A119), F140 (= F151), W141 (≠ H152), E198 (= E214), D226 (= D242), I228 (≠ V244), Q229 (= Q245), K255 (= K271)
Query Sequence
>Synpcc7942_0943 Synpcc7942_0943 acetylornithine aminotransferase
VSPETVLAAVDAAIASPFSTDAFDACVMQTYGRFPLALERGEGCRVWDTQGRSYLDFVAG
IATCTLGHAHPELVDAISDQIRKLHHVSNLYYIPEQGQLAAWLTANSCADRVFFCNSGAE
ANEAAIKLARKHGNTVLEAENPIILTAQASFHGRTLAAVTATGQPKYHKGFQPLVQGFRY
VPYNDLAALEATLAELDAAGETVAAILLEPLQGEGGVNPGDRAYFQAVRQLCDQRRMLLI
LDEVQVGMGRSGQLWGYENLGIEPDAFTVAKGLGGGVPIGALLVKASCNILQAGEHASTF
GGNPLACRAGLAIAQVMERDQLLANVQARGEQLRAGLQELVDRYPNLLAGVRGWGLINGL
VLRNDPNVTPIALVKAAIEQGLLLVPAGAEVVRFVPPLIVSAAEIDEALAMTERALLAIA
GE
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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