SitesBLAST
Comparing WP_027178028.1 NCBI__GCF_000429985.1:WP_027178028.1 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)
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
43% identity, 96% coverage: 15:396/399 of query aligns to 3:375/375 of 2eh6A
- active site: F127 (= F139), E179 (= E192), D212 (= D225), Q215 (= Q228), K241 (= K254), T270 (= T283), R352 (= R373)
- binding pyridoxal-5'-phosphate: G95 (= G106), T96 (≠ A107), F127 (= F139), H128 (= H140), E179 (= E192), D212 (= D225), V214 (= V227), K241 (= K254)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
43% identity, 96% coverage: 15:396/399 of query aligns to 4:376/376 of O66442
- GT 96:97 (≠ GA 106:107) binding pyridoxal 5'-phosphate
- K242 (= K254) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T283) 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
41% identity, 96% coverage: 15:397/399 of query aligns to 11:391/393 of 2ordA
- active site: F134 (= F139), E186 (= E192), D219 (= D225), Q222 (= Q228), K248 (= K254), T276 (= T283), R367 (= R373)
- binding pyridoxal-5'-phosphate: G102 (= G106), T103 (≠ A107), F134 (= F139), H135 (= H140), E186 (= E192), D219 (= D225), V221 (= V227), Q222 (= Q228), K248 (= K254)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
41% identity, 96% coverage: 15:397/399 of query aligns to 3:383/385 of Q9X2A5
- GT 94:95 (≠ GA 106:107) binding pyridoxal 5'-phosphate
- T268 (= T283) binding pyridoxal 5'-phosphate
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)
41% identity, 96% coverage: 15:399/399 of query aligns to 69:452/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
36% identity, 96% coverage: 16:397/399 of query aligns to 21:395/395 of Q5SHH5
- GT 113:114 (≠ GA 106:107) binding pyridoxal 5'-phosphate
- K254 (= K254) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T283) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 96% coverage: 16:397/399 of query aligns to 13:387/387 of 1wkhA
- active site: S13 (≠ C16), F132 (= F139), E184 (= E192), D217 (= D225), Q220 (= Q228), K246 (= K254), T275 (= T283), R363 (= R373)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I49), S104 (= S105), G105 (= G106), T106 (≠ A107), F132 (= F139), S133 (≠ H140), E184 (= E192), E189 (= E197), D217 (= D225), I219 (≠ V227), K246 (= K254), R363 (= R373)
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 96% coverage: 16:397/399 of query aligns to 13:387/387 of 1wkgA
- active site: S13 (≠ C16), F132 (= F139), E184 (= E192), D217 (= D225), Q220 (= Q228), K246 (= K254), T275 (= T283), R363 (= R373)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (= Y19), Y46 (≠ I49), G105 (= G106), T106 (≠ A107), F132 (= F139), S133 (≠ H140), R135 (= R142), E184 (= E192), D217 (= D225), I219 (≠ V227), Q220 (= Q228), K246 (= K254), G273 (≠ A281), T274 (= T282), T275 (= T283)
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 96% coverage: 16:397/399 of query aligns to 13:387/387 of 1vefA
- active site: S13 (≠ C16), F132 (= F139), D217 (= D225), K246 (= K254), T275 (= T283), R363 (= R373)
- binding pyridoxal-5'-phosphate: G105 (= G106), T106 (≠ A107), F132 (= F139), S133 (≠ H140), E184 (= E192), D217 (= D225), I219 (≠ V227), K246 (= K254)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
37% identity, 93% coverage: 18:389/399 of query aligns to 15:388/401 of 4adbB
- active site: F136 (= F139), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T279 (= T283), R372 (= R373)
- binding pyridoxal-5'-phosphate: S102 (= S105), G103 (= G106), A104 (= A107), F136 (= F139), H137 (= H140), D221 (= D225), V223 (= V227), Q224 (= Q228), K250 (= K254)
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, 90% coverage: 28:386/399 of query aligns to 30:390/405 of P40732
- GT 108:109 (≠ GA 106:107) binding pyridoxal 5'-phosphate
- K255 (= K254) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T283) binding pyridoxal 5'-phosphate
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
37% identity, 93% coverage: 18:389/399 of query aligns to 15:388/400 of 4addA
- active site: F136 (= F139), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T279 (= T283), R372 (= R373)
- binding pyridoxal-5'-phosphate: G103 (= G106), A104 (= A107), F136 (= F139), H137 (= H140), D221 (= D225), V223 (= V227), K250 (= K254)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (= Y19), F136 (= F139), R139 (= R142)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
38% identity, 90% coverage: 28:386/399 of query aligns to 25:385/402 of 4jevB
- active site: F136 (= F139), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T279 (= T283), R372 (= R373)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I49), S102 (= S105), G103 (= G106), T104 (≠ A107), F136 (= F139), H137 (= H140), E188 (= E192), E193 (= E197), D221 (= D225), V223 (= V227), Q224 (= Q228), K250 (= K254), R372 (= R373)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
41% identity, 95% coverage: 15:392/399 of query aligns to 10:385/390 of 8ht4B
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
38% identity, 96% coverage: 15:396/399 of query aligns to 11:383/390 of A0QYS9
- K304 (≠ E315) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2byjA Ornithine aminotransferase mutant y85i (see paper)
35% identity, 97% coverage: 5:393/399 of query aligns to 6:398/404 of 2byjA
- active site: F142 (= F139), E195 (= E192), D228 (= D225), Q231 (= Q228), K257 (= K254), T287 (= T283), R378 (= R373)
- binding pyridoxal-5'-phosphate: G107 (= G106), V108 (≠ A107), F142 (= F139), W143 (≠ H140), D228 (= D225), I230 (≠ V227), Q231 (= Q228), K257 (= K254)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
37% identity, 90% coverage: 28:386/399 of query aligns to 25:380/397 of 4jewA
- active site: F136 (= F139), E188 (= E192), D221 (= D225), Q224 (= Q228), K250 (= K254), T274 (= T283), R367 (= R373)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G106), T104 (≠ A107), F136 (= F139), H137 (= H140), R139 (= R142), E188 (= E192), E193 (= E197), D221 (= D225), V223 (= V227), K250 (= K254)
- binding picric acid: K25 (= K28), K27 (= K30), W32 (≠ Y35)
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, 97% coverage: 5:393/399 of query aligns to 41:433/439 of P04181
- G51 (≠ I15) to D: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs11553554
- Y55 (= Y19) to H: in HOGA; decreased protein abundance; dbSNP:rs121965037
- N89 (= N53) to K: in HOGA; no effect on protein abundance; dbSNP:rs386833602
- Q90 (≠ L54) to E: in HOGA; mistargeted, accumulates in cytoplasm; dbSNP:rs121965060
- C93 (= C57) to F: in HOGA; no effect on protein abundance; dbSNP:rs121965038
- Q104 (= Q68) to R: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833604
- R154 (= R118) to L: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965039
- R180 (= R142) to T: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965040
- A184 (≠ T146) natural variant: Missing (in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965035)
- P199 (= P162) to Q: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs267606925
- A226 (= A188) to V: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965059
- P241 (≠ L203) to L: in HOGA; no effect on protein abundance; dbSNP:rs121965051
- Y245 (= Y207) to C: in HOGA; no effect on protein abundance; dbSNP:rs121965046
- R250 (≠ A212) to P: in HOGA; no effect on protein abundance; dbSNP:rs121965052
- T267 (≠ S229) to I: in HOGA; decreased protein abundance; dbSNP:rs386833618
- A270 (≠ C232) to P: decreased protein abundance; dbSNP:rs121965041
- R271 (= R233) to K: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965042
- K292 (= K254) modified: N6-(pyridoxal phosphate)lysine
- E318 (≠ S279) to K: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833621
- V332 (= V293) to M: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965047
- G353 (= G314) to D: in HOGA; decreased protein abundance; dbSNP:rs121965053
- G375 (= G339) to A: in HOGA; decreased protein abundance; dbSNP:rs121965045
- C394 (≠ F354) 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 (≠ F362) to P: in HOGA; may affect protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965043
- P417 (= P377) to L: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965044
Sites not aligning to the query:
- 1:35 modified: transit peptide, Mitochondrion; in renal form
- 436 I → N: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833598
- 437 L → F: in HOGA; likely benign; no effect on protein stability; no effect on ornithine aminotransferase activity; dbSNP:rs1800456
7ta0A Human ornithine aminotransferase (hoat) soaked with 5-aminovaleric acid (see paper)
35% identity, 97% coverage: 5:393/399 of query aligns to 5:397/403 of 7ta0A
- binding 5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]pentanoic acid: Y19 (= Y19), Y49 (≠ I49), G106 (= G106), V107 (≠ A107), F141 (= F139), W142 (≠ H140), D227 (= D225), I229 (≠ V227), Q230 (= Q228), K256 (= K254), S285 (≠ T282), T286 (= T283)
8v9mA Human ornithine aminotransferase cocrystallized with its inhibitor, (r)-3-amino-5,5-difluorocyclohex-1-ene-1-carboxylic acid. (see paper)
35% identity, 97% coverage: 5:393/399 of query aligns to 6:398/404 of 8v9mA
- binding 3-fluoro-5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]benzoic acid: Y20 (= Y19), Y50 (≠ I49), G107 (= G106), V108 (≠ A107), F142 (= F139), W143 (≠ H140), E200 (= E197), D228 (= D225), I230 (≠ V227), Q231 (= Q228), K257 (= K254), K370 (≠ N365)
Query Sequence
>WP_027178028.1 NCBI__GCF_000429985.1:WP_027178028.1
MSKHDNLVKKVNNNICNTYGRYPVSISKAKGARLYDLDGNEYIDLLSGISVANLGHCRED
LAKVMAEQSQKLVQVSNLFYQEEQAELAEKLLKTSDAGKVFFCNSGAEANEAAIKLARRY
MRKVKNKEAYEIITLQGSFHGRTLATLTATGQDGLIKEGFGPLPEGFKSVPAGDIEAMRN
AISDKTAAIMVEMIQGEGGIRPLAPEYVTVLAALAKEKDVLLIADEVQSGLCRSGKWWAF
QHYGITPDIFTSAKSLANGLPMGAMFATDTVATGFEPGSHATTFGGGALVSKVASKVVDI
MNDEKIAERAAKLGEQFKKEAAELITRHPDKVETVRGLGLMLGIQLKIDGSSIFAALRDK
GFILNLTKGTILRLLPPLTIDFEDLRTFLKTLDGILSEN
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