SitesBLAST
Comparing WP_020562842.1 NCBI__GCF_000372865.1:WP_020562842.1 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)
4ppmA Crystal structure of pige: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (map) from serratia sp. Fs14 (see paper)
36% identity, 90% coverage: 15:431/462 of query aligns to 22:450/464 of 4ppmA
- active site: M35 (= M28), Y159 (= Y151), E212 (= E204), D245 (= D236), Q248 (= Q239), K274 (= K265), T309 (= T300), R431 (≠ K412)
- binding magnesium ion: A351 (≠ S342), Y354 (= Y345), V357 (≠ L348)
- binding pyridoxal-5'-phosphate: G132 (= G124), T133 (= T125), Y159 (= Y151), H160 (= H152), D245 (= D236), V247 (= V238), K274 (= K265)
A0A0J9X1Q5 Aminotransferase PigE; EC 2.6.1.- from Serratia sp. (strain FS14) (see paper)
35% identity, 90% coverage: 15:431/462 of query aligns to 393:841/853 of A0A0J9X1Q5
- GT 503:504 (= GT 124:125) binding pyridoxal 5'-phosphate
- K645 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T680 (= T300) binding pyridoxal 5'-phosphate
8cplC Yzw2 a scaffold for cryo-em of small proteins of interest
43% identity, 68% coverage: 49:362/462 of query aligns to 68:387/499 of 8cplC
4uoyA Crystal structure of ygjg in complex with pyridoxal-5'-phosphate (see paper)
43% identity, 68% coverage: 49:362/462 of query aligns to 70:389/454 of 4uoyA
- active site: F174 (≠ Y151), E232 (= E204), D265 (= D236), Q268 (= Q239), K294 (= K265), T326 (= T300)
- binding pyridoxal-5'-phosphate: G144 (= G124), T145 (= T125), F174 (≠ Y151), H175 (= H152), G176 (= G153), E232 (= E204), D265 (= D236), V267 (= V238), Q268 (= Q239), K294 (= K265)
Sites not aligning to the query:
4uoxA Crystal structure of ygjg in complex with pyridoxal-5'-phosphate and putrescine (see paper)
43% identity, 68% coverage: 49:362/462 of query aligns to 70:389/453 of 4uoxA
- active site: F174 (≠ Y151), E232 (= E204), D265 (= D236), Q268 (= Q239), K294 (= K265), T326 (= T300)
- binding pyridoxal-5'-phosphate: S143 (= S123), G144 (= G124), T145 (= T125), F174 (≠ Y151), H175 (= H152), G176 (= G153), D265 (= D236), V267 (= V238), Q268 (= Q239), T325 (≠ S299), T326 (= T300)
- binding 1,4-diaminobutane: E237 (≠ K209), K294 (= K265)
Sites not aligning to the query:
P42588 Putrescine aminotransferase; PAT; PATase; Cadaverine transaminase; Diamine transaminase; Putrescine transaminase; Putrescine--2-oxoglutaric acid transaminase; Putrescine:2-OG aminotransferase; EC 2.6.1.82; EC 2.6.1.29 from Escherichia coli (strain K12) (see paper)
38% identity, 84% coverage: 49:436/462 of query aligns to 76:450/459 of P42588
- GT 150:151 (= GT 124:125) binding in other chain
- Q274 (= Q239) binding in other chain
- K300 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T332 (= T300) binding pyridoxal 5'-phosphate
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
36% identity, 87% coverage: 37:436/462 of query aligns to 24:395/395 of Q5SHH5
- GT 113:114 (= GT 124:125) binding pyridoxal 5'-phosphate
- K254 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T300) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 87% coverage: 37:436/462 of query aligns to 16:387/387 of 1wkhA
- active site: F132 (≠ Y151), E184 (= E204), D217 (= D236), Q220 (= Q239), K246 (= K265), T275 (= T300), R363 (≠ K412)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ F64), S104 (= S123), G105 (= G124), T106 (= T125), F132 (≠ Y151), S133 (≠ H152), E184 (= E204), E189 (≠ K209), D217 (= D236), I219 (≠ V238), K246 (= K265), R363 (≠ K412)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 87% coverage: 37:436/462 of query aligns to 16:387/387 of 1wkgA
- active site: F132 (≠ Y151), E184 (= E204), D217 (= D236), Q220 (= Q239), K246 (= K265), T275 (= T300), R363 (≠ K412)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (= Y37), Y46 (≠ F64), G105 (= G124), T106 (= T125), F132 (≠ Y151), S133 (≠ H152), R135 (≠ L154), E184 (= E204), D217 (= D236), I219 (≠ V238), Q220 (= Q239), K246 (= K265), G273 (= G298), T274 (≠ S299), T275 (= T300)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 87% coverage: 37:436/462 of query aligns to 16:387/387 of 1vefA
- active site: F132 (≠ Y151), D217 (= D236), K246 (= K265), T275 (= T300), R363 (≠ K412)
- binding pyridoxal-5'-phosphate: G105 (= G124), T106 (= T125), F132 (≠ Y151), S133 (≠ H152), E184 (= E204), D217 (= D236), I219 (≠ V238), K246 (= K265)
Sites not aligning to the query:
P04181 Ornithine aminotransferase, mitochondrial; Ornithine delta-aminotransferase; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Homo sapiens (Human) (see 8 papers)
36% identity, 85% coverage: 43:435/462 of query aligns to 64:436/439 of P04181
- N89 (≠ A68) to K: in HOGA; no effect on protein abundance; dbSNP:rs386833602
- Q90 (≠ I69) to E: in HOGA; mistargeted, accumulates in cytoplasm; dbSNP:rs121965060
- C93 (≠ N72) to F: in HOGA; no effect on protein abundance; dbSNP:rs121965038
- Q104 (≠ E87) to R: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833604
- R154 (= R136) to L: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965039
- R180 (≠ L154) 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 (= A200) to V: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965059
- P241 (= P214) to L: in HOGA; no effect on protein abundance; dbSNP:rs121965051
- Y245 (= Y218) to C: in HOGA; no effect on protein abundance; dbSNP:rs121965046
- R250 (≠ E223) to P: in HOGA; no effect on protein abundance; dbSNP:rs121965052
- T267 (= T240) to I: in HOGA; decreased protein abundance; dbSNP:rs386833618
- A270 (≠ G243) to P: decreased protein abundance; dbSNP:rs121965041
- R271 (= R244) to K: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965042
- K292 (= K265) modified: N6-(pyridoxal phosphate)lysine
- E318 (≠ V296) to K: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833621
- V332 (≠ A310) to M: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965047
- G353 (= G331) to D: in HOGA; decreased protein abundance; dbSNP:rs121965053
- G375 (= G355) to A: in HOGA; decreased protein abundance; dbSNP:rs121965045
- C394 (vs. gap) 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 (= L384) to P: in HOGA; may affect protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965043
- P417 (= P416) to L: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965044
- I436 (= I435) to N: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833598
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
- 437 L → F: in HOGA; likely benign; no effect on protein stability; no effect on ornithine aminotransferase activity; dbSNP:rs1800456
8v9mA Human ornithine aminotransferase cocrystallized with its inhibitor, (r)-3-amino-5,5-difluorocyclohex-1-ene-1-carboxylic acid. (see paper)
36% identity, 85% coverage: 43:435/462 of query aligns to 29:401/404 of 8v9mA
- binding 3-fluoro-5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]benzoic acid: Y50 (≠ F64), G107 (= G124), V108 (≠ T125), F142 (≠ Y151), W143 (≠ H152), E200 (≠ K209), D228 (= D236), I230 (≠ V238), Q231 (= Q239), K257 (= K265), K370 (≠ Q387)
Sites not aligning to the query:
7tedA Human ornithine aminotransferase cocrystallized with its inhibitor, (s,e)-3-amino-4-(fluoromethylene)cyclopent-1-ene-1-carboxylate (see paper)
36% identity, 85% coverage: 43:435/462 of query aligns to 29:401/404 of 7tedA
- binding (1S,3R,4S)-3-formyl-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopentane-1-carboxylic acid: Y50 (≠ F64), G107 (= G124), V108 (≠ T125), F142 (≠ Y151), W143 (≠ H152), G144 (= G153), E200 (≠ K209), D228 (= D236), I230 (≠ V238), Q231 (= Q239), K257 (= K265), S286 (= S299), T287 (= T300)
Sites not aligning to the query:
7ta1A Human ornithine aminotransferase (hoat) soaked with gamma-aminobutyric acid (see paper)
36% identity, 85% coverage: 43:435/462 of query aligns to 29:401/404 of 7ta1A
Sites not aligning to the query:
7lnmB Ornithine aminotransferase (oat) cocrystallized with its inactivator - (1s,3s)-3-amino-4-(difluoromethylene)cyclopentene-1-carboxylic acid (see paper)
36% identity, 85% coverage: 43:435/462 of query aligns to 29:401/404 of 7lnmB
- binding (1~{R},3~{S},4~{R})-3-methyl-4-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]cyclopentane-1-carboxylic acid: Y50 (≠ F64), G107 (= G124), V108 (≠ T125), F142 (≠ Y151), W143 (≠ H152), D228 (= D236), I230 (≠ V238), Q231 (= Q239), K257 (= K265)
7lk1A Ornithine aminotransferase (oat) with its potent inhibitor - (s)-3- amino-4,4-difluorocyclopent-1-enecarboxylic acid (ss-1-148) - 1 hour soaking (see paper)
36% identity, 85% coverage: 43:435/462 of query aligns to 29:401/404 of 7lk1A
- binding (1R,4R)-4-fluoro-3-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]cyclopent-2-ene-1-carboxylic acid: Y50 (≠ F64), G107 (= G124), V108 (≠ T125), F142 (≠ Y151), W143 (≠ H152), E200 (≠ K209), D228 (= D236), I230 (≠ V238), Q231 (= Q239), K257 (= K265), R378 (≠ K412)
6v8cA Design, synthesis, and mechanism of fluorine-substituted cyclohexene analogues of gama-aminobutyric acid (gaba) as selective ornithine aminotransferase inactivators
36% identity, 85% coverage: 43:435/462 of query aligns to 29:401/404 of 6v8cA
- active site: F142 (≠ Y151), E195 (= E204), D228 (= D236), Q231 (= Q239), K257 (= K265), T287 (= T300), R378 (≠ K412)
- binding pyridoxal-5'-phosphate: G107 (= G124), V108 (≠ T125), F142 (≠ Y151), W143 (≠ H152), D228 (= D236), I230 (≠ V238), K257 (= K265)
- binding 3-aminocyclohexa-1,3-diene-1-carboxylic acid: Y50 (≠ F64), F142 (≠ Y151), K257 (= K265)
Sites not aligning to the query:
6oiaA (1s,3s)-3-amino-4-(perfluoropropan-2-ylidene)cyclopentane-1-carboxylic acid hydrochloride, a potent inhibitor of ornithine aminotransferase (see paper)
36% identity, 85% coverage: 43:435/462 of query aligns to 29:401/404 of 6oiaA
- active site: F142 (≠ Y151), E195 (= E204), D228 (= D236), Q231 (= Q239), K257 (= K265), T287 (= T300), R378 (≠ K412)
- binding (1S)-3-amino-4-[(2S)-1,1,1-trifluoro-3-oxopropan-2-yl]cyclopent-3-ene-1-carboxylic acid: S286 (= S299), T287 (= T300)
- binding pyridoxal-5'-phosphate: G107 (= G124), V108 (≠ T125), F142 (≠ Y151), W143 (≠ H152), D228 (= D236), I230 (≠ V238), K257 (= K265)
5vwoA Ornithine aminotransferase inactivated by (1r,3s,4s)-3-amino-4- fluorocyclopentane-1-carboxylic acid (fcp) (see paper)
36% identity, 85% coverage: 43:435/462 of query aligns to 29:401/404 of 5vwoA
- active site: F142 (≠ Y151), E195 (= E204), D228 (= D236), Q231 (= Q239), K257 (= K265), T287 (= T300), R378 (≠ K412)
- binding (1S,3S,4E)-3-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-4-iminocyclopentane-1-carboxylic acid: Y50 (≠ F64), G107 (= G124), V108 (≠ T125), F142 (≠ Y151), W143 (≠ H152), G144 (= G153), R145 (≠ L154), E200 (≠ K209), D228 (= D236), I230 (≠ V238), Q231 (= Q239), K257 (= K265)
2oatA Ornithine aminotransferase complexed with 5-fluoromethylornithine (see paper)
36% identity, 85% coverage: 43:435/462 of query aligns to 29:401/404 of 2oatA
- active site: F142 (≠ Y151), E195 (= E204), D228 (= D236), Q231 (= Q239), K257 (= K265), T287 (= T300), R378 (≠ K412)
- binding 1-amino-7-(2-methyl-3-oxido-5-((phosphonoxy)methyl)-4-pyridoxal-5-oxo-6-heptenate: G107 (= G124), V108 (≠ T125), F142 (≠ Y151), W143 (≠ H152), R145 (≠ L154), E195 (= E204), E200 (≠ K209), D228 (= D236), Q231 (= Q239), K257 (= K265), G285 (= G298), T287 (= T300)
Sites not aligning to the query:
Query Sequence
>WP_020562842.1 NCBI__GCF_000372865.1:WP_020562842.1
MSFSIAELFEQHSTDKFDLHEQFLNNQMVRVLKTIGYDRHYRKANGQYLYDEKGAEYLDL
LSGFGVFAIGRNHPTVINALKETLTLELPNLVQLDVSVLSGLLAQEILKTTPDNLDKMFF
CNSGTESVEAAIKFARFTTKREKIVFCEHAYHGLTMGALSLNGEPIFREGFGPLLPGCYS
IPFNDAEALEQALRDKDVAAFIVEPIQGKGVNVPDDNYLPEVERICKKYGTLFVADEVQT
GLGRTGKFWAIEHWNVRPDMICMAKALSGGFVPVGAVAMTQKIMDSVYNRMDRAVVHGST
FSKNNMAMAAGLATLHVMQEENLVDNSAKLGTDIIDSLNALSEQYEFLKEARGKGMMIAI
EFHSPKSLKLKAAWAMLEAANKGLFCQMITIPLFKEHRILAQVAGHGMNVVKLLPPLNLN
PKDRDTIVAAFDKTIADTHQIPGSIWDLGKNLASHALKGKKG
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