SitesBLAST
Comparing WP_013420082.1 NCBI__GCF_000166055.1:WP_013420082.1 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)
37% identity, 90% coverage: 5:421/463 of query aligns to 10:440/464 of 4ppmA
- active site: M35 (= M28), Y159 (≠ F150), E212 (= E203), D245 (= D235), Q248 (= Q238), K274 (= K265), T309 (= T300), R431 (≠ K412)
- binding magnesium ion: A351 (vs. gap), Y354 (≠ H345), V357 (≠ M348)
- binding pyridoxal-5'-phosphate: G132 (= G123), T133 (= T124), Y159 (≠ F150), H160 (= H151), D245 (= D235), V247 (≠ I237), K274 (= K265)
A0A0J9X1Q5 Aminotransferase PigE; EC 2.6.1.- from Serratia sp. (strain FS14) (see paper)
35% identity, 90% coverage: 5:421/463 of query aligns to 381:831/853 of A0A0J9X1Q5
- GT 503:504 (= GT 123:124) binding pyridoxal 5'-phosphate
- K645 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T680 (= T300) binding pyridoxal 5'-phosphate
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)
35% identity, 90% coverage: 23:437/463 of query aligns to 45:451/459 of P42588
- GT 150:151 (= GT 123:124) binding in other chain
- Q274 (= Q238) binding in other chain
- K300 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T332 (= T300) binding pyridoxal 5'-phosphate
8cplC Yzw2 a scaffold for cryo-em of small proteins of interest
36% identity, 90% coverage: 22:437/463 of query aligns to 36:443/499 of 8cplC
4uoxA Crystal structure of ygjg in complex with pyridoxal-5'-phosphate and putrescine (see paper)
35% identity, 90% coverage: 23:437/463 of query aligns to 39:445/453 of 4uoxA
- active site: F44 (≠ M28), F174 (= F150), E232 (= E203), D265 (= D235), Q268 (= Q238), K294 (= K265), T326 (= T300), R420 (≠ K412)
- binding pyridoxal-5'-phosphate: S143 (= S122), G144 (= G123), T145 (= T124), F174 (= F150), H175 (= H151), G176 (= G152), D265 (= D235), V267 (≠ I237), Q268 (= Q238), T325 (≠ S299), T326 (= T300)
- binding 1,4-diaminobutane: E237 (≠ K208), K294 (= K265)
4uoyA Crystal structure of ygjg in complex with pyridoxal-5'-phosphate (see paper)
35% identity, 90% coverage: 23:437/463 of query aligns to 39:445/454 of 4uoyA
- active site: F44 (≠ M28), F174 (= F150), E232 (= E203), D265 (= D235), Q268 (= Q238), K294 (= K265), T326 (= T300), R420 (≠ K412)
- binding pyridoxal-5'-phosphate: G144 (= G123), T145 (= T124), F174 (= F150), H175 (= H151), G176 (= G152), E232 (= E203), D265 (= D235), V267 (≠ I237), Q268 (= Q238), K294 (= K265)
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
34% identity, 86% coverage: 37:436/463 of query aligns to 27:395/395 of Q5SHH5
- GT 113:114 (= GT 123:124) binding pyridoxal 5'-phosphate
- K254 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T300) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 86% coverage: 37:436/463 of query aligns to 19:387/387 of 1wkhA
- active site: F132 (= F150), E184 (= E203), D217 (= D235), Q220 (= Q238), K246 (= K265), T275 (= T300), R363 (≠ K412)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ W64), S104 (= S122), G105 (= G123), T106 (= T124), F132 (= F150), S133 (≠ H151), E184 (= E203), E189 (≠ K208), D217 (= D235), I219 (= I237), K246 (= K265), R363 (≠ K412)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 86% coverage: 37:436/463 of query aligns to 19:387/387 of 1wkgA
- active site: F132 (= F150), E184 (= E203), D217 (= D235), Q220 (= Q238), 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: Y46 (≠ W64), G105 (= G123), T106 (= T124), F132 (= F150), S133 (≠ H151), R135 (≠ L153), E184 (= E203), D217 (= D235), I219 (= I237), Q220 (= Q238), K246 (= K265), G273 (= G298), T274 (≠ S299), T275 (= T300)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 86% coverage: 37:436/463 of query aligns to 19:387/387 of 1vefA
- active site: F132 (= F150), D217 (= D235), K246 (= K265), T275 (= T300), R363 (≠ K412)
- binding pyridoxal-5'-phosphate: G105 (= G123), T106 (= T124), F132 (= F150), S133 (≠ H151), E184 (= E203), D217 (= D235), I219 (= I237), K246 (= K265)
Sites not aligning to the query:
Q6LFH8 Ornithine aminotransferase; PfOAT; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Plasmodium falciparum (isolate 3D7) (see paper)
35% identity, 69% coverage: 43:362/463 of query aligns to 34:354/414 of Q6LFH8
- C154 (≠ S157) modified: Disulfide link with 163, Reversible; mutation to S: Severe reduction in catalytic activity. Does not affect TRX1-mediated activation. Severe reduction in catalytic activity and loss of TRX1-mediated activation; when associated with S-163.
- C163 (≠ F166) modified: Disulfide link with 154, Reversible; mutation to S: No effect on catalytic activity. Requires higher concentrations of TRX1 for activation. Severe reduction in catalytic activity and loss of TRX1-mediated activation; when associated with S-154.
- C316 (≠ I324) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C350 (≠ I358) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
Sites not aligning to the query:
- 390 C→S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
P04181 Ornithine aminotransferase, mitochondrial; Ornithine delta-aminotransferase; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Homo sapiens (Human) (see 8 papers)
34% identity, 86% coverage: 39:435/463 of query aligns to 60:436/439 of P04181
- N89 (≠ A68) to K: in HOGA; no effect on protein abundance; dbSNP:rs386833602
- Q90 (≠ L69) to E: in HOGA; mistargeted, accumulates in cytoplasm; dbSNP:rs121965060
- C93 (≠ N72) to F: in HOGA; no effect on protein abundance; dbSNP:rs121965038
- Q104 (≠ V83) to R: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs386833604
- R154 (= R135) to L: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965039
- R180 (≠ L153) to T: in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965040
- A184 (≠ S157) natural variant: Missing (in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity; dbSNP:rs121965035)
- P199 (≠ G172) to Q: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs267606925
- A226 (≠ G199) to V: in HOGA; loss of protein stability; loss of ornithine aminotransferase activity; dbSNP:rs121965059
- P241 (= P213) to L: in HOGA; no effect on protein abundance; dbSNP:rs121965051
- Y245 (= Y217) to C: in HOGA; no effect on protein abundance; dbSNP:rs121965046
- R250 (≠ Q222) to P: in HOGA; no effect on protein abundance; dbSNP:rs121965052
- T267 (= T239) to I: in HOGA; decreased protein abundance; dbSNP:rs386833618
- A270 (≠ G242) to P: decreased protein abundance; dbSNP:rs121965041
- R271 (= R243) 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 (≠ A376) 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 (≠ A416) 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)
34% identity, 86% coverage: 39:435/463 of query aligns to 25:401/404 of 8v9mA
- binding 3-fluoro-5-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]benzoic acid: Y50 (≠ W64), G107 (= G123), V108 (≠ T124), F142 (= F150), W143 (≠ H151), E200 (≠ K208), D228 (= D235), I230 (= I237), Q231 (= Q238), K257 (= K265), K370 (≠ Q387)
Sites not aligning to the query:
8ez1B Human ornithine aminotransferase (hoat) co-crystallized with its inactivator 3-amino-4-fluorocyclopentenecarboxylic acid (see paper)
34% identity, 86% coverage: 39:435/463 of query aligns to 23:399/402 of 8ez1B
- binding (1R,3S,4Z)-3-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-4-iminocyclopentane-1-carboxylic acid: Y48 (≠ W64), T104 (≠ S122), G105 (= G123), V106 (≠ T124), F140 (= F150), W141 (≠ H151), E198 (≠ K208), D226 (= D235), I228 (= I237), Q229 (= Q238), K255 (= K265), R376 (≠ K412)
8ez1A Human ornithine aminotransferase (hoat) co-crystallized with its inactivator 3-amino-4-fluorocyclopentenecarboxylic acid (see paper)
34% identity, 86% coverage: 39:435/463 of query aligns to 23:399/402 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 (≠ W64), G105 (= G123), V106 (≠ T124), F140 (= F150), W141 (≠ H151), E198 (≠ K208), D226 (= D235), I228 (= I237), Q229 (= Q238), K255 (= K265), R376 (≠ K412)
7tfpC Human ornithine aminotransferase cocrystallized with its inhibitor, (1s,3s)-3-amino-4-(difluoromethylene)cyclopentane-1-carboxylic acid. (see paper)
34% identity, 86% coverage: 39:435/463 of query aligns to 23:399/402 of 7tfpC
- binding (1S,3S,4S)-3-amino-4-(fluoromethyl)cyclopentane-1-carboxylic acid: Y48 (≠ W64), F140 (= F150), E198 (≠ K208), K255 (= K265), R376 (≠ K412)
- binding pyridoxal-5'-phosphate: G105 (= G123), V106 (≠ T124), F140 (= F150), W141 (≠ H151), D226 (= D235), I228 (= I237), Q229 (= Q238), K255 (= K265)
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)
34% identity, 86% coverage: 39:435/463 of query aligns to 25:401/404 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 (≠ W64), G107 (= G123), V108 (≠ T124), F142 (= F150), W143 (≠ H151), G144 (= G152), E200 (≠ K208), D228 (= D235), I230 (= I237), Q231 (= Q238), K257 (= K265), S286 (= S299), T287 (= T300)
Sites not aligning to the query:
7ta1A Human ornithine aminotransferase (hoat) soaked with gamma-aminobutyric acid (see paper)
34% identity, 86% coverage: 39:435/463 of query aligns to 25:401/404 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)
34% identity, 86% coverage: 39:435/463 of query aligns to 25:401/404 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 (≠ W64), G107 (= G123), V108 (≠ T124), F142 (= F150), W143 (≠ H151), D228 (= D235), I230 (= I237), Q231 (= Q238), 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)
34% identity, 86% coverage: 39:435/463 of query aligns to 25:401/404 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 (≠ W64), G107 (= G123), V108 (≠ T124), F142 (= F150), W143 (≠ H151), E200 (≠ K208), D228 (= D235), I230 (= I237), Q231 (= Q238), K257 (= K265), R378 (≠ K412)
Query Sequence
>WP_013420082.1 NCBI__GCF_000166055.1:WP_013420082.1
MSIDIKSLFAENEAGRYALHTRHLNEQMVRVLKTIGYDVGFVRGQGAYLWDRAGDKYLDL
LSGWGVFALGRNNPKVNDALRQVLDSELPNLVQMDVSPLAGVVAERLLARAPWLDKAFFA
NSGTESVEAAIKFVRAATGRAGLAHCGHAFHGLSYGSLSLNGDQIFRKGFEGFLTDTVEV
PFNDLTALEDALKTKKIAGFFVEPIQGKGVHVPDDGYLKGVQELCKKYGTLFVADEIQTG
VGRTGKFFAIDHWPGVEPDLVLVAKALSGGHVPVGAVLTRKWIFDKLFNRMDRAVVHGST
FAKNDMAMAAALATLSILEEDGVIENAAAKGERLAASFRSMIGRHELMKDVRGKGLMIGI
EFGEPKSFALRMSWHALETANKGLFSQMITIPLFKEHKVLCQVAGHGMNIVKLLPALTLT
EDDCKWIEDSFEETIAAAHKVPGAAWSLGKTLAGHALKSRAEA
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