SitesBLAST
Comparing Pf6N2E2_1623 Siderophore biosynthesis diaminobutyrate--2-oxoglutarate aminotransferase (EC 2.6.1.76) to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
6rl5G The first crystal structure of the daba aminotransferase ectb in the ectoine biosynthesis pathway of the model organism chromohalobacter salexigens dsm 3034 (see paper)
38% identity, 86% coverage: 40:450/476 of query aligns to 9:404/422 of 6rl5G
- active site: S16 (≠ P47), F137 (≠ Y168), D237 (= D276), K266 (= K305)
- binding pyridoxal-5'-phosphate: G110 (= G141), T111 (≠ A142), F137 (≠ Y168), H138 (= H169), D237 (= D276), I239 (≠ V278), Q240 (= Q279), K266 (= K305), G294 (= G332), T295 (= T333)
O58478 Alanine/serine racemase; ASR; Ala/Ser racemase; EC 5.1.1.-; EC 5.1.1.1 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
31% identity, 98% coverage: 10:474/476 of query aligns to 7:474/474 of O58478
- D251 (≠ E248) mutation to A: Loss of activity.
- K308 (= K305) mutation to A: Loss of activity.
7vo1A Structure of aminotransferase-substrate complex (see paper)
33% identity, 90% coverage: 47:474/476 of query aligns to 31:452/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ A77), S121 (≠ T140), G122 (= G141), T123 (≠ A142), F149 (≠ Y168), H150 (= H169), R152 (≠ M171), E234 (= E248), D262 (= D276), V264 (= V278), Q265 (= Q279), K291 (= K305), N318 (≠ G332), T319 (= T333), R417 (= R438)
7vntA Structure of aminotransferase-substrate complex (see paper)
33% identity, 90% coverage: 47:474/476 of query aligns to 31:452/452 of 7vntA
- binding L-ornithine: F149 (≠ Y168), R152 (≠ M171), E234 (= E248), K291 (= K305)
- binding pyridoxal-5'-phosphate: G122 (= G141), T123 (≠ A142), F149 (≠ Y168), H150 (= H169), E229 (= E243), D262 (= D276), V264 (= V278), Q265 (= Q279), K291 (= K305)
7vnoA Structure of aminotransferase (see paper)
33% identity, 90% coverage: 47:474/476 of query aligns to 31:452/452 of 7vnoA
O50131 Ornithine aminotransferase; Orn-AT; Ornithine delta-aminotransferase; EC 2.6.1.13 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
33% identity, 90% coverage: 47:474/476 of query aligns to 33:454/454 of O50131
- T92 (≠ L106) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (= D107) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G141) binding
- T125 (≠ A142) binding
- Q267 (= Q279) binding
- K293 (= K305) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T333) binding
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 86% coverage: 52:462/476 of query aligns to 21:387/387 of 1wkhA
- active site: F132 (≠ Y168), E184 (= E243), D217 (= D276), Q220 (= Q279), K246 (= K305), T275 (= T333), R363 (= R438)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ A77), S104 (≠ T140), G105 (= G141), T106 (≠ A142), F132 (≠ Y168), S133 (≠ H169), E184 (= E243), E189 (= E248), D217 (= D276), I219 (≠ V278), K246 (= K305), R363 (= R438)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 86% coverage: 52:462/476 of query aligns to 21:387/387 of 1wkgA
- active site: F132 (≠ Y168), E184 (= E243), D217 (= D276), Q220 (= Q279), K246 (= K305), T275 (= T333), R363 (= R438)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ A77), G105 (= G141), T106 (≠ A142), F132 (≠ Y168), S133 (≠ H169), R135 (≠ M171), E184 (= E243), D217 (= D276), I219 (≠ V278), Q220 (= Q279), K246 (= K305), G273 (≠ A331), T274 (≠ G332), T275 (= T333)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 86% coverage: 52:462/476 of query aligns to 21:387/387 of 1vefA
- active site: F132 (≠ Y168), D217 (= D276), K246 (= K305), T275 (= T333), R363 (= R438)
- binding pyridoxal-5'-phosphate: G105 (= G141), T106 (≠ A142), F132 (≠ Y168), S133 (≠ H169), E184 (= E243), D217 (= D276), I219 (≠ V278), K246 (= K305)
Sites not aligning to the query:
P50457 4-aminobutyrate aminotransferase PuuE; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; EC 2.6.1.19 from Escherichia coli (strain K12) (see paper)
36% identity, 86% coverage: 55:463/476 of query aligns to 27:421/421 of P50457
- K267 (= K305) mutation to A: No GABA-AT activity.
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
36% identity, 86% coverage: 52:462/476 of query aligns to 29:395/395 of Q5SHH5
- GT 113:114 (≠ GA 141:142) binding
- K254 (= K305) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T333) binding
4uoxA Crystal structure of ygjg in complex with pyridoxal-5'-phosphate and putrescine (see paper)
33% identity, 85% coverage: 64:469/476 of query aligns to 72:451/453 of 4uoxA
- active site: F174 (≠ Y168), E232 (= E243), D265 (= D276), Q268 (= Q279), K294 (= K305), T326 (= T333), R420 (= R438)
- binding pyridoxal-5'-phosphate: S143 (≠ T140), G144 (= G141), T145 (≠ A142), F174 (≠ Y168), H175 (= H169), G176 (= G170), D265 (= D276), V267 (= V278), Q268 (= Q279), T325 (≠ G332), T326 (= T333)
- binding 1,4-diaminobutane: E237 (= E248), K294 (= K305)
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)
32% identity, 85% coverage: 64:469/476 of query aligns to 78:457/459 of P42588
- GT 150:151 (≠ GA 141:142) binding in other chain
- Q274 (= Q279) binding in other chain
- K300 (= K305) modified: N6-(pyridoxal phosphate)lysine
- T332 (= T333) binding
4uoxC Crystal structure of ygjg in complex with pyridoxal-5'-phosphate and putrescine (see paper)
32% identity, 85% coverage: 64:469/476 of query aligns to 76:455/456 of 4uoxC
- active site: F178 (≠ Y168), E236 (= E243), D269 (= D276), Q272 (= Q279), K298 (= K305), T330 (= T333), R424 (= R438)
- binding pyridoxal-5'-phosphate: S147 (≠ T140), G148 (= G141), T149 (≠ A142), F178 (≠ Y168), H179 (= H169), G180 (= G170), D269 (= D276), V271 (= V278), Q272 (= Q279), K298 (= K305), T329 (≠ G332), T330 (= T333)
Sites not aligning to the query:
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)
32% identity, 86% coverage: 48:457/476 of query aligns to 42:450/464 of 4ppmA
- active site: Y159 (= Y168), E212 (= E243), D245 (= D276), Q248 (= Q279), K274 (= K305), T309 (= T333), R431 (= R438)
- binding magnesium ion: A351 (≠ Q375), Y354 (= Y378), V357 (≠ L381)
- binding pyridoxal-5'-phosphate: G132 (= G141), T133 (≠ A142), Y159 (= Y168), H160 (= H169), D245 (= D276), V247 (= V278), K274 (= K305)
Sites not aligning to the query:
A0A0J9X1Q5 Aminotransferase PigE; EC 2.6.1.- from Serratia sp. (strain FS14) (see paper)
32% identity, 86% coverage: 48:457/476 of query aligns to 413:841/853 of A0A0J9X1Q5
- GT 503:504 (≠ GA 141:142) binding
- K645 (= K305) modified: N6-(pyridoxal phosphate)lysine
- T680 (= T333) binding
1d7vA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with nma (see paper)
33% identity, 91% coverage: 33:465/476 of query aligns to 1:431/431 of 1d7vA
- active site: G19 (vs. gap), W136 (≠ Y168), E208 (= E243), D241 (= D276), Q244 (= Q279), K270 (= K305), T301 (= T333), R404 (= R438)
- binding potassium ion: H75 (≠ P102), L76 (= L103), F77 (≠ H104), S78 (≠ T105), T301 (= T333), H302 (≠ F334), V303 (≠ R335), S304 (≠ G336), D305 (≠ N337)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-2-methylalanine: A110 (= A142), W136 (≠ Y168), H137 (= H169), E208 (= E243), S213 (≠ E248), D241 (= D276), A243 (≠ V278), Q244 (= Q279), K270 (= K305), R404 (= R438)
1d7uA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with lcs (see paper)
33% identity, 91% coverage: 33:465/476 of query aligns to 1:431/431 of 1d7uA
- active site: G19 (vs. gap), W136 (≠ Y168), E208 (= E243), D241 (= D276), Q244 (= Q279), K270 (= K305), T301 (= T333), R404 (= R438)
- binding potassium ion: H75 (≠ P102), L76 (= L103), F77 (≠ H104), S78 (≠ T105), T301 (= T333), H302 (≠ F334), V303 (≠ R335), S304 (≠ G336), D305 (≠ N337)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G109 (= G141), A110 (= A142), W136 (≠ Y168), H137 (= H169), E208 (= E243), D241 (= D276), A243 (≠ V278), Q244 (= Q279), K270 (= K305), R404 (= R438)
1d7sA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with dcs (see paper)
33% identity, 91% coverage: 33:465/476 of query aligns to 1:431/431 of 1d7sA
- active site: G19 (vs. gap), W136 (≠ Y168), E208 (= E243), D241 (= D276), Q244 (= Q279), K270 (= K305), T301 (= T333), R404 (= R438)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: Q50 (≠ A77), G109 (= G141), A110 (= A142), W136 (≠ Y168), H137 (= H169), E208 (= E243), D241 (= D276), A243 (≠ V278), Q244 (= Q279), K270 (= K305), R404 (= R438)
- binding potassium ion: H75 (≠ P102), L76 (= L103), F77 (≠ H104), S78 (≠ T105), T301 (= T333), H302 (≠ F334), V303 (≠ R335), S304 (≠ G336), D305 (≠ N337)
1d7rA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with 5pa (see paper)
33% identity, 91% coverage: 33:465/476 of query aligns to 1:431/431 of 1d7rA
- active site: G19 (vs. gap), W136 (≠ Y168), E208 (= E243), D241 (= D276), Q244 (= Q279), K270 (= K305), T301 (= T333), R404 (= R438)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: G109 (= G141), A110 (= A142), W136 (≠ Y168), H137 (= H169), E208 (= E243), S213 (≠ E248), D241 (= D276), A243 (≠ V278), Q244 (= Q279), K270 (= K305), R404 (= R438)
- binding potassium ion: H75 (≠ P102), L76 (= L103), F77 (≠ H104), S78 (≠ T105), T301 (= T333), H302 (≠ F334), V303 (≠ R335), S304 (≠ G336), D305 (≠ N337)
Query Sequence
>Pf6N2E2_1623 Siderophore biosynthesis diaminobutyrate--2-oxoglutarate aminotransferase (EC 2.6.1.76)
MESVQPRLSSSATFTLEQFRQQAPRELNTNPYLQRQAARESNARSYPRRIPLALQEAHGL
YVRDTQGQLFMDCLAGAGTLALGHNHPVAIAAMRQTLDSGLPLHTLDLTTPVKDRFVEDL
FNALPENFARHARIQFCGPTGADGIEAALKLARTATGRKPILSFSGGYHGMTLGTLSLMG
NLGPKQALGSLMADVQFLPYPYDYRCPFGIGGEAGVDAGLHFIEQLLSDPESGVLPPAAV
VVEVVQGEGGVIPAPIRWLQGLRQLTRKFGVALIIDEVQTGLGRTGKLFAFEHADIEPDI
LVLSKAIGGGLPLAVMVYREELDTWKPGAHAGTFRGNQMAMAAGAATLRHIISEDLPGHA
DVMGQRLMAALRQLQDRYACLGQVRGRGLMVGVEIVSDTASDSRVPAADTALAQAIQRQC
LRLGVILELGGRHGAVVRFLPPLIIQAEEVDVLVELFQVALANALVEVKGRTLHIA
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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