SitesBLAST
Comparing 8502096 FitnessBrowser__Miya:8502096 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)
Q988B8 Pyridoxamine--pyruvate transaminase; Pyridoxamine-pyruvate aminotransferase; EC 2.6.1.30 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) (see 2 papers)
32% identity, 98% coverage: 9:366/367 of query aligns to 12:370/393 of Q988B8
- E68 (= E66) binding ; mutation E->A,G: Low but detectable pyridoxamine--pyruvate transaminase activity.
- Y95 (≠ F93) binding
- T146 (= T144) binding
- K197 (= K196) modified: N6-(pyridoxal phosphate)lysine; mutation to L: Loss of function.
- C198 (= C197) mutation to A: No effect on enzyme activity.
- R336 (≠ F332) mutation to A: Strongly decreased affinity for pyruvate.
- R345 (= R341) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2z9xA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxyl-l-alanine (see paper)
32% identity, 98% coverage: 9:366/367 of query aligns to 11:369/392 of 2z9xA
2z9wA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxal (see paper)
32% identity, 98% coverage: 9:366/367 of query aligns to 11:369/392 of 2z9wA
2z9vA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxamine (see paper)
32% identity, 98% coverage: 9:366/367 of query aligns to 11:369/392 of 2z9vA
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
31% identity, 96% coverage: 13:366/367 of query aligns to 24:377/377 of 1vjoA
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
31% identity, 97% coverage: 11:365/367 of query aligns to 11:365/387 of 3islA
O32148 (S)-ureidoglycine--glyoxylate transaminase; UGXT; (S)-ureidoglycine--glyoxylate aminotransferase; Purine catabolism protein PucG; EC 2.6.1.112 from Bacillus subtilis (strain 168) (see paper)
30% identity, 97% coverage: 11:365/367 of query aligns to 15:387/416 of O32148
- Q37 (= Q34) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K196) modified: N6-(pyridoxal phosphate)lysine
- N264 (vs. gap) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
28% identity, 96% coverage: 13:366/367 of query aligns to 28:383/388 of 3kgwB
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
29% identity, 96% coverage: 13:366/367 of query aligns to 25:380/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P13), G26 (= G14), L346 (≠ F332), R355 (= R341)
- binding pyridoxal-5'-phosphate: S78 (≠ E66), G79 (= G67), H80 (≠ M68), W105 (≠ F93), S153 (≠ T144), D178 (= D170), V180 (= V172), K204 (= K196)
Sites not aligning to the query:
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
29% identity, 96% coverage: 13:366/367 of query aligns to 23:380/384 of 6rv0A
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
28% identity, 96% coverage: 14:367/367 of query aligns to 23:374/381 of 2dr1A
5hhyA Structure of human alanine:glyoxylate aminotransferase major allele (agt-ma) showing x-ray induced reduction of plp internal aldimine to 4'-deoxy-piridoxine-phosphate (plr) (see paper)
29% identity, 96% coverage: 13:366/367 of query aligns to 23:380/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ E66), G77 (= G67), H78 (≠ M68), W103 (≠ F93), S153 (≠ T144), D178 (= D170), V180 (= V172), Q203 (= Q195), K204 (= K196), Y255 (= Y245), T258 (≠ G248)
P21549 Alanine--glyoxylate aminotransferase; AGT; Serine--pyruvate aminotransferase; SPT; EC 2.6.1.44; EC 2.6.1.51 from Homo sapiens (Human) (see 24 papers)
29% identity, 96% coverage: 13:366/367 of query aligns to 28:385/392 of P21549
- R36 (≠ A21) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ M26) to E: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177168; to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of protein stability; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; partial mitochondrial mistargeting; intraperoxisomal protein aggregation seen; dbSNP:rs121908523; to V: in HP1; reduced alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177168
- G47 (= G33) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity; reduced expression levels; reduced pyridoxal phosphate binding; reduced dimerization; reduced thermostability; increased propensity to aggregation; increased susceptibility to proteolytic degradation within the N-terminal region; mitochondrial mistargeting; exposure to pyridoxine can rescue the functionality by partially preventing aggregation and degradation and by redirecting all the protein to the peroxisome; dbSNP:rs180177173
- G82 (= G67) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F93) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs180177197
- A112 (≠ I97) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ M136) to P: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ T138) to I: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in protein destabilization; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; mitochondrial mistargeting; dbSNP:rs121908524
- G156 (≠ C142) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T144) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G147) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; reduced peroxisomal localization; dbSNP:rs180177227; to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; loss of dimerization; dbSNP:rs180177227; to S: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; reduced peroxisomal localization; dbSNP:rs180177227
- L166 (= L152) to P: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (= G156) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in mitochondrial mistargeting; slight decrease in alanine--glyoxylate aminotransferase activity; loss of dimerization; partial loss of protein stability but protein stability increases in the presence of pyridoxal phosphate; causes protein aggregation; dbSNP:rs121908529
- C173 (vs. gap) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D170) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S174) to F: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization but improved dimerization in the presence of pyridoxal phosphate; decreased protein stability; dbSNP:rs180177238
- I202 (≠ L189) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ G192) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K196) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (= S205) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ V220) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908526; to H: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908527
- I244 (≠ F231) to T: in HP1; prevalent mutation in the Canary islands; when associated with L-11 and M-340 on the minor AGXT allele; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; partial mitochondrial mistargeting; dbSNP:rs121908525
- C253 (= C240) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ L260) to T: in dbSNP:rs140992177
- A280 (≠ N261) to V: in dbSNP:rs73106685
- V326 (= V308) to I: in dbSNP:rs115057148
- I340 (≠ R322) to M: associated with hyperoxaluria; dbSNP:rs4426527
Sites not aligning to the query:
- 9 T → N: no loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs115014558
- 11 P → L: reduction of specific alanine--glyoxylate aminotransferase activity in vitro; causes mitochondrial mistargeting when associated with R-170; dbSNP:rs34116584
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
28% identity, 96% coverage: 13:366/367 of query aligns to 24:378/383 of 3kgxA
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
29% identity, 96% coverage: 13:366/367 of query aligns to 25:382/387 of 1j04A
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
29% identity, 98% coverage: 9:366/367 of query aligns to 20:381/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (≠ E66), A78 (≠ G67), H79 (≠ M68), W104 (≠ F93), S154 (≠ T144), D179 (= D170), V181 (= V172), Q204 (= Q195), K205 (= K196), Y256 (≠ C240), T259 (= T243)
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
30% identity, 93% coverage: 9:350/367 of query aligns to 18:363/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G14), S41 (= S32), N42 (≠ Q34), S152 (≠ T144), Y254 (≠ W246), Q342 (≠ S329), L345 (≠ F332), R354 (= R341)
- binding pyridoxal-5'-phosphate: S75 (≠ E66), A76 (≠ G67), H77 (≠ M68), W102 (≠ F93), S152 (≠ T144), D177 (= D170), V179 (= V172), K203 (= K196), Y254 (≠ W246), T257 (= T249)
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
30% identity, 93% coverage: 9:350/367 of query aligns to 19:364/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (≠ E66), A77 (≠ G67), H78 (≠ M68), W103 (≠ F93), S153 (≠ T144), D178 (= D170), V180 (= V172), Q203 (= Q195), K204 (= K196), Y255 (≠ W246), T258 (= T249)
Q7PRG3 3-hydroxykynurenine transaminase; AgHKT; Alanine--glyoxylate aminotransferase; EC 2.6.1.63; EC 2.6.1.44 from Anopheles gambiae (African malaria mosquito) (see paper)
30% identity, 93% coverage: 9:350/367 of query aligns to 20:365/396 of Q7PRG3
- SAH 77:79 (≠ EGM 66:68) binding in other chain
- S154 (≠ T144) binding in other chain
- Q204 (= Q195) binding in other chain
- K205 (= K196) modified: N6-(pyridoxal phosphate)lysine
- Y256 (≠ W246) binding
- T259 (= T249) binding
Q0IG34 3-hydroxykynurenine transaminase; 3-hydroxykynurenine transaminase and alanine--glyoxylate aminotransferase; Ae-HKT/AGT; Alanine--glyoxylate aminotransferase; EC 2.6.1.63; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
29% identity, 98% coverage: 9:366/367 of query aligns to 20:381/400 of Q0IG34
- SAH 77:79 (≠ EGM 66:68) binding in other chain
- S154 (≠ T144) binding in other chain
- Q204 (= Q195) binding in other chain
- K205 (= K196) modified: N6-(pyridoxal phosphate)lysine
- Y256 (≠ C240) binding
- T259 (= T243) binding
Query Sequence
>8502096 FitnessBrowser__Miya:8502096
MAHKPYAPIPMVPGPVTLHPAVLTAMTRDYGSGQIEPDYLKLYAETGRNLAQLMGTQSDM
VLMTGEGMLALWAALKSCLVPGDRVLSVGTGVFGDGIGDMAAAIGCEVLKVSLPYNETID
DLTGIEDAIRSFKPKMLTAVHCETPSGTLNPLADLGALKQTCGVPLFYVDAVASVGGAPV
QADAWHADLVLGGSQKCLSAPPSMSFLSVSPAAWEVVEAVGYQGYDAIAPFRTVQQDGRC
PYTPYWHGTAALNAGALAILNEKGGMQGCFDRHREVAERCRAGLAKLGIDLWTAEGAVNS
PTVTAAIVPEGFTWPEWRQGLRERGLIVSGSFGPMAGKVFRLGHMGTQATEALVDAALDV
IESVMQD
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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