SitesBLAST
Comparing GFF2363 FitnessBrowser__Phaeo:GFF2363 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)
Q56YA5 Serine--glyoxylate aminotransferase; Alanine--glyoxylate aminotransferase; AGT; Asparagine aminotransferase; Serine--pyruvate aminotransferase; EC 2.6.1.45; EC 2.6.1.44; EC 2.6.1.-; EC 2.6.1.51 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
36% identity, 94% coverage: 4:398/421 of query aligns to 2:390/401 of Q56YA5
- TGT 68:70 (≠ NGH 69:71) binding
- T148 (= T149) binding
- QK 200:201 (= QK 201:202) binding
- K201 (= K202) binding
- P251 (≠ A252) mutation to L: Abolishes aminotransferase activity.
- R347 (= R357) binding
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
36% identity, 94% coverage: 4:398/421 of query aligns to 1:389/400 of 6pk3B
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
36% identity, 92% coverage: 10:398/421 of query aligns to 6:388/399 of 6pk1A
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
30% identity, 72% coverage: 17:318/421 of query aligns to 24:322/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (≠ N69), A78 (≠ G70), H79 (= H71), W104 (≠ F96), S154 (≠ T149), D179 (= D176), V181 (≠ I178), Q204 (= Q201), K205 (= K202), Y256 (≠ F248), T259 (= T251)
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)
30% identity, 72% coverage: 17:318/421 of query aligns to 24:322/400 of Q0IG34
- SAH 77:79 (≠ NGH 69:71) binding in other chain
- S154 (≠ T149) binding in other chain
- Q204 (= Q201) binding in other chain
- K205 (= K202) modified: N6-(pyridoxal phosphate)lysine
- Y256 (≠ F248) binding
- T259 (= T251) binding
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
28% identity, 87% coverage: 17:382/421 of query aligns to 23:381/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (≠ N69), A77 (≠ G70), H78 (= H71), W103 (≠ F96), S153 (≠ T149), D178 (= D176), V180 (≠ I178), Q203 (= Q201), K204 (= K202), Y255 (≠ F244), T258 (= T251)
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
28% identity, 87% coverage: 17:382/421 of query aligns to 22:380/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G18), S41 (≠ N36), N42 (≠ I37), S152 (≠ T149), Y254 (≠ F244), Q342 (≠ G339), L345 (= L342), R354 (= R357)
- binding pyridoxal-5'-phosphate: S75 (≠ N69), A76 (≠ G70), H77 (= H71), W102 (≠ F96), S152 (≠ T149), D177 (= D176), V179 (≠ I178), K203 (= K202), Y254 (≠ F244), T257 (= T251)
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)
28% identity, 87% coverage: 17:382/421 of query aligns to 24:382/396 of Q7PRG3
- SAH 77:79 (≠ NGH 69:71) binding in other chain
- S154 (≠ T149) binding in other chain
- Q204 (= Q201) binding in other chain
- K205 (= K202) modified: N6-(pyridoxal phosphate)lysine
- Y256 (≠ F244) binding
- T259 (= T251) binding
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
27% identity, 82% coverage: 17:362/421 of query aligns to 25:362/387 of 1j04A
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
30% identity, 64% coverage: 17:287/421 of query aligns to 25:296/393 of Q3LSM4
- SGH 78:80 (≠ NGH 69:71) binding in other chain
- S155 (≠ T149) binding ; binding
- Q205 (= Q201) binding in other chain
- K206 (= K202) modified: N6-(pyridoxal phosphate)lysine
- Y257 (≠ T254) binding
- T260 (vs. gap) binding
Sites not aligning to the query:
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
30% identity, 64% coverage: 17:287/421 of query aligns to 25:296/385 of 2huuA
Sites not aligning to the query:
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
30% identity, 64% coverage: 17:287/421 of query aligns to 25:296/385 of 2huiA
Sites not aligning to the query:
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
30% identity, 64% coverage: 17:287/421 of query aligns to 25:296/385 of 2hufA
Sites not aligning to the query:
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
25% identity, 82% coverage: 17:363/421 of query aligns to 24:359/383 of 3kgxA
Sites not aligning to the query:
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
27% identity, 82% coverage: 17:362/421 of query aligns to 23:360/384 of 6rv0A
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
25% identity, 82% coverage: 17:363/421 of query aligns to 28:364/388 of 3kgwB
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)
27% identity, 82% coverage: 17:362/421 of query aligns to 23:360/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ N69), G77 (= G70), H78 (= H71), W103 (≠ F96), S153 (≠ T149), D178 (= D176), V180 (≠ I178), Q203 (= Q201), K204 (= K202), Y255 (≠ F248), T258 (= T251)
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)
27% identity, 82% coverage: 17:362/421 of query aligns to 28:365/392 of P21549
- R36 (≠ A25) 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 (≠ M30) 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 (≠ N36) 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 (= G70) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F96) 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 (≠ W100) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ A141) 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 (≠ L143) 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 (≠ V147) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T149) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (≠ S152) 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 (≠ M160) 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 (≠ L164) 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 (= C167) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D176) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S180) 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 (≠ V195) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ A198) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K202) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (≠ G211) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (= R223) 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 (≠ W235) 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 (≠ P241) 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 (= I267) to T: in dbSNP:rs140992177
- A280 (≠ H268) to V: in dbSNP:rs73106685
- V326 (≠ L318) to I: in dbSNP:rs115057148
- I340 (≠ E331) 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
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
30% identity, 66% coverage: 17:294/421 of query aligns to 24:299/377 of 1vjoA
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
27% identity, 91% coverage: 14:398/421 of query aligns to 10:384/387 of 3islA
Query Sequence
>GFF2363 FitnessBrowser__Phaeo:GFF2363
MTADVSLAAGRGYLAIPGPSVIPDAVLQAMHRPSPNIYAGELVEMTATLIPDLRRVARTE
HNVAIYISNGHGAWEAALQNTLQPGDTVLVASSGRFAIGWSEMAEALGIKVELLDFGTGA
PWDMDRIASHLAADTAHRIKAVLAVHVDTSSSIRNDVAAMRAALDACDHPALLMADCIAS
LGCDRFEMDAWGVDVMVAACQKGLMVPAGMGFVFFSPKAAEARARLPRVSRYWDWEPRAN
PEEFYQYFGGTAPTHHLYGLRAALDLIHGEGMEAVWARHHRLAQAIWAACDRWGDGGPLR
MNVQDVALRSNAVTSLHLGGDEATRLRTWVEQTLGLTLGIGLGMAPPNSPEWHGFLRLGH
MGHVSGQMIMGLLGGVDAGLKALEIPHGSGALEAASQVIAGAGATAVPASPELSAVGSCC
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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