SitesBLAST
Comparing WP_086511813.1 NCBI__GCF_002151265.1:WP_086511813.1 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)
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
45% identity, 95% coverage: 10:393/406 of query aligns to 6:388/399 of 6pk1A
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
45% identity, 95% coverage: 10:393/406 of query aligns to 7:389/400 of 6pk3B
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)
45% identity, 95% coverage: 10:393/406 of query aligns to 8:390/401 of Q56YA5
- TGT 68:70 (≠ SGT 69:71) binding
- T148 (= T153) binding
- QK 200:201 (= QK 205:206) binding
- K201 (= K206) binding
- P251 (= P255) mutation to L: Abolishes aminotransferase activity.
- R347 (= R351) binding
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
34% identity, 84% coverage: 17:356/406 of query aligns to 24:357/377 of 1vjoA
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
29% identity, 94% coverage: 14:395/406 of query aligns to 10:387/387 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)
29% identity, 94% coverage: 14:395/406 of query aligns to 14:409/416 of O32148
- Q37 (≠ H37) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K206) modified: N6-(pyridoxal phosphate)lysine
- N264 (vs. gap) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
30% identity, 85% coverage: 11:356/406 of query aligns to 16:354/381 of 2dr1A
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
33% identity, 84% coverage: 17:359/406 of query aligns to 25:364/387 of 1j04A
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
33% identity, 84% coverage: 17:359/406 of query aligns to 25:362/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P17), G26 (= G18), L346 (= L342), R355 (= R351)
- binding pyridoxal-5'-phosphate: S78 (= S69), G79 (= G70), H80 (≠ T71), W105 (≠ F96), S153 (≠ T153), D178 (= D180), V180 (≠ I182), K204 (= K206)
Sites not aligning to the query:
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, 86% coverage: 17:364/406 of query aligns to 24:369/400 of Q0IG34
- SAH 77:79 (≠ SGT 69:71) binding in other chain
- S154 (≠ T153) binding in other chain
- Q204 (= Q205) binding in other chain
- K205 (= K206) modified: N6-(pyridoxal phosphate)lysine
- Y256 (vs. gap) binding
- T259 (= T254) binding
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
30% identity, 86% coverage: 17:364/406 of query aligns to 22:367/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G18), S41 (≠ D36), N42 (≠ H37), S152 (≠ T153), Y254 (vs. gap), Q342 (≠ G339), L345 (= L342), R354 (= R351)
- binding pyridoxal-5'-phosphate: S75 (= S69), A76 (≠ G70), H77 (≠ T71), W102 (≠ F96), S152 (≠ T153), D177 (= D180), V179 (≠ I182), K203 (= K206), Y254 (vs. gap), T257 (= T254)
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, 86% coverage: 17:364/406 of query aligns to 24:369/396 of Q7PRG3
- SAH 77:79 (≠ SGT 69:71) binding in other chain
- S154 (≠ T153) binding in other chain
- Q204 (= Q205) binding in other chain
- K205 (= K206) modified: N6-(pyridoxal phosphate)lysine
- Y256 (vs. gap) binding
- T259 (= T254) binding
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
30% identity, 86% coverage: 17:364/406 of query aligns to 23:368/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (= S69), A77 (≠ G70), H78 (≠ T71), W103 (≠ F96), S153 (≠ T153), D178 (= D180), V180 (≠ I182), Q203 (= Q205), K204 (= K206), Y255 (vs. gap), T258 (= T254)
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)
33% identity, 84% coverage: 17:359/406 of query aligns to 23:362/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (= S69), G77 (= G70), H78 (≠ T71), W103 (= W100), S153 (≠ T153), D178 (= D180), V180 (≠ I182), Q203 (= Q205), K204 (= K206), Y255 (≠ W251), T258 (= T254)
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
33% identity, 84% coverage: 17:359/406 of query aligns to 23:362/384 of 6rv0A
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)
33% identity, 84% coverage: 17:359/406 of query aligns to 28:367/392 of P21549
- R36 (= R25) 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 (≠ D36) 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 (= W100) 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 (= A104) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ A145) 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 (≠ C147) 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 (≠ N151) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T153) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G156) 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 (≠ I161) 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 (≠ R165) 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 (≠ I168) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D180) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (≠ G184) 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 (≠ V199) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (= S202) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K206) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (= S215) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (= R228) 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 (≠ E241) 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 (vs. gap) 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 (≠ L270) to T: in dbSNP:rs140992177
- A280 (≠ L271) to V: in dbSNP:rs73106685
- V326 (≠ M317) to I: in dbSNP:rs115057148
- I340 (≠ Y331) 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
2z9xA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxyl-l-alanine (see paper)
30% identity, 92% coverage: 18:390/406 of query aligns to 16:385/392 of 2z9xA
2z9wA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxal (see paper)
30% identity, 92% coverage: 18:390/406 of query aligns to 16:385/392 of 2z9wA
2z9vA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxamine (see paper)
30% identity, 92% coverage: 18:390/406 of query aligns to 16:385/392 of 2z9vA
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
29% identity, 86% coverage: 17:364/406 of query aligns to 24:369/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (= S69), A78 (≠ G70), H79 (≠ T71), W104 (≠ F96), S154 (≠ T153), D179 (= D180), V181 (≠ I182), Q204 (= Q205), K205 (= K206), Y256 (vs. gap), T259 (= T254)
Query Sequence
>WP_086511813.1 NCBI__GCF_002151265.1:WP_086511813.1
MLNLDFHPSGRHFLQIPGPSPVPDRILRAMSLPTIDHRGPEFGALGLELLAKLKQVFKTE
GPVMIYPASGTGAWEAALANVLSPGDRVLMYETGHFAALWHKMALRLQLEPEFIGLPGYE
GWRQGVQADMIEARLREDAEHRLKAVCVVHNETSTGVTSDIAAVRRAIDAAGHPALLLVD
TISGLASADYRHDEWGVDVTISGSQKGLMLPPGISFNALSDKAIAASRESTMPRSFWAWD
EILEANRNGYWPYTPSTNLLYGLNEALDMLLDEGLEHVFARHQRWAAGVRTAVEAWGLEI
QCQDPALYSPVLTGVVMPDGVDADAVRKIIYERFDLSLGMGLGKAKGKMFRIGHLGDCND
LTLIATLGGCEAGMKLCGVPLAGSGVAAALEYFADNPLRSSDSCNG
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