SitesBLAST
Comparing WP_012709136.1 NCBI__GCF_000018545.1:WP_012709136.1 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)
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)
55% identity, 96% coverage: 3:380/395 of query aligns to 8:386/401 of Q56YA5
- TGT 68:70 (≠ SGT 63:65) binding pyridoxal 5'-phosphate
- T148 (= T143) binding pyridoxal 5'-phosphate
- QK 200:201 (= QK 195:196) binding pyridoxal 5'-phosphate
- K201 (= K196) binding 3-hydroxypyruvate
- P251 (= P245) mutation to L: Abolishes aminotransferase activity.
- R347 (= R341) binding 3-hydroxypyruvate
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
55% identity, 96% coverage: 3:380/395 of query aligns to 6:384/399 of 6pk1A
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
55% identity, 96% coverage: 3:380/395 of query aligns to 7:385/400 of 6pk3B
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
30% identity, 95% coverage: 7:381/395 of query aligns to 10:382/387 of 3islA
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
32% identity, 86% coverage: 7:347/395 of query aligns to 22:362/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
32% identity, 86% coverage: 7:347/395 of query aligns to 22:362/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
32% identity, 86% coverage: 7:347/395 of query aligns to 22:362/385 of 2hufA
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
32% identity, 86% coverage: 7:347/395 of query aligns to 22:362/393 of Q3LSM4
- SGH 78:80 (≠ SGT 63:65) binding in other chain
- S155 (≠ T143) binding glyoxylate; binding L-alanine
- Q205 (= Q195) binding in other chain
- K206 (= K196) modified: N6-(pyridoxal phosphate)lysine
- Y257 (≠ F241) binding pyridoxal 5'-phosphate
- T260 (= T244) binding pyridoxal 5'-phosphate
- R356 (= R341) binding glyoxylate
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, 98% coverage: 7:392/395 of query aligns to 14:415/416 of O32148
- Q37 (≠ M30) 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.
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
33% identity, 87% coverage: 6:349/395 of query aligns to 18:357/381 of 2dr1A
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
32% identity, 87% coverage: 5:346/395 of query aligns to 19:362/387 of 1j04A
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
31% identity, 86% coverage: 7:346/395 of query aligns to 21:357/377 of 1vjoA
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)
32% identity, 87% coverage: 5:346/395 of query aligns to 17:360/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (= S63), G77 (= G64), H78 (≠ T65), W103 (≠ F90), S153 (≠ T143), D178 (= D170), V180 (= V172), Q203 (= Q195), K204 (= K196), Y255 (≠ F241), T258 (= T244)
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)
32% identity, 87% coverage: 5:346/395 of query aligns to 22:365/392 of P21549
- R36 (≠ Q18) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ M23) to E: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177168; to R: in HP1; associated in cis with L-11 and M-340; 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 (≠ D29) to R: in HP1; associated in cis with L-11 and M-340; 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 (= G64) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F90) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs180177197
- A112 (≠ W94) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ A135) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (= F137) to I: in HP1; associated in cis with L-11 and M-340; results in protein destabilization; no loss of dimerization; decreased alanine--glyoxylate aminotransferase activity; loss of alanine--glyoxylate aminotransferase activity when associated with L-11 and M-340; mitochondrial mistargeting when associated with L-11 and M-340; dbSNP:rs121908524
- G156 (≠ N141) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T143) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G146) to C: in HP1; associated in cis with L-11 and M-340; 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; associated in cis with L-11 and M-340; 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 (= L158) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (= G162) to R: in HP1; associated in cis with L-11 and M-340; 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; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and M-340; results in mitochondrial mistargeting when associated with L-11 and M-340; 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 (≠ C189) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (= S192) 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 (≠ G205) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ A220) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908526; to H: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908527
- I244 (= I233) to T: in HP1; associated in cis with L-11 and M-340; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity in vitro; no loss of dimerization; partial mitochondrial mistargeting; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and M-340; dbSNP:rs121908525
- C253 (vs. gap) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (= I260) to T: in dbSNP:rs140992177
- A280 (≠ F261) to V: in dbSNP:rs73106685
- V326 (≠ L307) to I: in dbSNP:rs115057148
- I340 (≠ F321) to M: in allele minor; associated in cis with L-11; no effect on alanine--glyoxylate aminotransferase activity in vitro; decreased specific alanine--glyoxylate aminotransferase activity in vitro when associated with L-11; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and I-152; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and R-170; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and T-244; results in mitochondrial mistargeting when associated with L-11 and R-170; dbSNP:rs4426527
Sites not aligning to the query:
- 9 T → N: no loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs115014558
- 11 P → L: in allele minor; associated in cis with M-340; decreased specific alanine--glyoxylate aminotransferase activity in vitro when associated with M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with I-152 and M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with R-170 and M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with T-244 and M-340; causes mitochondrial mistargeting when associated with R-170 and M-340; dbSNP:rs34116584
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
32% identity, 87% coverage: 5:346/395 of query aligns to 17:360/384 of 6rv0A
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
32% identity, 87% coverage: 5:346/395 of query aligns to 19:360/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P10), G26 (= G11), L346 (= L332), R355 (= R341)
- binding pyridoxal-5'-phosphate: S78 (= S63), G79 (= G64), H80 (≠ T65), W105 (≠ F90), S153 (≠ T143), D178 (= D170), V180 (= V172), K204 (= K196)
Sites not aligning to the query:
2bkwA Yeast alanine:glyoxylate aminotransferase yfl030w (see paper)
31% identity, 86% coverage: 7:346/395 of query aligns to 6:357/381 of 2bkwA
Sites not aligning to the query:
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
29% identity, 87% coverage: 10:351/395 of query aligns to 23:365/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (= S63), A77 (≠ G64), H78 (≠ T65), W103 (≠ F90), S153 (≠ T143), D178 (= D170), V180 (= V172), Q203 (= Q195), K204 (= K196), Y255 (vs. gap), T258 (= T244)
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
29% identity, 87% coverage: 10:351/395 of query aligns to 22:364/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G11), S41 (= S32), N42 (≠ P33), S152 (≠ T143), Y254 (vs. gap), Q342 (≠ G329), L345 (= L332), R354 (= R341)
- binding pyridoxal-5'-phosphate: S75 (= S63), A76 (≠ G64), H77 (≠ T65), W102 (≠ F90), S152 (≠ T143), D177 (= D170), V179 (= V172), K203 (= K196), Y254 (vs. gap), T257 (= T244)
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)
29% identity, 87% coverage: 10:351/395 of query aligns to 24:366/396 of Q7PRG3
- SAH 77:79 (≠ SGT 63:65) binding in other chain
- S154 (≠ T143) binding in other chain
- Q204 (= Q195) binding in other chain
- K205 (= K196) modified: N6-(pyridoxal phosphate)lysine
- Y256 (vs. gap) binding pyridoxal 5'-phosphate
- T259 (= T244) binding pyridoxal 5'-phosphate
Query Sequence
>WP_012709136.1 NCBI__GCF_000018545.1:WP_012709136.1
MSGYNHLFIPGPTNIPEQIRQAMNLPMEDMRSPRYPELTLPLFADVKKVFKNRNGRVFIY
PSSGTGAWEAAMTNVLSPGDRVLMSRFGQFSHLWVDMAERLGLEVDCLDREWGTGVPVDL
YTERLAADKAHRIKAVFVTHNETATGVTSDVAAVRAALDASGHPALLFVDGVSSIGSIDF
RQDEWGVDCAVSGSQKGFMLPAGLGFLSVSQKALEAAKTARHMRCYFSFEDMIKTNDTGY
FPYTPPTQLLHGLRAALDVIFEEGLENIFARHRHLADGVRAAVSAWGLKLCATEPKWYSD
TVSAIRLPEGIDGVKVIRHAFDTYNTSLGSGLSKVAGKVFRIGHLGSLNEVMVLGALSAA
ELTLLDCGVKIEPGAGVGAAIRQFRAAATATAKAA
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