SitesBLAST
Comparing YP_004141244.1 NCBI__GCF_000185905.1:YP_004141244.1 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)
53% identity, 96% coverage: 4:389/401 of query aligns to 6:392/399 of 6pk1A
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)
53% identity, 96% coverage: 4:389/401 of query aligns to 8:394/401 of Q56YA5
- TGT 68:70 (≠ SGT 64:66) binding
- T148 (= T144) binding
- QK 200:201 (= QK 196:197) binding
- K201 (= K197) binding
- P251 (= P246) mutation to L: Abolishes aminotransferase activity.
- R347 (= R342) binding
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
53% identity, 96% coverage: 4:389/401 of query aligns to 7:393/400 of 6pk3B
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
31% identity, 85% coverage: 8:347/401 of query aligns to 22:361/393 of Q3LSM4
- SGH 78:80 (≠ SGT 64:66) binding in other chain
- S155 (≠ T144) binding ; binding
- Q205 (= Q196) binding in other chain
- K206 (= K197) modified: N6-(pyridoxal phosphate)lysine
- Y257 (≠ F242) binding
- T260 (= T245) binding
- R356 (= R342) binding
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
31% identity, 85% coverage: 8:347/401 of query aligns to 22:361/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
31% identity, 85% coverage: 8:347/401 of query aligns to 22:361/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
31% identity, 85% coverage: 8:347/401 of query aligns to 22:361/385 of 2hufA
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
31% identity, 85% coverage: 8:347/401 of query aligns to 21:357/377 of 1vjoA
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
30% identity, 86% coverage: 7:350/401 of query aligns to 18:357/381 of 2dr1A
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
27% identity, 94% coverage: 8:385/401 of query aligns to 10:385/387 of 3islA
2bkwA Yeast alanine:glyoxylate aminotransferase yfl030w (see paper)
31% identity, 85% coverage: 8:347/401 of query aligns to 6:357/381 of 2bkwA
Sites not aligning to the query:
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)
27% identity, 94% coverage: 8:385/401 of query aligns to 14:407/416 of O32148
- Q37 (≠ M31) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K197) modified: N6-(pyridoxal phosphate)lysine
- N264 (≠ F242) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
28% identity, 85% coverage: 11:352/401 of query aligns to 22:364/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G12), S41 (≠ Q29), N42 (≠ D30), S152 (≠ T144), Y254 (vs. gap), Q342 (≠ G330), L345 (= L333), R354 (= R342)
- binding pyridoxal-5'-phosphate: S75 (= S64), A76 (≠ G65), H77 (≠ T66), W102 (≠ F91), S152 (≠ T144), D177 (= D171), V179 (= V173), K203 (= K197), Y254 (vs. gap), T257 (= T245)
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
28% identity, 85% coverage: 11:352/401 of query aligns to 23:365/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (= S64), A77 (≠ G65), H78 (≠ T66), W103 (≠ F91), S153 (≠ T144), D178 (= D171), V180 (= V173), Q203 (= Q196), K204 (= K197), Y255 (vs. gap), T258 (= T245)
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, 85% coverage: 11:352/401 of query aligns to 24:366/396 of Q7PRG3
- SAH 77:79 (≠ SGT 64:66) binding in other chain
- S154 (≠ T144) binding in other chain
- Q204 (= Q196) binding in other chain
- K205 (= K197) modified: N6-(pyridoxal phosphate)lysine
- Y256 (vs. gap) binding
- T259 (= T245) binding
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
28% identity, 85% coverage: 8:347/401 of query aligns to 22:362/387 of 1j04A
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
26% identity, 84% coverage: 11:348/401 of query aligns to 24:362/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (= S64), A78 (≠ G65), H79 (≠ T66), W104 (≠ F91), S154 (≠ T144), D179 (= D171), V181 (= V173), Q204 (= Q196), K205 (= K197), Y256 (vs. gap), T259 (= T245)
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)
26% identity, 84% coverage: 11:348/401 of query aligns to 24:362/400 of Q0IG34
- SAH 77:79 (≠ SGT 64:66) binding in other chain
- S154 (≠ T144) binding in other chain
- Q204 (= Q196) binding in other chain
- K205 (= K197) modified: N6-(pyridoxal phosphate)lysine
- Y256 (vs. gap) binding
- T259 (= T245) binding
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)
28% identity, 85% coverage: 8:347/401 of query aligns to 25:365/392 of P21549
- R36 (≠ A19) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ M24) 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 (≠ D30) 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 (= G65) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F91) 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 (≠ W95) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ A136) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (= F138) 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 (≠ N142) 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; 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 (≠ I152) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ D160) 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 (≠ A163) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D171) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S175) 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 (≠ L190) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ T193) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K197) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (≠ G206) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ H222) 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 (≠ M233) 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 (≠ A235) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (= I261) to T: in dbSNP:rs140992177
- A280 (≠ F262) to V: in dbSNP:rs73106685
- V326 (= V308) to I: in dbSNP:rs115057148
- I340 (≠ Y322) 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
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)
28% identity, 85% coverage: 8:347/401 of query aligns to 20:360/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (= S64), G77 (= G65), H78 (≠ T66), W103 (≠ F91), S153 (≠ T144), D178 (= D171), V180 (= V173), Q203 (= Q196), K204 (= K197), Y255 (≠ F242), T258 (= T245)
Query Sequence
>YP_004141244.1 NCBI__GCF_000185905.1:YP_004141244.1
MKNGTAHLFIPGPTNIPDAVRRAMNVPMQDMRAPDFPELVLPLFRDLKQIFKTETGSVFI
FPGSGTGAWEAAISNTLNRGDRVLMSRFGQFSHLWVDMAERLGLKVDCVDVEWGEGVPLD
AYRQRLGDDKGHEIKAVFATHNETATGVTSDIAGVRAALDETAHDALLFVDGVSSIGSID
FRMDEWGVDLAITGSQKGLMLPAGLGILAVSAKGLEAHKQSHMERCYFSFEDMQASSKTG
FFPYTPPTQLLLGLRASLDLIFAEGLEQIFARHHRLAEGVRRGVHAWGLKLCANEEKWWS
DTVSAIVVSEDVDARQVIANGYSRYRTSFGAGLSKVAGRVFRIGHLGDLNEVMCLAALAS
AEMSLRDAGARIEAGSGVAAAQEWYRAEIGRTLQPRHERAA
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