SitesBLAST
Comparing BWI76_RS10590 FitnessBrowser__Koxy:BWI76_RS10590 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)
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)
51% identity, 97% coverage: 8:409/413 of query aligns to 6:409/416 of O32148
- Q37 (= Q39) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K200) modified: N6-(pyridoxal phosphate)lysine
- N264 (= N264) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
49% identity, 97% coverage: 8:409/413 of query aligns to 2:387/387 of 3islA
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
39% identity, 93% coverage: 5:387/413 of query aligns to 10:376/377 of 1vjoA
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
36% identity, 86% coverage: 12:368/413 of query aligns to 16:360/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (≠ T72), A77 (≠ S73), H78 (≠ R74), W103 (≠ F99), S153 (≠ T149), D178 (= D174), V180 (≠ T176), Q203 (= Q199), K204 (= K200), Y255 (≠ L263), T258 (= T267)
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
36% identity, 86% coverage: 12:368/413 of query aligns to 15:359/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G20), S41 (≠ G38), N42 (≠ Q39), S152 (≠ T149), Y254 (≠ L263), Q342 (≠ G351), L345 (≠ F354), R354 (= R363)
- binding pyridoxal-5'-phosphate: S75 (≠ T72), A76 (≠ S73), H77 (≠ R74), W102 (≠ F99), S152 (≠ T149), D177 (= D174), V179 (≠ T176), K203 (= K200), Y254 (≠ L263), T257 (= T267)
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)
36% identity, 86% coverage: 12:368/413 of query aligns to 17:361/396 of Q7PRG3
- SAH 77:79 (≠ TSR 72:74) binding in other chain
- S154 (≠ T149) binding in other chain
- Q204 (= Q199) binding in other chain
- K205 (= K200) modified: N6-(pyridoxal phosphate)lysine
- Y256 (≠ L263) binding
- T259 (= T267) binding
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
34% identity, 91% coverage: 12:388/413 of query aligns to 17:381/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (≠ T72), A78 (≠ S73), H79 (≠ R74), W104 (≠ F99), S154 (≠ T149), D179 (= D174), V181 (≠ T176), Q204 (= Q199), K205 (= K200), Y256 (≠ N264), T259 (= T267)
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
34% identity, 93% coverage: 9:391/413 of query aligns to 15:384/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
34% identity, 93% coverage: 9:391/413 of query aligns to 15:384/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
34% identity, 93% coverage: 9:391/413 of query aligns to 15:384/385 of 2hufA
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
34% identity, 93% coverage: 9:391/413 of query aligns to 15:384/393 of Q3LSM4
- SGH 78:80 (≠ TSR 72:74) binding in other chain
- S155 (≠ T149) binding ; binding
- Q205 (= Q199) binding in other chain
- K206 (= K200) modified: N6-(pyridoxal phosphate)lysine
- Y257 (≠ N264) binding
- T260 (= T267) binding
- R356 (= R363) 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)
34% identity, 91% coverage: 12:388/413 of query aligns to 17:381/400 of Q0IG34
- SAH 77:79 (≠ TSR 72:74) binding in other chain
- S154 (≠ T149) binding in other chain
- Q204 (= Q199) binding in other chain
- K205 (= K200) modified: N6-(pyridoxal phosphate)lysine
- Y256 (≠ N264) binding
- T259 (= T267) 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)
34% identity, 92% coverage: 9:389/413 of query aligns to 18:386/392 of P21549
- R36 (= R27) 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 (≠ M32) 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 (= G38) 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 (≠ S73) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F99) 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 (≠ L103) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (= L141) 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 (= G147) 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 (≠ T152) 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 (= L157) 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 (= G161) 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 (= C164) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D174) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S178) 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 (≠ A193) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ A196) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K200) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (= S209) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (= R224) 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 (≠ L251) 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 (≠ P260) 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 (= I283) to T: in dbSNP:rs140992177
- A280 (≠ L284) to V: in dbSNP:rs73106685
- V326 (≠ I329) to I: in dbSNP:rs115057148
- I340 (≠ L343) 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
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)
34% identity, 92% coverage: 9:389/413 of query aligns to 13:381/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ T72), G77 (≠ S73), H78 (≠ R74), W103 (≠ F99), S153 (≠ T149), D178 (= D174), V180 (≠ T176), Q203 (= Q199), K204 (= K200), Y255 (≠ N264), T258 (= T267)
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
35% identity, 92% coverage: 9:389/413 of query aligns to 14:379/383 of 3kgxA
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
34% identity, 92% coverage: 9:389/413 of query aligns to 13:381/384 of 6rv0A
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
35% identity, 92% coverage: 9:389/413 of query aligns to 18:384/388 of 3kgwB
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
34% identity, 92% coverage: 9:389/413 of query aligns to 15:383/387 of 1j04A
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
34% identity, 92% coverage: 9:389/413 of query aligns to 15:381/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P19), G26 (= G20), L346 (≠ F354), R355 (= R363)
- binding pyridoxal-5'-phosphate: S78 (≠ T72), G79 (≠ S73), H80 (≠ R74), W105 (≠ F99), S153 (≠ T149), D178 (= D174), V180 (≠ T176), K204 (= K200)
Sites not aligning to the query:
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
26% identity, 93% coverage: 8:391/413 of query aligns to 11:376/381 of 2dr1A
Query Sequence
>BWI76_RS10590 FitnessBrowser__Koxy:BWI76_RS10590
MDITQFSQLNPPSRLLMGPGPINADPRVLRAMSSQLIGQYDPAMTHYMNEVMALYRGVFR
TENRWTMLVDGTSRAGIEAILVSAIRPGDKVLVPVFGRFGHLLCEIARRCRAEVHTIEVP
WGEVFTPDQVEDAVKRIRPRLLLTVQGDTSTTMLQPLAELGEICRRYDALFYTDATASLG
GNPLETDVWGLDAVSAGMQKCLGGPSGTSPITLSARMEEAIRRRKCVEEGIRTDAHRDGD
EEMIYSNYFDLGMVMDYWGPERLNHHTEATTALFGARECARLILQEGLDYGIARHKLHGD
ALVKGIQAMGLETFGDLKHKMNNVLGVVIPQGINGDQARKLMLEDFGIEIGTSFGPLHGK
VWRIGTMGYNARKDCVMTTLSALESVLNYLKFPTTQGAAMQAAWDHYRSERAQ
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