SitesBLAST
Comparing WP_085635109.1 NCBI__GCF_002115805.1:WP_085635109.1 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)
P96060 2-aminoethylphosphonate--pyruvate transaminase; 2-aminoethylphosphonate aminotransferase; AEP transaminase; AEPT; EC 2.6.1.37 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
47% identity, 90% coverage: 16:370/393 of query aligns to 8:363/367 of P96060
- D168 (= D176) mutation to A: Loss of enzymatic activity.
- K194 (= K202) mutation K->L,R: Loss of enzymatic activity.
- R340 (= R347) mutation R->A,K: Decreased affinity for all of the substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1m32A Crystal structure of 2-aminoethylphosphonate transaminase (see paper)
47% identity, 90% coverage: 16:370/393 of query aligns to 3:358/361 of 1m32A
1m32B Crystal structure of 2-aminoethylphosphonate transaminase (see paper)
47% identity, 90% coverage: 16:370/393 of query aligns to 4:359/362 of 1m32B
6pd2C Pntc-aept: fusion protein of phosphonate-specific cytidylyltransferase and 2-aminoethylphosphonate (aep) transaminase from treponema denticola in complex with cytidine monophosphate-aep (see paper)
32% identity, 92% coverage: 16:375/393 of query aligns to 252:614/616 of 6pd2C
Sites not aligning to the query:
- binding 5'-O-[(S)-{[(R)-(2-aminoethyl)(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]cytidine: 8, 9, 10, 11, 15, 25, 83, 84, 85, 88, 104, 105, 106, 136, 153, 196, 220, 222
- binding magnesium ion: 106, 136, 220, 220, 222, 222
Q73MU2 Bifunctional 2-aminoethylphosphonate cytidylyltransferase/aminotransferase; EC 2.7.7.107; EC 2.6.1.37 from Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104) (see paper)
32% identity, 92% coverage: 16:375/393 of query aligns to 252:614/616 of Q73MU2
- S313 (= S73) binding pyridoxal 5'-phosphate
- G314 (= G74) binding pyridoxal 5'-phosphate
- T315 (≠ S75) binding pyridoxal 5'-phosphate
- T390 (= T151) binding pyridoxal 5'-phosphate
- K441 (= K202) binding pyridoxal 5'-phosphate
- T490 (= T250) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 8 binding CMP-(2-aminoethyl)phosphonate
- 10 binding CMP-(2-aminoethyl)phosphonate
- 11 binding CMP-(2-aminoethyl)phosphonate
- 15 R→A: Strong decrease in cytidylyltransferase activity.
- 25 binding CMP-(2-aminoethyl)phosphonate; K→A: Almost loss of cytidylyltransferase activity.
- 83 binding CMP-(2-aminoethyl)phosphonate
- 88 binding CMP-(2-aminoethyl)phosphonate
- 104 binding CMP-(2-aminoethyl)phosphonate
- 105 binding CMP-(2-aminoethyl)phosphonate
- 106 binding Mg(2+)
- 136 binding CMP-(2-aminoethyl)phosphonate; binding Mg(2+)
- 153 binding CMP-(2-aminoethyl)phosphonate; K→A: Strong decrease in cytidylyltransferase activity.
- 196 binding CMP-(2-aminoethyl)phosphonate
- 220 binding Mg(2+); binding Mg(2+)
- 222 binding Mg(2+); binding Mg(2+)
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
26% identity, 91% coverage: 16:374/393 of query aligns to 19:376/381 of 2dr1A
2yrrA Hypothetical alanine aminotransferase (tth0173) from thermus thermophilus hb8
31% identity, 71% coverage: 16:295/393 of query aligns to 3:276/352 of 2yrrA
2yriA Crystal structure of alanine-pyruvate aminotransferase with 2- methylserine
31% identity, 71% coverage: 16:295/393 of query aligns to 3:276/352 of 2yriA
- binding (s,e)-3-hydroxy-2-((3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl)methyleneamino)-2-methylpropanoic acid: G7 (= G20), S60 (= S73), G61 (= G74), S62 (= S75), F85 (≠ Y100), T135 (= T151), D160 (= D176), V162 (≠ M178), K186 (= K202)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y229 (≠ W247), T232 (= T250)
Sites not aligning to the query:
2z9xA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxyl-l-alanine (see paper)
28% identity, 73% coverage: 68:352/393 of query aligns to 62:349/392 of 2z9xA
2z9wA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxal (see paper)
28% identity, 73% coverage: 68:352/393 of query aligns to 62:349/392 of 2z9wA
2z9vA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxamine (see paper)
28% identity, 73% coverage: 68:352/393 of query aligns to 62:349/392 of 2z9vA
Q988B8 Pyridoxamine--pyruvate transaminase; Pyridoxamine-pyruvate aminotransferase; EC 2.6.1.30 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) (see 2 papers)
28% identity, 73% coverage: 68:352/393 of query aligns to 63:350/393 of Q988B8
- E68 (≠ S73) binding pyridoxal 5'-phosphate; mutation E->A,G: Low but detectable pyridoxamine--pyruvate transaminase activity.
- Y95 (= Y100) binding pyridoxal 5'-phosphate
- T146 (= T151) binding pyridoxal 5'-phosphate
- K197 (= K202) modified: N6-(pyridoxal phosphate)lysine; mutation to L: Loss of function.
- C198 (= C203) mutation to A: No effect on enzyme activity.
- R336 (vs. gap) mutation to A: Strongly decreased affinity for pyruvate.
- R345 (= R347) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3zrrA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
25% identity, 86% coverage: 16:352/393 of query aligns to 1:338/379 of 3zrrA
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: V4 (≠ P19), F24 (≠ S38), G58 (≠ S73), G59 (= G74), T60 (≠ S75), F84 (≠ Y100), T134 (= T151), D159 (= D176), V161 (≠ M178), Y236 (≠ W247), T239 (= T250), R333 (= R347)
3zrqA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
25% identity, 86% coverage: 16:352/393 of query aligns to 4:341/382 of 3zrqA
3zrpA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
25% identity, 85% coverage: 17:352/393 of query aligns to 1:337/377 of 3zrpA
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
24% identity, 76% coverage: 16:314/393 of query aligns to 21:319/377 of 1vjoA
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)
22% identity, 88% coverage: 12:356/393 of query aligns to 8:356/401 of Q56YA5
- TGT 68:70 (≠ QGS 71:73) binding pyridoxal 5'-phosphate
- T148 (= T151) binding pyridoxal 5'-phosphate
- QK 200:201 (≠ NK 201:202) binding pyridoxal 5'-phosphate
- K201 (= K202) binding 3-hydroxypyruvate
- P251 (= P251) mutation to L: Abolishes aminotransferase activity.
- R347 (= R347) binding 3-hydroxypyruvate
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
22% identity, 88% coverage: 12:356/393 of query aligns to 7:355/400 of 6pk3B
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
22% identity, 88% coverage: 12:356/393 of query aligns to 6:354/399 of 6pk1A
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)
25% identity, 77% coverage: 70:370/393 of query aligns to 78:384/392 of P21549
- G82 (= G74) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ Y100) 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 (= A104) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ T142) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ V144) 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 (≠ C149) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T151) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G154) 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 (≠ V159) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ A163) 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 (≠ T166) 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 (≠ A180) 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 (≠ A195) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (= S198) 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 (vs. gap) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ S223) 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 (≠ V234) 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 (≠ T240) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ E267) to T: in dbSNP:rs140992177
- A280 (= A268) to V: in dbSNP:rs73106685
- V326 (≠ C313) to I: in dbSNP:rs115057148
- I340 (= I335) 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
- 36 R → C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- 41 G → E: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177168; G → 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; G → V: in HP1; reduced alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177168
- 47 G → 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
Query Sequence
>WP_085635109.1 NCBI__GCF_002115805.1:WP_085635109.1
MSATPLPAPELGEPYLLTPGPLTTAYSVKQAMLKDWGSWDDDFRAMTRALRSRLLALIGG
GASDYDCVPIQGSGSYCVEAMLGSFVPRDGKVLVLANGAYGLRAAQTLGYLERDYHLLDK
GDYLPPRGDEVAAILAADPAITHVLAIHCETSSGIQNPVEEIAEATKAAGRKLLIDSMSA
FGALPLDPVKLNCAAFVSSANKCIEGVPGFGFVIARKDEIEASKGNSHSLSLDVHAQWAT
MEKTGQWRFTPPTHVVAAFLKALDLHEAEGGVSARGARYTRNRDVVVQGMRDLGFETLLA
DRWLSPIIVTFFCPADPSFTFQGFYDAMKARGFIIYPGKLTVVNSFRIGVIGQMDEHVMR
RVVEAARDALTDMNVSSAAPPAAALEERKKLAA
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