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Comparing WP_053768287.1 NCBI__GCF_001280255.1:WP_053768287.1 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)
O58478 Alanine/serine racemase; ASR; Ala/Ser racemase; EC 5.1.1.-; EC 5.1.1.1 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
45% identity, 99% coverage: 3:431/432 of query aligns to 21:460/474 of O58478
- D251 (≠ E226) mutation to A: Loss of activity.
- K308 (= K283) mutation to A: Loss of activity.
O50131 Ornithine aminotransferase; Orn-AT; Ornithine delta-aminotransferase; EC 2.6.1.13 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
44% identity, 100% coverage: 1:430/432 of query aligns to 3:443/454 of O50131
- T92 (≠ S89) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (= D90) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G119) binding pyridoxal 5'-phosphate
- T125 (= T120) binding pyridoxal 5'-phosphate
- Q267 (= Q257) binding pyridoxal 5'-phosphate
- K293 (= K283) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T311) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
44% identity, 100% coverage: 1:430/432 of query aligns to 1:441/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I60), S121 (= S118), G122 (= G119), T123 (= T120), F149 (= F146), H150 (= H147), R152 (= R149), E234 (= E226), D262 (= D254), V264 (= V256), Q265 (= Q257), K291 (= K283), N318 (≠ T310), T319 (= T311), R417 (= R406)
7vntA Structure of aminotransferase-substrate complex (see paper)
44% identity, 100% coverage: 1:430/432 of query aligns to 1:441/452 of 7vntA
- binding L-ornithine: F149 (= F146), R152 (= R149), E234 (= E226), K291 (= K283)
- binding pyridoxal-5'-phosphate: G122 (= G119), T123 (= T120), F149 (= F146), H150 (= H147), E229 (= E221), D262 (= D254), V264 (= V256), Q265 (= Q257), K291 (= K283)
7vnoA Structure of aminotransferase (see paper)
44% identity, 100% coverage: 1:430/432 of query aligns to 1:441/452 of 7vnoA
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
42% identity, 97% coverage: 14:430/432 of query aligns to 3:410/412 of 2eo5A
- active site: T18 (≠ Y29), F139 (= F146), E219 (= E221), D252 (= D254), Q255 (= Q257), K281 (= K283), T303 (= T311), R386 (= R406)
- binding pyridoxal-5'-phosphate: G113 (= G119), T114 (= T120), F139 (= F146), H140 (= H147), E219 (= E221), D252 (= D254), V254 (= V256), Q255 (= Q257), K281 (= K283)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
35% identity, 97% coverage: 13:432/432 of query aligns to 13:441/448 of 4ysnC
- active site: A29 (vs. gap), Y149 (≠ F146), E224 (= E221), D257 (= D254), N260 (≠ Q257), K287 (= K283), T316 (= T311), R415 (= R406)
- binding pyridoxal-5'-phosphate: S121 (= S118), G122 (= G119), S123 (≠ T120), Y149 (≠ F146), H150 (= H147), E224 (= E221), D257 (= D254), V259 (= V256), K287 (= K283), F315 (≠ T310), T316 (= T311)
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
35% identity, 97% coverage: 13:432/432 of query aligns to 4:432/439 of 5wyaA
- active site: A20 (vs. gap), Y140 (≠ F146), E215 (= E221), D248 (= D254), N251 (≠ Q257), K278 (= K283), T307 (= T311), R406 (= R406)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I60), Y82 (≠ D90), S112 (= S118), G113 (= G119), S114 (≠ T120), Y140 (≠ F146), H141 (= H147), E215 (= E221), D248 (= D254), V250 (= V256), N251 (≠ Q257), K278 (= K283), F306 (≠ T310), T307 (= T311), R406 (= R406)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
35% identity, 97% coverage: 13:432/432 of query aligns to 6:434/446 of 5wyfA
- active site: A22 (vs. gap), Y142 (≠ F146), E217 (= E221), D250 (= D254), N253 (≠ Q257), K280 (= K283), T309 (= T311), R408 (= R406)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I60), Y84 (≠ D90), G115 (= G119), S116 (≠ T120), Y142 (≠ F146), H143 (= H147), D222 (≠ E226), D250 (= D254), V252 (= V256), N253 (≠ Q257), K280 (= K283), F308 (≠ T310), T309 (= T311), R408 (= R406)
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
36% identity, 96% coverage: 15:429/432 of query aligns to 4:420/425 of 1sffA
- active site: V18 (≠ Y29), Y137 (≠ F146), E205 (= E221), D238 (= D254), Q241 (= Q257), K267 (= K283), T296 (= T311), R397 (= R406)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ S89), G110 (= G119), S111 (≠ T120), Y137 (≠ F146), H138 (= H147), R140 (= R149), E205 (= E221), D238 (= D254), V240 (= V256), Q241 (= Q257), K267 (= K283), T296 (= T311)
- binding sulfate ion: N152 (≠ S161), Y393 (vs. gap)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
36% identity, 96% coverage: 15:429/432 of query aligns to 4:420/425 of 1sf2A
- active site: V18 (≠ Y29), Y137 (≠ F146), E205 (= E221), D238 (= D254), Q241 (= Q257), K267 (= K283), T296 (= T311), R397 (= R406)
- binding pyridoxal-5'-phosphate: G110 (= G119), S111 (≠ T120), Y137 (≠ F146), H138 (= H147), E205 (= E221), D238 (= D254), V240 (= V256), Q241 (= Q257), K267 (= K283)
- binding sulfate ion: N152 (≠ S161), Y393 (vs. gap)
P22256 4-aminobutyrate aminotransferase GabT; 5-aminovalerate transaminase; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; L-AIBAT; EC 2.6.1.19; EC 2.6.1.48 from Escherichia coli (strain K12) (see 2 papers)
36% identity, 96% coverage: 15:429/432 of query aligns to 5:421/426 of P22256
- I50 (= I60) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GT 119:120) binding pyridoxal 5'-phosphate
- E211 (= E226) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V256) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q257) binding pyridoxal 5'-phosphate
- K268 (= K283) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T311) binding pyridoxal 5'-phosphate
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
36% identity, 96% coverage: 15:429/432 of query aligns to 4:420/425 of 1szkA
- active site: V18 (≠ Y29), Y137 (≠ F146), E205 (= E221), D238 (= D254), Q241 (= Q257), K267 (= K283), T296 (= T311), R397 (= R406)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G119), S111 (≠ T120), Y137 (≠ F146), H138 (= H147), E205 (= E221), D238 (= D254), V240 (= V256), Q241 (= Q257), K267 (= K283)
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
38% identity, 94% coverage: 25:432/432 of query aligns to 11:393/393 of 2ordA
- active site: F134 (= F146), E186 (= E221), D219 (= D254), Q222 (= Q257), K248 (= K283), T276 (= T311), R367 (= R406)
- binding pyridoxal-5'-phosphate: G102 (= G119), T103 (= T120), F134 (= F146), H135 (= H147), E186 (= E221), D219 (= D254), V221 (= V256), Q222 (= Q257), K248 (= K283)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
38% identity, 94% coverage: 25:432/432 of query aligns to 3:385/385 of Q9X2A5
- GT 94:95 (= GT 119:120) binding pyridoxal 5'-phosphate
- T268 (= T311) binding pyridoxal 5'-phosphate
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
38% identity, 97% coverage: 12:432/432 of query aligns to 22:428/429 of P73133
- Y39 (= Y29) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S118) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G119) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (≠ T120) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R149) mutation to A: 4100-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 9.5% of N-acetylornithine aminotransferase wild-type activity.
- E223 (= E226) mutation to A: 65-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 50% of N-acetylornithine aminotransferase wild-type activity.; mutation to S: 73-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Shows 160% of N-acetylornithine aminotransferase wild-type activity.
- D251 (= D254) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q257) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K283) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T311) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R406) mutation to A: 2080-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 18% of N-acetylornithine aminotransferase wild-type activity.
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
38% identity, 94% coverage: 25:429/432 of query aligns to 3:375/375 of 2eh6A
- active site: F127 (= F146), E179 (= E221), D212 (= D254), Q215 (= Q257), K241 (= K283), T270 (= T311), R352 (= R406)
- binding pyridoxal-5'-phosphate: G95 (= G119), T96 (= T120), F127 (= F146), H128 (= H147), E179 (= E221), D212 (= D254), V214 (= V256), K241 (= K283)
P50457 4-aminobutyrate aminotransferase PuuE; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; EC 2.6.1.19 from Escherichia coli (strain K12) (see paper)
36% identity, 92% coverage: 35:431/432 of query aligns to 24:421/421 of P50457
- K267 (= K283) mutation to A: No GABA-AT activity.
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
38% identity, 94% coverage: 25:429/432 of query aligns to 4:376/376 of O66442
- GT 96:97 (= GT 119:120) binding pyridoxal 5'-phosphate
- K242 (= K283) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T311) binding pyridoxal 5'-phosphate
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
37% identity, 100% coverage: 2:431/432 of query aligns to 8:443/444 of 4atqF
- active site: V35 (≠ Y29), Y154 (≠ F146), E226 (= E221), D259 (= D254), Q262 (= Q257), K288 (= K283), T317 (= T311), R418 (= R406)
- binding gamma-amino-butanoic acid: M95 (≠ S89), Y154 (≠ F146), R157 (= R149), E231 (= E226), K288 (= K283), G316 (≠ T310)
- binding pyridoxal-5'-phosphate: G127 (= G119), A128 (≠ T120), Y154 (≠ F146), H155 (= H147), D259 (= D254), V261 (= V256)
Query Sequence
>WP_053768287.1 NCBI__GCF_001280255.1:WP_053768287.1
MKPEVKTPLPGPKAQELLARGEKVLSPSYVRPYPFVPARGQGVFLEDVDGNVFLDFMAGI
AVNTTGYAHPRGLAAVKAQAERFAHVCFSDFTHEPTLSLAERLVAKVGGGYRVFFGNSGT
EGIEAAIKLVRHHTGRPYLLAFTGAFHGRSLGALSLTASKSAYRKGFAPLLPGVVHVPFP
NPFRPPLGASPEEVGEAVLAHLEHLFATVLPPEEVAAFFLEPIQGEGGYVLPPAGFLPKL
KALLERHGILLVADEVQTGAGRTGRFLALEHEGVEADVYVLAKGLASGYPLSAVLFREEL
GSWRPGAHGTTFGGQAVAAAAAQATLDLLEGGLMENAREVGAFLLAGLREMQKRFPFLGD
VRGRGLMIGLDFGSPEEPRPDLRDKAQRLAFEKGLLTLAAGPSALRLAPPLVLSREEAAL
GLEILEEALKSL
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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