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Comparing WP_011317102.1 NCBI__GCF_000204075.1:WP_011317102.1 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)
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)
42% identity, 96% coverage: 17:431/431 of query aligns to 7:443/454 of O50131
- T92 (= T100) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (= D101) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G132) binding pyridoxal 5'-phosphate
- T125 (≠ A133) 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)
42% identity, 96% coverage: 17:431/431 of query aligns to 5:441/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I71), S121 (= S131), G122 (= G132), T123 (≠ A133), F149 (= F159), H150 (= H160), R152 (= R162), E234 (= E226), D262 (= D254), V264 (= V256), Q265 (= Q257), K291 (= K283), N318 (≠ T310), T319 (= T311), R417 (= R407)
7vntA Structure of aminotransferase-substrate complex (see paper)
42% identity, 96% coverage: 17:431/431 of query aligns to 5:441/452 of 7vntA
- binding L-ornithine: F149 (= F159), R152 (= R162), E234 (= E226), K291 (= K283)
- binding pyridoxal-5'-phosphate: G122 (= G132), T123 (≠ A133), F149 (= F159), H150 (= H160), E229 (= E221), D262 (= D254), V264 (= V256), Q265 (= Q257), K291 (= K283)
7vnoA Structure of aminotransferase (see paper)
42% identity, 96% coverage: 17:431/431 of query aligns to 5:441/452 of 7vnoA
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)
38% identity, 98% coverage: 10:431/431 of query aligns to 17:459/474 of O58478
- D251 (≠ E226) mutation to A: Loss of activity.
- K308 (= K283) mutation to A: Loss of activity.
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
41% identity, 94% coverage: 25:431/431 of query aligns to 3:410/412 of 2eo5A
- active site: T18 (= T41), F139 (= F159), E219 (= E221), D252 (= D254), Q255 (= Q257), K281 (= K283), T303 (= T311), R386 (= R407)
- binding pyridoxal-5'-phosphate: G113 (= G132), T114 (≠ A133), F139 (= F159), H140 (= H160), E219 (= E221), D252 (= D254), V254 (= V256), Q255 (= Q257), K281 (= K283)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
41% identity, 91% coverage: 39:430/431 of query aligns to 38:425/429 of P73133
- Y39 (= Y40) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (= S131) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G132) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (= A133) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R162) 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 (= R407) 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.
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
43% identity, 90% coverage: 45:430/431 of query aligns to 18:389/390 of 8ht4B
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
38% identity, 94% coverage: 26:430/431 of query aligns to 4:420/425 of 1sffA
- active site: V18 (≠ Y40), Y137 (≠ F159), E205 (= E221), D238 (= D254), Q241 (= Q257), K267 (= K283), T296 (= T311), R397 (= R407)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ T100), G110 (= G132), S111 (≠ A133), Y137 (≠ F159), H138 (= H160), R140 (= R162), E205 (= E221), D238 (= D254), V240 (= V256), Q241 (= Q257), K267 (= K283), T296 (= T311)
- binding sulfate ion: N152 (≠ T174), Y393 (vs. gap)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
38% identity, 94% coverage: 26:430/431 of query aligns to 4:420/425 of 1sf2A
- active site: V18 (≠ Y40), Y137 (≠ F159), E205 (= E221), D238 (= D254), Q241 (= Q257), K267 (= K283), T296 (= T311), R397 (= R407)
- binding pyridoxal-5'-phosphate: G110 (= G132), S111 (≠ A133), Y137 (≠ F159), H138 (= H160), E205 (= E221), D238 (= D254), V240 (= V256), Q241 (= Q257), K267 (= K283)
- binding sulfate ion: N152 (≠ T174), 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)
38% identity, 94% coverage: 26:430/431 of query aligns to 5:421/426 of P22256
- I50 (= I71) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 132:133) 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)
38% identity, 94% coverage: 26:430/431 of query aligns to 4:420/425 of 1szkA
- active site: V18 (≠ Y40), Y137 (≠ F159), E205 (= E221), D238 (= D254), Q241 (= Q257), K267 (= K283), T296 (= T311), R397 (= R407)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G132), S111 (≠ A133), Y137 (≠ F159), H138 (= H160), E205 (= E221), D238 (= D254), V240 (= V256), Q241 (= Q257), K267 (= 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)
41% identity, 88% coverage: 52:430/431 of query aligns to 30:419/421 of P50457
- K267 (= K283) mutation to A: No GABA-AT activity.
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
38% identity, 91% coverage: 39:431/431 of query aligns to 6:383/385 of Q9X2A5
- GT 94:95 (≠ GA 132:133) binding pyridoxal 5'-phosphate
- T268 (= T311) binding pyridoxal 5'-phosphate
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
38% identity, 91% coverage: 39:431/431 of query aligns to 14:391/393 of 2ordA
- active site: F134 (= F159), E186 (= E221), D219 (= D254), Q222 (= Q257), K248 (= K283), T276 (= T311), R367 (= R407)
- binding pyridoxal-5'-phosphate: G102 (= G132), T103 (≠ A133), F134 (= F159), H135 (= H160), E186 (= E221), D219 (= D254), V221 (= V256), Q222 (= Q257), K248 (= K283)
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
34% identity, 94% coverage: 25:428/431 of query aligns to 6:427/439 of 5wyaA
- active site: A20 (≠ S39), Y140 (≠ F159), E215 (= E221), D248 (= D254), N251 (≠ Q257), K278 (= K283), T307 (= T311), R406 (= R407)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I71), Y82 (≠ D101), S112 (= S131), G113 (= G132), S114 (≠ A133), Y140 (≠ F159), H141 (= H160), E215 (= E221), D248 (= D254), V250 (= V256), N251 (≠ Q257), K278 (= K283), F306 (≠ T310), T307 (= T311), R406 (= R407)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
34% identity, 94% coverage: 25:428/431 of query aligns to 8:429/446 of 5wyfA
- active site: A22 (≠ S39), Y142 (≠ F159), E217 (= E221), D250 (= D254), N253 (≠ Q257), K280 (= K283), T309 (= T311), R408 (= R407)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I71), Y84 (≠ D101), G115 (= G132), S116 (≠ A133), Y142 (≠ F159), H143 (= H160), D222 (≠ E226), D250 (= D254), V252 (= V256), N253 (≠ Q257), K280 (= K283), F308 (≠ T310), T309 (= T311), R408 (= R407)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
34% identity, 94% coverage: 25:428/431 of query aligns to 15:436/448 of 4ysnC
- active site: A29 (≠ S39), Y149 (≠ F159), E224 (= E221), D257 (= D254), N260 (≠ Q257), K287 (= K283), T316 (= T311), R415 (= R407)
- binding pyridoxal-5'-phosphate: S121 (= S131), G122 (= G132), S123 (≠ A133), Y149 (≠ F159), H150 (= H160), E224 (= E221), D257 (= D254), V259 (= V256), K287 (= K283), F315 (≠ T310), T316 (= T311)
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
38% identity, 97% coverage: 15:430/431 of query aligns to 7:435/439 of 3q8nC
- active site: V32 (≠ Y40), Y151 (≠ F159), E221 (= E221), D254 (= D254), Q257 (= Q257), K283 (= K283), T312 (= T311), R412 (= R407)
- binding 4-oxobutanoic acid: G124 (= G132), A125 (= A133), V256 (= V256), K283 (= K283)
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
38% identity, 91% coverage: 39:430/431 of query aligns to 6:375/375 of 2eh6A
- active site: F127 (= F159), E179 (= E221), D212 (= D254), Q215 (= Q257), K241 (= K283), T270 (= T311), R352 (= R407)
- binding pyridoxal-5'-phosphate: G95 (= G132), T96 (≠ A133), F127 (= F159), H128 (= H160), E179 (= E221), D212 (= D254), V214 (= V256), K241 (= K283)
Query Sequence
>WP_011317102.1 NCBI__GCF_000204075.1:WP_011317102.1
MLSIPINQHLPHTPHLVTSLPGPRAKAIVERDRAVTSPSYTRDYPLVVNRGEGCMVEDVD
GNVFLDMTAGIAVTATGHAHPEVVRAIQEQSARLIHMSGTDFYYEPMVELAENLASQAPF
VHDTKVFFTNSGAESNEGAIKLARYYTKRSLIIAFLGAFHGRTYGAMSLTGSKTVQRANF
GPLVPGVTHIPYGTHASLDYLENNLLTTIIPAHEVAAIVVEPIQGEGGYIVPEDGFLQRI
RNICDRYGILMVVDEVQSGMGRTGRLFAIEHWNVTPDIITTAKGIASGMPLGAILARAEL
MTWPPGSHATTFGGNPVACAAGIVTLKLLESGLMDNATQMGELLQTGLTQLHQQFPRMSL
PRGKGLMVAVDLLDEDGNFDSKLRDRIIQEAFYHGLLLLGCGKAAIRFCPPLVINREQIQ
TTLDILAEILR
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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