SitesBLAST
Comparing WP_013258178.1 NCBI__GCF_000143965.1:WP_013258178.1 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)
6rl5G The first crystal structure of the daba aminotransferase ectb in the ectoine biosynthesis pathway of the model organism chromohalobacter salexigens dsm 3034 (see paper)
61% identity, 97% coverage: 2:411/422 of query aligns to 3:417/422 of 6rl5G
- active site: S16 (≠ C15), F137 (= F136), D237 (= D235), K266 (= K264)
- binding pyridoxal-5'-phosphate: G110 (= G109), T111 (= T110), F137 (= F136), H138 (= H137), D237 (= D235), I239 (= I237), Q240 (= Q238), K266 (= K264), G294 (= G292), T295 (= T293)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
31% identity, 94% coverage: 11:407/422 of query aligns to 5:374/376 of O66442
- GT 96:97 (= GT 109:110) binding pyridoxal 5'-phosphate
- K242 (= K264) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T293) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
31% identity, 94% coverage: 11:407/422 of query aligns to 4:373/375 of 2eh6A
- active site: F127 (= F136), E179 (= E202), D212 (= D235), Q215 (= Q238), K241 (= K264), T270 (= T293), R352 (≠ K386)
- binding pyridoxal-5'-phosphate: G95 (= G109), T96 (= T110), F127 (= F136), H128 (= H137), E179 (= E202), D212 (= D235), V214 (≠ I237), K241 (= K264)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
34% identity, 97% coverage: 2:410/422 of query aligns to 1:390/390 of 8ht4B
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)
32% identity, 96% coverage: 6:411/422 of query aligns to 11:423/426 of P22256
- I50 (≠ A45) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GT 109:110) binding pyridoxal 5'-phosphate
- E211 (= E207) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I237) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q238) binding pyridoxal 5'-phosphate
- K268 (= K264) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T293) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
32% identity, 96% coverage: 6:411/422 of query aligns to 10:422/425 of 1sffA
- active site: V18 (≠ Y14), Y137 (≠ F136), E205 (= E202), D238 (= D235), Q241 (= Q238), K267 (= K264), T296 (= T293), R397 (≠ K386)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ A77), G110 (= G109), S111 (≠ T110), Y137 (≠ F136), H138 (= H137), R140 (≠ V139), E205 (= E202), D238 (= D235), V240 (≠ I237), Q241 (= Q238), K267 (= K264), T296 (= T293)
- binding sulfate ion: N152 (≠ Y151), Y393 (≠ G382)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
32% identity, 96% coverage: 6:411/422 of query aligns to 10:422/425 of 1sf2A
- active site: V18 (≠ Y14), Y137 (≠ F136), E205 (= E202), D238 (= D235), Q241 (= Q238), K267 (= K264), T296 (= T293), R397 (≠ K386)
- binding pyridoxal-5'-phosphate: G110 (= G109), S111 (≠ T110), Y137 (≠ F136), H138 (= H137), E205 (= E202), D238 (= D235), V240 (≠ I237), Q241 (= Q238), K267 (= K264)
- binding sulfate ion: N152 (≠ Y151), Y393 (≠ G382)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
30% identity, 95% coverage: 11:410/422 of query aligns to 36:426/429 of P73133
- Y39 (= Y14) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (≠ T108) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G109) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (≠ T110) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (≠ V139) 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 (= E207) 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 (= D235) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q238) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K264) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T293) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (≠ K386) 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.
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
32% identity, 96% coverage: 6:411/422 of query aligns to 10:422/425 of 1szkA
- active site: V18 (≠ Y14), Y137 (≠ F136), E205 (= E202), D238 (= D235), Q241 (= Q238), K267 (= K264), T296 (= T293), R397 (≠ K386)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G109), S111 (≠ T110), Y137 (≠ F136), H138 (= H137), E205 (= E202), D238 (= D235), V240 (≠ I237), Q241 (= Q238), K267 (= K264)
7vo1A Structure of aminotransferase-substrate complex (see paper)
31% identity, 92% coverage: 22:409/422 of query aligns to 38:440/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ A45), S121 (≠ T108), G122 (= G109), T123 (= T110), F149 (= F136), H150 (= H137), R152 (≠ V139), E234 (= E207), D262 (= D235), V264 (≠ I237), Q265 (= Q238), K291 (= K264), N318 (≠ G292), T319 (= T293), R417 (≠ K386)
7vntA Structure of aminotransferase-substrate complex (see paper)
31% identity, 92% coverage: 22:409/422 of query aligns to 38:440/452 of 7vntA
- binding L-ornithine: F149 (= F136), R152 (≠ V139), E234 (= E207), K291 (= K264)
- binding pyridoxal-5'-phosphate: G122 (= G109), T123 (= T110), F149 (= F136), H150 (= H137), E229 (= E202), D262 (= D235), V264 (≠ I237), Q265 (= Q238), K291 (= K264)
7vnoA Structure of aminotransferase (see paper)
31% identity, 92% coverage: 22:409/422 of query aligns to 38:440/452 of 7vnoA
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)
31% identity, 92% coverage: 22:409/422 of query aligns to 40:442/454 of O50131
- T92 (≠ K82) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (= D83) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G109) binding pyridoxal 5'-phosphate
- T125 (= T110) binding pyridoxal 5'-phosphate
- Q267 (= Q238) binding pyridoxal 5'-phosphate
- K293 (= K264) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T293) binding pyridoxal 5'-phosphate
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)
34% identity, 92% coverage: 25:411/422 of query aligns to 29:421/421 of P50457
- K267 (= K264) mutation to A: No GABA-AT activity.
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
30% identity, 97% coverage: 2:409/422 of query aligns to 5:409/412 of 2eo5A
- active site: T18 (≠ C15), F139 (= F136), E219 (= E202), D252 (= D235), Q255 (= Q238), K281 (= K264), T303 (= T293), R386 (≠ K386)
- binding pyridoxal-5'-phosphate: G113 (= G109), T114 (= T110), F139 (= F136), H140 (= H137), E219 (= E202), D252 (= D235), V254 (≠ I237), Q255 (= Q238), K281 (= K264)
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 90% coverage: 24:403/422 of query aligns to 25:380/387 of 1wkhA
- active site: F132 (= F136), E184 (= E202), D217 (= D235), Q220 (= Q238), K246 (= K264), T275 (= T293), R363 (≠ K386)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ A45), S104 (≠ T108), G105 (= G109), T106 (= T110), F132 (= F136), S133 (≠ H137), E184 (= E202), E189 (= E207), D217 (= D235), I219 (= I237), K246 (= K264), R363 (≠ K386)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 90% coverage: 24:403/422 of query aligns to 25:380/387 of 1wkgA
- active site: F132 (= F136), E184 (= E202), D217 (= D235), Q220 (= Q238), K246 (= K264), T275 (= T293), R363 (≠ K386)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ A45), G105 (= G109), T106 (= T110), F132 (= F136), S133 (≠ H137), R135 (≠ V139), E184 (= E202), D217 (= D235), I219 (= I237), Q220 (= Q238), K246 (= K264), G273 (≠ N291), T274 (≠ G292), T275 (= T293)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 90% coverage: 24:403/422 of query aligns to 25:380/387 of 1vefA
- active site: F132 (= F136), D217 (= D235), K246 (= K264), T275 (= T293), R363 (≠ K386)
- binding pyridoxal-5'-phosphate: G105 (= G109), T106 (= T110), F132 (= F136), S133 (≠ H137), E184 (= E202), D217 (= D235), I219 (= I237), K246 (= K264)
Sites not aligning to the query:
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
29% identity, 94% coverage: 11:407/422 of query aligns to 4:380/385 of Q9X2A5
- GT 94:95 (= GT 109:110) binding pyridoxal 5'-phosphate
- T268 (= T293) binding pyridoxal 5'-phosphate
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
34% identity, 90% coverage: 24:403/422 of query aligns to 33:388/395 of Q5SHH5
- GT 113:114 (= GT 109:110) binding pyridoxal 5'-phosphate
- K254 (= K264) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T293) binding pyridoxal 5'-phosphate
Query Sequence
>WP_013258178.1 NCBI__GCF_000143965.1:WP_013258178.1
MKTIERLESNVRSYCRSFPVKFDRAQGAVLSDHQGHAYLDFLAGAGTLNYGHNHPVLKKA
LGDYLAADRIVHGLDMATVAKKDFLDTFERLILKPRGLDYKVQFTGPTGTNAVEAALKIA
RNHTGRHNVVAFTNAFHGVTSGSLACTANSYYRQAGGMPPQGVNFAPYDGYLGPDVDTVD
VLEKMILDGSSGLDLPAAVIVETVQGEGGLNVAGMGWLRKLAALCRRHDILLIVDDIQMG
CGRTGWFFSFEPAGVKPDIVTLSKSLSGYGLPMSLVLLKPRLDNWRPGEHNGTFRGNNLA
FVTARAALAHFWADDALALDVRRKGKILAERLRAVAEDDGGIESRGRGMAQGLDCKSGER
AGRICRRAFELGMVIETSGSEGQVVKCLCPLTIGDQELSRGLDILAQSVAETPLDDSDAI
AC
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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