SitesBLAST
Comparing WP_007694040.1 NCBI__GCF_000336675.1:WP_007694040.1 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)
35% identity, 97% coverage: 8:448/454 of query aligns to 1:421/422 of 6rl5G
- active site: S16 (≠ P26), F137 (≠ Y147), D237 (= D255), K266 (= K284)
- binding pyridoxal-5'-phosphate: G110 (= G120), T111 (= T121), F137 (≠ Y147), H138 (= H148), D237 (= D255), I239 (= I257), Q240 (= Q258), K266 (= K284), G294 (= G311), T295 (= T312)
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)
36% identity, 93% coverage: 26:446/454 of query aligns to 33:446/454 of O50131
- T92 (≠ L85) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (= D86) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G120) binding pyridoxal 5'-phosphate
- T125 (= T121) binding pyridoxal 5'-phosphate
- Q267 (= Q258) binding pyridoxal 5'-phosphate
- K293 (= K284) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T312) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
36% identity, 93% coverage: 26:446/454 of query aligns to 31:444/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ A56), S121 (≠ A119), G122 (= G120), T123 (= T121), F149 (≠ Y147), H150 (= H148), R152 (≠ M150), E234 (= E227), D262 (= D255), V264 (≠ I257), Q265 (= Q258), K291 (= K284), N318 (≠ G311), T319 (= T312), R417 (= R419)
7vntA Structure of aminotransferase-substrate complex (see paper)
36% identity, 93% coverage: 26:446/454 of query aligns to 31:444/452 of 7vntA
- binding L-ornithine: F149 (≠ Y147), R152 (≠ M150), E234 (= E227), K291 (= K284)
- binding pyridoxal-5'-phosphate: G122 (= G120), T123 (= T121), F149 (≠ Y147), H150 (= H148), E229 (= E222), D262 (= D255), V264 (≠ I257), Q265 (= Q258), K291 (= K284)
7vnoA Structure of aminotransferase (see paper)
36% identity, 93% coverage: 26:446/454 of query aligns to 31:444/452 of 7vnoA
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 95% coverage: 15:447/454 of query aligns to 6:387/387 of 1wkhA
- active site: S13 (≠ A22), F132 (≠ Y147), E184 (= E222), D217 (= D255), Q220 (= Q258), K246 (= K284), T275 (= T312), R363 (= R419)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ A56), S104 (≠ A119), G105 (= G120), T106 (= T121), F132 (≠ Y147), S133 (≠ H148), E184 (= E222), E189 (= E227), D217 (= D255), I219 (= I257), K246 (= K284), R363 (= R419)
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 95% coverage: 15:447/454 of query aligns to 6:387/387 of 1wkgA
- active site: S13 (≠ A22), F132 (≠ Y147), E184 (= E222), D217 (= D255), Q220 (= Q258), K246 (= K284), T275 (= T312), R363 (= R419)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (= Y25), Y46 (≠ A56), G105 (= G120), T106 (= T121), F132 (≠ Y147), S133 (≠ H148), R135 (≠ M150), E184 (= E222), D217 (= D255), I219 (= I257), Q220 (= Q258), K246 (= K284), G273 (≠ A310), T274 (≠ G311), T275 (= T312)
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
34% identity, 95% coverage: 15:447/454 of query aligns to 6:387/387 of 1vefA
- active site: S13 (≠ A22), F132 (≠ Y147), D217 (= D255), K246 (= K284), T275 (= T312), R363 (= R419)
- binding pyridoxal-5'-phosphate: G105 (= G120), T106 (= T121), F132 (≠ Y147), S133 (≠ H148), E184 (= E222), D217 (= D255), I219 (= I257), K246 (= K284)
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
34% identity, 95% coverage: 15:447/454 of query aligns to 14:395/395 of Q5SHH5
- GT 113:114 (= GT 120:121) binding pyridoxal 5'-phosphate
- K254 (= K284) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T312) binding pyridoxal 5'-phosphate
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)
32% identity, 92% coverage: 27:442/454 of query aligns to 50:458/474 of O58478
- D251 (≠ E227) mutation to A: Loss of activity.
- K308 (= K284) mutation to A: Loss of activity.
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
31% identity, 93% coverage: 26:445/454 of query aligns to 21:412/412 of 2eo5A
- active site: F139 (≠ Y147), E219 (= E222), D252 (= D255), Q255 (= Q258), K281 (= K284), T303 (= T312), R386 (= R419)
- binding pyridoxal-5'-phosphate: G113 (= G120), T114 (= T121), F139 (≠ Y147), H140 (= H148), E219 (= E222), D252 (= D255), V254 (≠ I257), Q255 (= Q258), K281 (= K284)
Sites not aligning to the query:
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
32% identity, 93% coverage: 31:453/454 of query aligns to 27:438/439 of 5wyaA
- active site: Y140 (= Y147), E215 (= E222), D248 (= D255), N251 (≠ Q258), K278 (= K284), T307 (= T312), R406 (= R419)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (= A56), Y82 (≠ K92), S112 (≠ A119), G113 (= G120), S114 (≠ T121), Y140 (= Y147), H141 (= H148), E215 (= E222), D248 (= D255), V250 (≠ I257), N251 (≠ Q258), K278 (= K284), F306 (≠ G311), T307 (= T312), R406 (= R419)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
32% identity, 93% coverage: 31:453/454 of query aligns to 29:440/446 of 5wyfA
- active site: Y142 (= Y147), E217 (= E222), D250 (= D255), N253 (≠ Q258), K280 (= K284), T309 (= T312), R408 (= R419)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (= A56), Y84 (≠ K92), G115 (= G120), S116 (≠ T121), Y142 (= Y147), H143 (= H148), D222 (≠ E227), D250 (= D255), V252 (≠ I257), N253 (≠ Q258), K280 (= K284), F308 (≠ G311), T309 (= T312), R408 (= R419)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
32% identity, 93% coverage: 31:453/454 of query aligns to 36:447/448 of 4ysnC
- active site: Y149 (= Y147), E224 (= E222), D257 (= D255), N260 (≠ Q258), K287 (= K284), T316 (= T312), R415 (= R419)
- binding pyridoxal-5'-phosphate: S121 (≠ A119), G122 (= G120), S123 (≠ T121), Y149 (= Y147), H150 (= H148), E224 (= E222), D257 (= D255), V259 (≠ I257), K287 (= K284), F315 (≠ G311), T316 (= T312)
Sites not aligning to the query:
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
33% identity, 93% coverage: 20:443/454 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)
31% identity, 96% coverage: 8:441/454 of query aligns to 4:424/426 of P22256
- I50 (≠ A56) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GT 120:121) binding pyridoxal 5'-phosphate
- E211 (= E227) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I257) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q258) binding pyridoxal 5'-phosphate
- K268 (= K284) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T312) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
31% identity, 96% coverage: 8:441/454 of query aligns to 3:423/425 of 1sffA
- active site: V18 (vs. gap), Y137 (= Y147), E205 (= E222), D238 (= D255), Q241 (= Q258), K267 (= K284), T296 (= T312), R397 (= R419)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ L85), G110 (= G120), S111 (≠ T121), Y137 (= Y147), H138 (= H148), R140 (≠ M150), E205 (= E222), D238 (= D255), V240 (≠ I257), Q241 (= Q258), K267 (= K284), T296 (= T312)
- binding sulfate ion: N152 (≠ D162), Y393 (≠ D415)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
31% identity, 96% coverage: 8:441/454 of query aligns to 3:423/425 of 1sf2A
- active site: V18 (vs. gap), Y137 (= Y147), E205 (= E222), D238 (= D255), Q241 (= Q258), K267 (= K284), T296 (= T312), R397 (= R419)
- binding pyridoxal-5'-phosphate: G110 (= G120), S111 (≠ T121), Y137 (= Y147), H138 (= H148), E205 (= E222), D238 (= D255), V240 (≠ I257), Q241 (= Q258), K267 (= K284)
- binding sulfate ion: N152 (≠ D162), Y393 (≠ D415)
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)
33% identity, 91% coverage: 31:443/454 of query aligns to 24:420/421 of P50457
- K267 (= K284) mutation to A: No GABA-AT activity.
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
33% identity, 96% coverage: 12:448/454 of query aligns to 1:388/390 of A0QYS9
- K304 (≠ R344) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Query Sequence
>WP_007694040.1 NCBI__GCF_000336675.1:WP_007694040.1
MSYLDGGNSEVLTRQSERESNARTYPRHLPFAIREATGVTVTDMDGNEYYDCLAGAGTLA
LGHNHPRVVEAMERVIDEDRPIHTLDISTPTKERFVDSLFESLPDEFTDRAKIQFCSPAG
TDAVEAALKLVKTATGNRSVLGFQGAYHGMTSGALGLMGDVDVKGTLPASTGEVHHLPYP
SNYRPPFGVGGEEGHRIASRYVRNLLADSKSGITDPAGMILEPIQGEGGSVPAPDEWLRE
MRRITREHDIPLILDEIQTGLGRTGETYAFEHADIVPDVVTLSKAIGGGLPLAVVVYDES
LDVWEPGAHAGTFRGNQLAMAAGEATIDHVVENDLAEHAADVGRRLREAFEATAERFEAV
GDVRGRGLMLGVEFVDHGAEWQGPGPHAPDGDFAEAVQAACFERGLVVERGGRGDATARF
LPPLIVTRAQVDEIATIFEEAVAAVAAERWEVTA
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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