SitesBLAST
Comparing GFF4018 FitnessBrowser__psRCH2:GFF4018 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)
57% identity, 98% coverage: 2:418/425 of query aligns to 3:421/422 of 6rl5G
- active site: S16 (≠ C15), F137 (= F137), D237 (= D236), K266 (= K265)
- binding pyridoxal-5'-phosphate: G110 (= G110), T111 (= T111), F137 (= F137), H138 (= H138), D237 (= D236), I239 (= I238), Q240 (= Q239), K266 (= K265), G294 (= G293), T295 (= T294)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
34% identity, 94% coverage: 11:408/425 of query aligns to 5:372/376 of O66442
- GT 96:97 (= GT 110:111) binding pyridoxal 5'-phosphate
- K242 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T294) binding pyridoxal 5'-phosphate
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
34% identity, 93% coverage: 13:408/425 of query aligns to 6:371/375 of 2eh6A
- active site: F127 (= F137), E179 (= E203), D212 (= D236), Q215 (= Q239), K241 (= K265), T270 (= T294), R352 (≠ K389)
- binding pyridoxal-5'-phosphate: G95 (= G110), T96 (= T111), F127 (= F137), H128 (= H138), E179 (= E203), D212 (= D236), V214 (≠ I238), K241 (= K265)
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
32% identity, 93% coverage: 19:412/425 of query aligns to 23:420/425 of 1sffA
- active site: Y137 (≠ F137), E205 (= E203), D238 (= D236), Q241 (= Q239), K267 (= K265), T296 (= T294), R397 (≠ K389)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ Y77), G110 (= G110), S111 (≠ T111), Y137 (≠ F137), H138 (= H138), R140 (≠ C140), E205 (= E203), D238 (= D236), V240 (≠ I238), Q241 (= Q239), K267 (= K265), T296 (= T294)
- binding sulfate ion: N152 (≠ H152), Y393 (≠ S385)
Sites not aligning to the query:
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
32% identity, 93% coverage: 19:412/425 of query aligns to 23:420/425 of 1sf2A
- active site: Y137 (≠ F137), E205 (= E203), D238 (= D236), Q241 (= Q239), K267 (= K265), T296 (= T294), R397 (≠ K389)
- binding pyridoxal-5'-phosphate: G110 (= G110), S111 (≠ T111), Y137 (≠ F137), H138 (= H138), E205 (= E203), D238 (= D236), V240 (≠ I238), Q241 (= Q239), K267 (= K265)
- binding sulfate ion: N152 (≠ H152), Y393 (≠ S385)
Sites not aligning to the query:
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, 93% coverage: 19:412/425 of query aligns to 24:421/426 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 110:111) binding pyridoxal 5'-phosphate
- E211 (= E208) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I238) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q239) binding pyridoxal 5'-phosphate
- K268 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T294) binding pyridoxal 5'-phosphate
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
32% identity, 93% coverage: 19:412/425 of query aligns to 23:420/425 of 1szkA
- active site: Y137 (≠ F137), E205 (= E203), D238 (= D236), Q241 (= Q239), K267 (= K265), T296 (= T294), R397 (≠ K389)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G110), S111 (≠ T111), Y137 (≠ F137), H138 (= H138), E205 (= E203), D238 (= D236), V240 (≠ I238), Q241 (= Q239), K267 (= K265)
Sites not aligning to the query:
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
28% identity, 98% coverage: 1:416/425 of query aligns to 26:429/429 of P73133
- Y39 (= Y14) mutation to F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
- S125 (≠ T109) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G110) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (≠ T111) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (≠ C140) 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 (= E208) 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 (= D236) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q239) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K265) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T294) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (≠ K389) 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.
4ppmA Crystal structure of pige: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (map) from serratia sp. Fs14 (see paper)
32% identity, 94% coverage: 21:418/425 of query aligns to 47:456/464 of 4ppmA
- active site: Y159 (≠ F137), E212 (= E203), D245 (= D236), Q248 (= Q239), K274 (= K265), T309 (= T294), R431 (≠ K389)
- binding magnesium ion: A351 (≠ I337), Y354 (≠ H340), V357 (≠ S344)
- binding pyridoxal-5'-phosphate: G132 (= G110), T133 (= T111), Y159 (≠ F137), H160 (= H138), D245 (= D236), V247 (≠ I238), K274 (= K265)
Sites not aligning to the query:
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)
32% identity, 97% coverage: 1:413/425 of query aligns to 1:420/421 of P50457
- K267 (= K265) mutation to A: No GABA-AT activity.
Q9M8M7 Acetylornithine aminotransferase, chloroplastic/mitochondrial; ACOAT; Acetylornithine transaminase; AOTA; Protein HOPW1-1-INTERACTING 1; EC 2.6.1.11 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 95% coverage: 11:415/425 of query aligns to 70:456/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
A0A0J9X1Q5 Aminotransferase PigE; EC 2.6.1.- from Serratia sp. (strain FS14) (see paper)
34% identity, 79% coverage: 21:356/425 of query aligns to 418:740/853 of A0A0J9X1Q5
- GT 503:504 (= GT 110:111) binding pyridoxal 5'-phosphate
- K645 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T680 (= T294) 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)
29% identity, 98% coverage: 8:424/425 of query aligns to 39:470/474 of O58478
- D251 (≠ E208) mutation to A: Loss of activity.
- K308 (= K265) mutation to A: Loss of activity.
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
30% identity, 93% coverage: 19:413/425 of query aligns to 18:390/390 of 8ht4B
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
29% identity, 93% coverage: 20:413/425 of query aligns to 21:387/387 of 1wkhA
- active site: F132 (= F137), E184 (= E203), D217 (= D236), Q220 (= Q239), K246 (= K265), T275 (= T294), R363 (≠ K389)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ A45), S104 (≠ T109), G105 (= G110), T106 (= T111), F132 (= F137), S133 (≠ H138), E184 (= E203), E189 (= E208), D217 (= D236), I219 (= I238), K246 (= K265), R363 (≠ K389)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
29% identity, 93% coverage: 20:413/425 of query aligns to 21:387/387 of 1wkgA
- active site: F132 (= F137), E184 (= E203), D217 (= D236), Q220 (= Q239), K246 (= K265), T275 (= T294), R363 (≠ K389)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ A45), G105 (= G110), T106 (= T111), F132 (= F137), S133 (≠ H138), R135 (≠ C140), E184 (= E203), D217 (= D236), I219 (= I238), Q220 (= Q239), K246 (= K265), G273 (≠ N292), T274 (≠ G293), T275 (= T294)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
29% identity, 93% coverage: 20:413/425 of query aligns to 21:387/387 of 1vefA
- active site: F132 (= F137), D217 (= D236), K246 (= K265), T275 (= T294), R363 (≠ K389)
- binding pyridoxal-5'-phosphate: G105 (= G110), T106 (= T111), F132 (= F137), S133 (≠ H138), E184 (= E203), D217 (= D236), I219 (= I238), K246 (= K265)
Sites not aligning to the query:
4uoxA Crystal structure of ygjg in complex with pyridoxal-5'-phosphate and putrescine (see paper)
29% identity, 91% coverage: 30:415/425 of query aligns to 70:446/453 of 4uoxA
- active site: F174 (= F137), E232 (= E203), D265 (= D236), Q268 (= Q239), K294 (= K265), T326 (= T294), R420 (≠ K389)
- binding pyridoxal-5'-phosphate: S143 (≠ T109), G144 (= G110), T145 (= T111), F174 (= F137), H175 (= H138), G176 (= G139), D265 (= D236), V267 (≠ I238), Q268 (= Q239), T325 (≠ G293), T326 (= T294)
- binding 1,4-diaminobutane: E237 (= E208), K294 (= K265)
Sites not aligning to the query:
P42588 Putrescine aminotransferase; PAT; PATase; Cadaverine transaminase; Diamine transaminase; Putrescine transaminase; Putrescine--2-oxoglutaric acid transaminase; Putrescine:2-OG aminotransferase; EC 2.6.1.82; EC 2.6.1.29 from Escherichia coli (strain K12) (see paper)
29% identity, 91% coverage: 30:415/425 of query aligns to 76:452/459 of P42588
- GT 150:151 (= GT 110:111) binding in other chain
- Q274 (= Q239) binding in other chain
- K300 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T332 (= T294) binding pyridoxal 5'-phosphate
8r2pD Yzwideal x16 a scaffold for cryo-em of small proteins of interest crystallizing in space group 19 (p 21 21 21)
29% identity, 91% coverage: 30:415/425 of query aligns to 69:445/507 of 8r2pD
Query Sequence
>GFF4018 FitnessBrowser__psRCH2:GFF4018
MKTFELNESKVRSYCRSFPVVFNQAQGAELVTQDGKRYIDFLAGAGTLNYGHNHPVLKQA
LLEYIENDGITHGLDMYTAAKERFLETFNRLILEPRGMGDYRMQFTGPTGTNAVEAAMKL
ARKVTGRNNIISFTNGFHGCSIGALAATGNQHHRGGSGISLTDVSRMPYANYFGDKTNTI
GMMDKLLSDPSSGIDKPAAVIVEVVQGEGGLNTASTEWMRKLEKLCRKHEMLLIVDDIQA
GCGRTGTFFSFEEMGIQPDIVTLSKSLSGYGLPFAMVLLRQELDQWKPGEHNGTFRGNNH
AFVTAAAAVEHFWQNDAFANSVKAKGKRIADGMQRIIRRHGPDSLYLKGRGMMIGISCPD
GEIAAAVCRHAFENGLVIETSGAHSEVVKCLCPLIISEEQIDKALAILDKAFAAVMSEQT
ENQAS
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