SitesBLAST
Comparing BWI76_RS14020 BWI76_RS14020 aspartate aminotransferase family protein 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)
40% identity, 92% coverage: 31:453/461 of query aligns to 9:415/422 of 6rl5G
- active site: S16 (≠ P38), F137 (≠ Y158), D237 (= D266), K266 (= K295)
- binding pyridoxal-5'-phosphate: G110 (= G131), T111 (≠ A132), F137 (≠ Y158), H138 (= H159), D237 (= D266), I239 (≠ V268), Q240 (= Q269), K266 (= K295), G294 (= G322), T295 (= T323)
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, 88% coverage: 47:453/461 of query aligns to 28:419/421 of P50457
- K267 (= K295) mutation to A: No GABA-AT activity.
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
37% identity, 87% coverage: 43:443/461 of query aligns to 21:376/387 of 1wkhA
- active site: F132 (≠ Y158), E184 (= E233), D217 (= D266), Q220 (= Q269), K246 (= K295), T275 (= T323), R363 (= R430)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ A68), S104 (= S130), G105 (= G131), T106 (≠ A132), F132 (≠ Y158), S133 (≠ H159), E184 (= E233), E189 (= E238), D217 (= D266), I219 (≠ V268), K246 (= K295), R363 (= R430)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
37% identity, 87% coverage: 43:443/461 of query aligns to 21:376/387 of 1wkgA
- active site: F132 (≠ Y158), E184 (= E233), D217 (= D266), Q220 (= Q269), K246 (= K295), T275 (= T323), R363 (= R430)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ A68), G105 (= G131), T106 (≠ A132), F132 (≠ Y158), S133 (≠ H159), R135 (≠ M161), E184 (= E233), D217 (= D266), I219 (≠ V268), Q220 (= Q269), K246 (= K295), G273 (≠ T321), T274 (≠ G322), T275 (= T323)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
37% identity, 87% coverage: 43:443/461 of query aligns to 21:376/387 of 1vefA
- active site: F132 (≠ Y158), D217 (= D266), K246 (= K295), T275 (= T323), R363 (= R430)
- binding pyridoxal-5'-phosphate: G105 (= G131), T106 (≠ A132), F132 (≠ Y158), S133 (≠ H159), E184 (= E233), D217 (= D266), I219 (≠ V268), K246 (= K295)
Sites not aligning to the query:
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
37% identity, 87% coverage: 43:443/461 of query aligns to 29:384/395 of Q5SHH5
- GT 113:114 (≠ GA 131:132) binding
- K254 (= K295) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T323) binding
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
36% identity, 89% coverage: 42:452/461 of query aligns to 23:423/425 of 1sffA
- active site: Y137 (= Y158), E205 (= E233), D238 (= D266), Q241 (= Q269), K267 (= K295), T296 (= T323), R397 (= R430)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ H95), G110 (= G131), S111 (≠ A132), Y137 (= Y158), H138 (= H159), R140 (≠ M161), E205 (= E233), D238 (= D266), V240 (= V268), Q241 (= Q269), K267 (= K295), T296 (= T323)
- binding sulfate ion: N152 (≠ S173), Y393 (≠ G426)
Sites not aligning to the query:
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
36% identity, 89% coverage: 42:452/461 of query aligns to 23:423/425 of 1sf2A
- active site: Y137 (= Y158), E205 (= E233), D238 (= D266), Q241 (= Q269), K267 (= K295), T296 (= T323), R397 (= R430)
- binding pyridoxal-5'-phosphate: G110 (= G131), S111 (≠ A132), Y137 (= Y158), H138 (= H159), E205 (= E233), D238 (= D266), V240 (= V268), Q241 (= Q269), K267 (= K295)
- binding sulfate ion: N152 (≠ S173), Y393 (≠ G426)
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)
36% identity, 89% coverage: 42:452/461 of query aligns to 24:424/426 of P22256
- I50 (≠ A68) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 131:132) binding
- E211 (= E238) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V268) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q269) binding
- K268 (= K295) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T323) binding
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)
33% identity, 90% coverage: 38:453/461 of query aligns to 33:442/454 of O50131
- T92 (≠ L97) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (= D98) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G131) binding
- T125 (≠ A132) binding
- Q267 (= Q269) binding
- K293 (= K295) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T323) binding
7vo1A Structure of aminotransferase-substrate complex (see paper)
33% identity, 90% coverage: 38:453/461 of query aligns to 31:440/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ A68), S121 (= S130), G122 (= G131), T123 (≠ A132), F149 (≠ Y158), H150 (= H159), R152 (≠ M161), E234 (= E238), D262 (= D266), V264 (= V268), Q265 (= Q269), K291 (= K295), N318 (≠ G322), T319 (= T323), R417 (= R430)
7vntA Structure of aminotransferase-substrate complex (see paper)
33% identity, 90% coverage: 38:453/461 of query aligns to 31:440/452 of 7vntA
- binding L-ornithine: F149 (≠ Y158), R152 (≠ M161), E234 (= E238), K291 (= K295)
- binding pyridoxal-5'-phosphate: G122 (= G131), T123 (≠ A132), F149 (≠ Y158), H150 (= H159), E229 (= E233), D262 (= D266), V264 (= V268), Q265 (= Q269), K291 (= K295)
7vnoA Structure of aminotransferase (see paper)
33% identity, 90% coverage: 38:453/461 of query aligns to 31:440/452 of 7vnoA
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
35% identity, 89% coverage: 42:452/461 of query aligns to 23:423/425 of 1szkA
- active site: Y137 (= Y158), E205 (= E233), D238 (= D266), Q241 (= Q269), K267 (= K295), T296 (= T323), R397 (= R430)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G131), S111 (≠ A132), Y137 (= Y158), H138 (= H159), E205 (= E233), D238 (= D266), V240 (= V268), Q241 (= Q269), K267 (= K295)
Sites not aligning to the query:
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)
33% identity, 90% coverage: 41:453/461 of query aligns to 52:458/474 of O58478
- D251 (≠ E238) mutation to A: Loss of activity.
- K308 (= K295) mutation to A: Loss of activity.
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
33% identity, 90% coverage: 43:455/461 of query aligns to 27:431/439 of 5wyaA
- active site: Y140 (= Y158), E215 (= E233), D248 (= D266), N251 (≠ Q269), K278 (= K295), T307 (= T323), R406 (= R430)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (= A68), Y82 (≠ L92), S112 (= S130), G113 (= G131), S114 (≠ A132), Y140 (= Y158), H141 (= H159), E215 (= E233), D248 (= D266), V250 (= V268), N251 (≠ Q269), K278 (= K295), F306 (≠ G322), T307 (= T323), R406 (= R430)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
33% identity, 90% coverage: 43:455/461 of query aligns to 36:440/448 of 4ysnC
- active site: Y149 (= Y158), E224 (= E233), D257 (= D266), N260 (≠ Q269), K287 (= K295), T316 (= T323), R415 (= R430)
- binding pyridoxal-5'-phosphate: S121 (= S130), G122 (= G131), S123 (≠ A132), Y149 (= Y158), H150 (= H159), E224 (= E233), D257 (= D266), V259 (= V268), K287 (= K295), F315 (≠ G322), T316 (= T323)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
33% identity, 90% coverage: 43:455/461 of query aligns to 29:433/446 of 5wyfA
- active site: Y142 (= Y158), E217 (= E233), D250 (= D266), N253 (≠ Q269), K280 (= K295), T309 (= T323), R408 (= R430)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (= A68), Y84 (≠ L92), G115 (= G131), S116 (≠ A132), Y142 (= Y158), H143 (= H159), D222 (≠ E238), D250 (= D266), V252 (= V268), N253 (≠ Q269), K280 (= K295), F308 (≠ G322), T309 (= T323), R408 (= R430)
Sites not aligning to the query:
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
32% identity, 89% coverage: 34:443/461 of query aligns to 5:366/376 of O66442
- GT 96:97 (≠ GA 131:132) binding
- K242 (= K295) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T323) binding
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
32% identity, 89% coverage: 34:443/461 of query aligns to 4:365/375 of 2eh6A
- active site: F127 (≠ Y158), E179 (= E233), D212 (= D266), Q215 (= Q269), K241 (= K295), T270 (= T323), R352 (= R430)
- binding pyridoxal-5'-phosphate: G95 (= G131), T96 (≠ A132), F127 (≠ Y158), H128 (= H159), E179 (= E233), D212 (= D266), V214 (= V268), K241 (= K295)
Query Sequence
>BWI76_RS14020 BWI76_RS14020 aspartate aminotransferase family protein
MMTDKVRIDTLGADLLDANNDTFLARQAEFESNVRSYPRKLPLAITKAEGVWLTDADNKQ
YLDCLAGAGTLALGHNHPDVLQSIQSVITSGLPLHTLDLTTPLKDRFSEYLLSLLPGEGK
EYCLQFTGPSGADAVEAALKLAKKYTGRSSVISFSGGYHGMTHGALSVTGNLSPKAAVNG
MMPEVQFMPYPHQYRCPLGIGGEAGVKALTYYFENLINDVESGVRKPAAVILEAVQGEGG
VNPAPVEWLQRIRKVTQEHGILLIIDEVQAGFARTGKFFAFEHAGIEPDIIVMSKAVGGG
LPLAVLGIKKQFDAWEPGHHTGTFRGNQLAMATGLTTLRHLKDNKIADKTAAQGEWLKGK
LAEMQKRYPVIGHVRGLGLMIGIEIVKPNEAPDHMGCYPADGELSALLQKKCFEAGLILE
RGGRHGCVLRLLPSLLISNAELEIFFDKFEQALLAAGVKPV
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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