SitesBLAST
Comparing WP_012061607.1 NCBI__GCF_000017145.1:WP_012061607.1 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)
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)
61% identity, 97% coverage: 7:417/422 of query aligns to 9:419/421 of P50457
- K267 (= K265) mutation to A: No GABA-AT activity.
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)
57% identity, 99% coverage: 4:421/422 of query aligns to 7:425/426 of P22256
- I50 (= I47) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 108:109) binding pyridoxal 5'-phosphate
- E211 (= E208) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V238) 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
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
57% identity, 99% coverage: 4:421/422 of query aligns to 6:424/425 of 1sffA
- active site: V18 (= V16), Y137 (≠ F135), E205 (= E203), D238 (= D236), Q241 (= Q239), K267 (= K265), T296 (= T294), R397 (= R394)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q76), G110 (= G108), S111 (≠ A109), Y137 (≠ F135), H138 (= H136), R140 (= R138), E205 (= E203), D238 (= D236), V240 (= V238), Q241 (= Q239), K267 (= K265), T296 (= T294)
- binding sulfate ion: N152 (≠ V150), Y393 (≠ G390)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
57% identity, 99% coverage: 4:421/422 of query aligns to 6:424/425 of 1sf2A
- active site: V18 (= V16), Y137 (≠ F135), E205 (= E203), D238 (= D236), Q241 (= Q239), K267 (= K265), T296 (= T294), R397 (= R394)
- binding pyridoxal-5'-phosphate: G110 (= G108), S111 (≠ A109), Y137 (≠ F135), H138 (= H136), E205 (= E203), D238 (= D236), V240 (= V238), Q241 (= Q239), K267 (= K265)
- binding sulfate ion: N152 (≠ V150), Y393 (≠ G390)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
57% identity, 99% coverage: 4:421/422 of query aligns to 6:424/425 of 1szkA
- active site: V18 (= V16), Y137 (≠ F135), E205 (= E203), D238 (= D236), Q241 (= Q239), K267 (= K265), T296 (= T294), R397 (= R394)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G108), S111 (≠ A109), Y137 (≠ F135), H138 (= H136), E205 (= E203), D238 (= D236), V240 (= V238), Q241 (= Q239), K267 (= K265)
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
49% identity, 99% coverage: 4:421/422 of query aligns to 20:439/439 of 3q8nC
- active site: V32 (= V16), Y151 (≠ F135), E221 (= E203), D254 (= D236), Q257 (= Q239), K283 (= K265), T312 (= T294), R412 (= R394)
- binding 4-oxobutanoic acid: G124 (= G108), A125 (= A109), V256 (= V238), K283 (= K265)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
46% identity, 98% coverage: 3:417/422 of query aligns to 22:435/440 of 6j2vA
- active site: L35 (≠ V16), Y154 (≠ F135), D256 (= D236), K285 (= K265)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G108), A128 (= A109), Y154 (≠ F135), H155 (= H136), R157 (= R138), E223 (= E203), E228 (= E208), D256 (= D236), I258 (≠ V238), K285 (= K265), G313 (= G293), T314 (= T294)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
46% identity, 98% coverage: 3:417/422 of query aligns to 22:441/444 of 4atqF
- active site: V35 (= V16), Y154 (≠ F135), E226 (= E203), D259 (= D236), Q262 (= Q239), K288 (= K265), T317 (= T294), R418 (= R394)
- binding gamma-amino-butanoic acid: M95 (≠ Q76), Y154 (≠ F135), R157 (= R138), E231 (= E208), K288 (= K265), G316 (= G293)
- binding pyridoxal-5'-phosphate: G127 (= G108), A128 (= A109), Y154 (≠ F135), H155 (= H136), D259 (= D236), V261 (= V238)
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)
36% identity, 98% coverage: 4:417/422 of query aligns to 35:458/474 of O58478
- D251 (≠ E208) mutation to A: Loss of activity.
- K308 (= K265) mutation to A: Loss of activity.
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)
40% identity, 93% coverage: 25:417/422 of query aligns to 41:442/454 of O50131
- T92 (≠ C74) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ H75) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G108) binding pyridoxal 5'-phosphate
- T125 (≠ A109) binding pyridoxal 5'-phosphate
- Q267 (= Q239) binding pyridoxal 5'-phosphate
- K293 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T294) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
40% identity, 93% coverage: 25:417/422 of query aligns to 39:440/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I47), S121 (≠ T107), G122 (= G108), T123 (≠ A109), F149 (= F135), H150 (= H136), R152 (= R138), E234 (= E208), D262 (= D236), V264 (= V238), Q265 (= Q239), K291 (= K265), N318 (≠ G293), T319 (= T294), R417 (= R394)
7vntA Structure of aminotransferase-substrate complex (see paper)
40% identity, 93% coverage: 25:417/422 of query aligns to 39:440/452 of 7vntA
- binding L-ornithine: F149 (= F135), R152 (= R138), E234 (= E208), K291 (= K265)
- binding pyridoxal-5'-phosphate: G122 (= G108), T123 (≠ A109), F149 (= F135), H150 (= H136), E229 (= E203), D262 (= D236), V264 (= V238), Q265 (= Q239), K291 (= K265)
7vnoA Structure of aminotransferase (see paper)
40% identity, 93% coverage: 25:417/422 of query aligns to 39:440/452 of 7vnoA
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
33% identity, 99% coverage: 2:417/422 of query aligns to 6:429/439 of 5wyaA
- active site: A20 (≠ V16), Y140 (≠ F135), E215 (= E203), D248 (= D236), N251 (≠ Q239), K278 (= K265), T307 (= T294), R406 (= R394)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I47), Y82 (≠ V77), S112 (≠ T107), G113 (= G108), S114 (≠ A109), Y140 (≠ F135), H141 (= H136), E215 (= E203), D248 (= D236), V250 (= V238), N251 (≠ Q239), K278 (= K265), F306 (≠ G293), T307 (= T294), R406 (= R394)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
33% identity, 99% coverage: 2:417/422 of query aligns to 15:438/448 of 4ysnC
- active site: A29 (≠ V16), Y149 (≠ F135), E224 (= E203), D257 (= D236), N260 (≠ Q239), K287 (= K265), T316 (= T294), R415 (= R394)
- binding pyridoxal-5'-phosphate: S121 (≠ T107), G122 (= G108), S123 (≠ A109), Y149 (≠ F135), H150 (= H136), E224 (= E203), D257 (= D236), V259 (= V238), K287 (= K265), F315 (≠ G293), T316 (= T294)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
33% identity, 99% coverage: 2:417/422 of query aligns to 8:431/446 of 5wyfA
- active site: A22 (≠ V16), Y142 (≠ F135), E217 (= E203), D250 (= D236), N253 (≠ Q239), K280 (= K265), T309 (= T294), R408 (= R394)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I47), Y84 (≠ V77), G115 (= G108), S116 (≠ A109), Y142 (≠ F135), H143 (= H136), D222 (≠ E208), D250 (= D236), V252 (= V238), N253 (≠ Q239), K280 (= K265), F308 (≠ G293), T309 (= T294), R408 (= R394)
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
39% identity, 90% coverage: 26:404/422 of query aligns to 33:381/395 of Q5SHH5
- GT 113:114 (≠ GA 108:109) binding pyridoxal 5'-phosphate
- K254 (= K265) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T294) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
38% identity, 90% coverage: 26:404/422 of query aligns to 25:373/387 of 1wkhA
- active site: F132 (= F135), E184 (= E203), D217 (= D236), Q220 (= Q239), K246 (= K265), T275 (= T294), R363 (= R394)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I47), S104 (≠ T107), G105 (= G108), T106 (≠ A109), F132 (= F135), S133 (≠ H136), E184 (= E203), E189 (= E208), D217 (= D236), I219 (≠ V238), K246 (= K265), R363 (= R394)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
38% identity, 90% coverage: 26:404/422 of query aligns to 25:373/387 of 1wkgA
- active site: F132 (= F135), E184 (= E203), D217 (= D236), Q220 (= Q239), K246 (= K265), T275 (= T294), R363 (= R394)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ I47), G105 (= G108), T106 (≠ A109), F132 (= F135), S133 (≠ H136), R135 (= R138), E184 (= E203), D217 (= D236), I219 (≠ V238), Q220 (= Q239), K246 (= K265), G273 (= G292), T274 (≠ G293), T275 (= T294)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
38% identity, 90% coverage: 26:404/422 of query aligns to 25:373/387 of 1vefA
- active site: F132 (= F135), D217 (= D236), K246 (= K265), T275 (= T294), R363 (= R394)
- binding pyridoxal-5'-phosphate: G105 (= G108), T106 (≠ A109), F132 (= F135), S133 (≠ H136), E184 (= E203), D217 (= D236), I219 (≠ V238), K246 (= K265)
Sites not aligning to the query:
Query Sequence
>WP_012061607.1 NCBI__GCF_000017145.1:WP_012061607.1
MTSLTDRKNAAISRGVGMTTQIYAERAENAEIWDKEGNRYIDFASGIAVVNTGHRHPKVI
AAVKAQLDRFTHTCHQVVPYENYVHLAERLNAIVPGDFAKKTIFVTTGAEAVENAVKIAR
AATGRQAIVAFGGGFHGRTFMGMALTGKVVPYKVGFGAMPADVFHAPFPVELHGVSVEQS
LAALKKLFAADVDPNRVAAIIIEPVQGEGGFYPVPTAFMKALREICDQNGILLIADEVQT
GFARTGKLLAMEHHGVAPDLTTMAKSLAGGFPLAAVTGRAEIMDAPGPGGLGGTYGGNPL
GIAAAHAVLDVIAEENLCERANQLGNRLKQRLAAIREKAPEIVDIRGPGFMNAVEFNDVK
TNVPSAEFANKVRLLALEKGLILLTCGVHGNVIRFLAPITIQDDVFAEALDILESSILEA
RG
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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