SitesBLAST
Comparing WP_008805274.1 NCBI__GCF_000025465.1:WP_008805274.1 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)
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)
89% identity, 100% coverage: 1:426/427 of query aligns to 1:426/426 of P22256
- I50 (= I50) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (= GS 111:112) binding pyridoxal 5'-phosphate
- E211 (= E211) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V241) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q242) binding pyridoxal 5'-phosphate
- K268 (= K268) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T297) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
89% identity, 100% coverage: 2:426/427 of query aligns to 1:425/425 of 1sffA
- active site: V18 (= V19), Y137 (= Y138), E205 (= E206), D238 (= D239), Q241 (= Q242), K267 (= K268), T296 (= T297), R397 (= R398)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q79), G110 (= G111), S111 (= S112), Y137 (= Y138), H138 (= H139), R140 (= R141), E205 (= E206), D238 (= D239), V240 (= V241), Q241 (= Q242), K267 (= K268), T296 (= T297)
- binding sulfate ion: N152 (= N153), Y393 (= Y394)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
89% identity, 100% coverage: 2:426/427 of query aligns to 1:425/425 of 1sf2A
- active site: V18 (= V19), Y137 (= Y138), E205 (= E206), D238 (= D239), Q241 (= Q242), K267 (= K268), T296 (= T297), R397 (= R398)
- binding pyridoxal-5'-phosphate: G110 (= G111), S111 (= S112), Y137 (= Y138), H138 (= H139), E205 (= E206), D238 (= D239), V240 (= V241), Q241 (= Q242), K267 (= K268)
- binding sulfate ion: N152 (= N153), Y393 (= Y394)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
89% identity, 100% coverage: 2:426/427 of query aligns to 1:425/425 of 1szkA
- active site: V18 (= V19), Y137 (= Y138), E205 (= E206), D238 (= D239), Q241 (= Q242), K267 (= K268), T296 (= T297), R397 (= R398)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G111), S111 (= S112), Y137 (= Y138), H138 (= H139), E205 (= E206), D238 (= D239), V240 (= V241), Q241 (= Q242), K267 (= K268)
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)
55% identity, 99% coverage: 3:423/427 of query aligns to 2:421/421 of P50457
- K267 (= K268) mutation to A: No GABA-AT activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
45% identity, 99% coverage: 4:425/427 of query aligns to 17:439/439 of 3q8nC
- active site: V32 (= V19), Y151 (= Y138), E221 (= E206), D254 (= D239), Q257 (= Q242), K283 (= K268), T312 (= T297), R412 (= R398)
- binding 4-oxobutanoic acid: G124 (= G111), A125 (≠ S112), V256 (= V241), K283 (= K268)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
44% identity, 97% coverage: 4:417/427 of query aligns to 20:431/440 of 6j2vA
- active site: L35 (≠ V19), Y154 (= Y138), D256 (= D239), K285 (= K268)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G111), A128 (≠ S112), Y154 (= Y138), H155 (= H139), R157 (= R141), E223 (= E206), E228 (= E211), D256 (= D239), I258 (≠ V241), K285 (= K268), G313 (= G296), T314 (= T297)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
45% identity, 97% coverage: 3:418/427 of query aligns to 19:438/444 of 4atqF
- active site: V35 (= V19), Y154 (= Y138), E226 (= E206), D259 (= D239), Q262 (= Q242), K288 (= K268), T317 (= T297), R418 (= R398)
- binding gamma-amino-butanoic acid: M95 (≠ Q79), Y154 (= Y138), R157 (= R141), E231 (= E211), K288 (= K268), G316 (= G296)
- binding pyridoxal-5'-phosphate: G127 (= G111), A128 (≠ S112), Y154 (= Y138), H155 (= H139), D259 (= D239), V261 (= V241)
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)
35% identity, 97% coverage: 5:417/427 of query aligns to 33:454/474 of O58478
- D251 (≠ E211) mutation to A: Loss of activity.
- K308 (= K268) mutation to A: Loss of activity.
P40732 Acetylornithine/succinyldiaminopimelate aminotransferase; ACOAT; DapATase; Succinyldiaminopimelate transferase; EC 2.6.1.11; EC 2.6.1.17 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
37% identity, 96% coverage: 8:418/427 of query aligns to 1:397/405 of P40732
- GT 108:109 (≠ GS 111:112) binding pyridoxal 5'-phosphate
- K255 (= K268) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T297) binding pyridoxal 5'-phosphate
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
38% identity, 91% coverage: 29:418/427 of query aligns to 25:392/402 of 4jevB
- active site: F136 (≠ Y138), E188 (= E206), D221 (= D239), Q224 (= Q242), K250 (= K268), T279 (= T297), R372 (= R398)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I50), S102 (≠ T110), G103 (= G111), T104 (≠ S112), F136 (≠ Y138), H137 (= H139), E188 (= E206), E193 (= E211), D221 (= D239), V223 (= V241), Q224 (= Q242), K250 (= K268), R372 (= R398)
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)
39% identity, 93% coverage: 28:424/427 of query aligns to 41:441/454 of O50131
- T92 (≠ V80) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ L81) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G111) binding pyridoxal 5'-phosphate
- T125 (≠ S112) binding pyridoxal 5'-phosphate
- Q267 (= Q242) binding pyridoxal 5'-phosphate
- K293 (= K268) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T297) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
39% identity, 93% coverage: 28:424/427 of query aligns to 39:439/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I50), S121 (≠ T110), G122 (= G111), T123 (≠ S112), F149 (≠ Y138), H150 (= H139), R152 (= R141), E234 (= E211), D262 (= D239), V264 (= V241), Q265 (= Q242), K291 (= K268), N318 (≠ G296), T319 (= T297), R417 (= R398)
7vntA Structure of aminotransferase-substrate complex (see paper)
39% identity, 93% coverage: 28:424/427 of query aligns to 39:439/452 of 7vntA
- binding L-ornithine: F149 (≠ Y138), R152 (= R141), E234 (= E211), K291 (= K268)
- binding pyridoxal-5'-phosphate: G122 (= G111), T123 (≠ S112), F149 (≠ Y138), H150 (= H139), E229 (= E206), D262 (= D239), V264 (= V241), Q265 (= Q242), K291 (= K268)
7vnoA Structure of aminotransferase (see paper)
39% identity, 93% coverage: 28:424/427 of query aligns to 39:439/452 of 7vnoA
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
33% identity, 93% coverage: 28:422/427 of query aligns to 32:432/446 of 5wyfA
- active site: Y142 (= Y138), E217 (= E206), D250 (= D239), N253 (≠ Q242), K280 (= K268), T309 (≠ G296), R408 (= R398)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I50), Y84 (≠ V80), G115 (= G111), S116 (= S112), Y142 (= Y138), H143 (= H139), D222 (≠ E211), D250 (= D239), V252 (= V241), N253 (≠ Q242), K280 (= K268), F308 (≠ G295), T309 (≠ G296), R408 (= R398)
Sites not aligning to the query:
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
33% identity, 93% coverage: 28:422/427 of query aligns to 30:430/439 of 5wyaA
- active site: Y140 (= Y138), E215 (= E206), D248 (= D239), N251 (≠ Q242), K278 (= K268), T307 (≠ G296), R406 (= R398)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I50), Y82 (≠ V80), S112 (≠ T110), G113 (= G111), S114 (= S112), Y140 (= Y138), H141 (= H139), E215 (= E206), D248 (= D239), V250 (= V241), N251 (≠ Q242), K278 (= K268), F306 (≠ G295), T307 (≠ G296), R406 (= R398)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
33% identity, 93% coverage: 28:422/427 of query aligns to 39:439/448 of 4ysnC
- active site: Y149 (= Y138), E224 (= E206), D257 (= D239), N260 (≠ Q242), K287 (= K268), T316 (≠ G296), R415 (= R398)
- binding pyridoxal-5'-phosphate: S121 (≠ T110), G122 (= G111), S123 (= S112), Y149 (= Y138), H150 (= H139), E224 (= E206), D257 (= D239), V259 (= V241), K287 (= K268), F315 (≠ G295), T316 (≠ G296)
Sites not aligning to the query:
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
37% identity, 93% coverage: 22:418/427 of query aligns to 12:387/397 of 4jewA
- active site: F136 (≠ Y138), E188 (= E206), D221 (= D239), Q224 (= Q242), K250 (= K268), T274 (= T297), R367 (= R398)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G111), T104 (≠ S112), F136 (≠ Y138), H137 (= H139), R139 (= R141), E188 (= E206), E193 (= E211), D221 (= D239), V223 (= V241), K250 (= K268)
- binding picric acid: K25 (≠ R29), K27 (≠ E31), W32 (= W36)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
37% identity, 91% coverage: 29:418/427 of query aligns to 19:381/389 of 2pb0A
- active site: F130 (≠ Y138), E182 (= E206), D215 (= D239), Q218 (= Q242), K244 (= K268), T268 (= T297), R361 (= R398)
- binding pyridoxal-5'-phosphate: S96 (≠ T110), G97 (= G111), T98 (≠ S112), F130 (≠ Y138), H131 (= H139), E182 (= E206), D215 (= D239), V217 (= V241), Q218 (= Q242), K244 (= K268)
Query Sequence
>WP_008805274.1 NCBI__GCF_000025465.1:WP_008805274.1
MNSNKAMMARRSDAVPRGVGQIHPIFAERAENCRVWDVEGREYLDFAGGIAVLNTGHLHP
QVVAAVEDQLKKLSHTCFQVLAYEPYLALCEKMNQKVPGDFAKKTLLVTTGSEAVENAVK
IARAATGRSGAIAFTGAYHGRTHYTLSLTGKVNPYSAGMGLMPGHVYRALYPCALHGVSD
DEAIASIHRIFKNDAAPEDIAAIIIEPVQGEGGFYAASPAFMQRLRALCDEHGIMLIADE
VQSGAGRTGTLFAMEQMGVAADITTFAKSIAGGFPLAGVTGRAEVMDAIAPGGLGGTYAG
NPIACAAALAVLQIFEQENLLEKANQLGDTLRQGLLAIAEDHPEIGDVRGLGAMIAIELF
EEGDRSKPNARLTADIVARARDKGLILLSCGPYYNVLRILVPLTIEEAQIEQGLKIIADC
FTEAKQA
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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