SitesBLAST
Comparing WP_035703857.1 NCBI__GCF_000691145.1:WP_035703857.1 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)
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
45% identity, 97% coverage: 10:435/438 of query aligns to 2:420/425 of 1sffA
- active site: V18 (= V26), Y137 (≠ F145), E205 (= E220), D238 (= D253), Q241 (= Q256), K267 (= K282), T296 (= T311), R397 (= R412)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ N86), G110 (= G118), S111 (≠ A119), Y137 (≠ F145), H138 (= H146), R140 (= R148), E205 (= E220), D238 (= D253), V240 (≠ I255), Q241 (= Q256), K267 (= K282), T296 (= T311)
- binding sulfate ion: N152 (≠ K160), Y393 (≠ G408)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
45% identity, 97% coverage: 10:435/438 of query aligns to 2:420/425 of 1sf2A
- active site: V18 (= V26), Y137 (≠ F145), E205 (= E220), D238 (= D253), Q241 (= Q256), K267 (= K282), T296 (= T311), R397 (= R412)
- binding pyridoxal-5'-phosphate: G110 (= G118), S111 (≠ A119), Y137 (≠ F145), H138 (= H146), E205 (= E220), D238 (= D253), V240 (≠ I255), Q241 (= Q256), K267 (= K282)
- binding sulfate ion: N152 (≠ K160), Y393 (≠ G408)
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)
45% identity, 97% coverage: 10:435/438 of query aligns to 3:421/426 of P22256
- I50 (= I57) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 118:119) binding pyridoxal 5'-phosphate
- E211 (= E225) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I255) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q256) binding pyridoxal 5'-phosphate
- K268 (= K282) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T311) binding pyridoxal 5'-phosphate
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
44% identity, 97% coverage: 10:435/438 of query aligns to 2:420/425 of 1szkA
- active site: V18 (= V26), Y137 (≠ F145), E205 (= E220), D238 (= D253), Q241 (= Q256), K267 (= K282), T296 (= T311), R397 (= R412)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G118), S111 (≠ A119), Y137 (≠ F145), H138 (= H146), E205 (= E220), D238 (= D253), V240 (≠ I255), Q241 (= Q256), K267 (= K282)
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
49% identity, 97% coverage: 11:435/438 of query aligns to 17:435/439 of 3q8nC
- active site: V32 (= V26), Y151 (≠ F145), E221 (= E220), D254 (= D253), Q257 (= Q256), K283 (= K282), T312 (= T311), R412 (= R412)
- binding 4-oxobutanoic acid: G124 (= G118), A125 (= A119), V256 (≠ I255), K283 (= K282)
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)
46% identity, 98% coverage: 9:436/438 of query aligns to 1:420/421 of P50457
- K267 (= K282) mutation to A: No GABA-AT activity.
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
47% identity, 96% coverage: 17:435/438 of query aligns to 26:435/440 of 6j2vA
- active site: L35 (≠ V26), Y154 (≠ F145), D256 (= D253), K285 (= K282)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G118), A128 (= A119), Y154 (≠ F145), H155 (= H146), R157 (= R148), E223 (= E220), E228 (= E225), D256 (= D253), I258 (= I255), K285 (= K282), G313 (= G310), T314 (= T311)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
46% identity, 96% coverage: 17:437/438 of query aligns to 26:443/444 of 4atqF
- active site: V35 (= V26), Y154 (≠ F145), E226 (= E220), D259 (= D253), Q262 (= Q256), K288 (= K282), T317 (= T311), R418 (= R412)
- binding gamma-amino-butanoic acid: M95 (≠ N86), Y154 (≠ F145), R157 (= R148), E231 (= E225), K288 (= K282), G316 (= G310)
- binding pyridoxal-5'-phosphate: G127 (= G118), A128 (= A119), Y154 (≠ F145), H155 (= H146), D259 (= D253), V261 (≠ I255)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
38% identity, 96% coverage: 17:437/438 of query aligns to 13:433/446 of 5wyfA
- active site: A22 (≠ V26), Y142 (≠ F145), E217 (= E220), D250 (= D253), N253 (≠ Q256), K280 (= K282), T309 (= T311), R408 (= R412)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I57), Y84 (≠ V87), G115 (= G118), S116 (≠ A119), Y142 (≠ F145), H143 (= H146), D222 (≠ E225), D250 (= D253), V252 (≠ I255), N253 (≠ Q256), K280 (= K282), F308 (≠ G310), T309 (= T311), R408 (= R412)
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
38% identity, 96% coverage: 17:437/438 of query aligns to 11:431/439 of 5wyaA
- active site: A20 (≠ V26), Y140 (≠ F145), E215 (= E220), D248 (= D253), N251 (≠ Q256), K278 (= K282), T307 (= T311), R406 (= R412)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I57), Y82 (≠ V87), S112 (= S117), G113 (= G118), S114 (≠ A119), Y140 (≠ F145), H141 (= H146), E215 (= E220), D248 (= D253), V250 (≠ I255), N251 (≠ Q256), K278 (= K282), F306 (≠ G310), T307 (= T311), R406 (= R412)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
38% identity, 96% coverage: 17:437/438 of query aligns to 20:440/448 of 4ysnC
- active site: A29 (≠ V26), Y149 (≠ F145), E224 (= E220), D257 (= D253), N260 (≠ Q256), K287 (= K282), T316 (= T311), R415 (= R412)
- binding pyridoxal-5'-phosphate: S121 (= S117), G122 (= G118), S123 (≠ A119), Y149 (≠ F145), H150 (= H146), E224 (= E220), D257 (= D253), V259 (≠ I255), K287 (= K282), F315 (≠ G310), T316 (= T311)
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, 95% coverage: 20:435/438 of query aligns to 24:442/454 of O50131
- T92 (≠ N86) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ V87) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G118) binding pyridoxal 5'-phosphate
- T125 (≠ A119) binding pyridoxal 5'-phosphate
- Q267 (= Q256) binding pyridoxal 5'-phosphate
- K293 (= K282) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T311) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
36% identity, 95% coverage: 20:435/438 of query aligns to 22:440/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I57), S121 (= S117), G122 (= G118), T123 (≠ A119), F149 (= F145), H150 (= H146), R152 (= R148), E234 (= E225), D262 (= D253), V264 (≠ I255), Q265 (= Q256), K291 (= K282), N318 (≠ G310), T319 (= T311), R417 (= R412)
7vntA Structure of aminotransferase-substrate complex (see paper)
36% identity, 95% coverage: 20:435/438 of query aligns to 22:440/452 of 7vntA
- binding L-ornithine: F149 (= F145), R152 (= R148), E234 (= E225), K291 (= K282)
- binding pyridoxal-5'-phosphate: G122 (= G118), T123 (≠ A119), F149 (= F145), H150 (= H146), E229 (= E220), D262 (= D253), V264 (≠ I255), Q265 (= Q256), K291 (= K282)
7vnoA Structure of aminotransferase (see paper)
36% identity, 95% coverage: 20:435/438 of query aligns to 22:440/452 of 7vnoA
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, 91% coverage: 36:434/438 of query aligns to 58:457/474 of O58478
- D251 (≠ E225) mutation to A: Loss of activity.
- K308 (= K282) mutation to A: Loss of activity.
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
35% identity, 90% coverage: 37:432/438 of query aligns to 31:406/412 of 2eo5A
- active site: F139 (= F145), E219 (= E220), D252 (= D253), Q255 (= Q256), K281 (= K282), T303 (= T311), R386 (= R412)
- binding pyridoxal-5'-phosphate: G113 (= G118), T114 (≠ A119), F139 (= F145), H140 (= H146), E219 (= E220), D252 (= D253), V254 (≠ I255), Q255 (= Q256), K281 (= K282)
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)
35% identity, 95% coverage: 10:425/438 of query aligns to 5:384/395 of Q5SHH5
- GT 113:114 (≠ GA 118:119) binding pyridoxal 5'-phosphate
- K254 (= K282) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T311) binding pyridoxal 5'-phosphate
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 92% coverage: 25:425/438 of query aligns to 14:376/387 of 1wkhA
- active site: F132 (= F145), E184 (= E220), D217 (= D253), Q220 (= Q256), K246 (= K282), T275 (= T311), R363 (= R412)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I57), S104 (= S117), G105 (= G118), T106 (≠ A119), F132 (= F145), S133 (≠ H146), E184 (= E220), E189 (= E225), D217 (= D253), I219 (= I255), K246 (= K282), R363 (= R412)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 92% coverage: 25:425/438 of query aligns to 14:376/387 of 1wkgA
- active site: F132 (= F145), E184 (= E220), D217 (= D253), Q220 (= Q256), K246 (= K282), T275 (= T311), R363 (= R412)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (≠ S27), Y46 (≠ I57), G105 (= G118), T106 (≠ A119), F132 (= F145), S133 (≠ H146), R135 (= R148), E184 (= E220), D217 (= D253), I219 (= I255), Q220 (= Q256), K246 (= K282), G273 (= G309), T274 (≠ G310), T275 (= T311)
Sites not aligning to the query:
Query Sequence
>WP_035703857.1 NCBI__GCF_000691145.1:WP_035703857.1
MSQTTTNRFSTEEWQGKRDQYVARGVSNGNRHLATKGKGAELFDIDGNRFIDFAGAIGTL
NVGHSHPKVVEAVKAQADSLIHPGFNVMMYESYIELAEKLCHLTPGDHDKKAIFLNSGAE
AVENAVKIARKYTKRQAVVSFTRGFHGRTNMTMSMTSKVKPYKFGFGPFASEVYQAPYPY
YYQKPEGLSDAAYDEYIIDQFNQFFVATVAPETVACVVMEPVQGEGGFIVPSKRFVQHVA
SFCQQHGIVFVADEIQTGFARTGKYFAIEHFDVVPDLITVSKSLAAGLPLSGVVGRKELL
DAADPGELGGTYAGSPLGCVAALAVLDIIETEQLNERSEHIGQVIEDKANEWRSQYSFIG
EVRRLGAMAAIEIVEDQKTRTPDKKTAAAIAAYANKHGLLLLTAGINGNIIRFLTPLVIT
DELLQEGLGIIEDAFTAR
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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