SitesBLAST
Comparing AO356_27515 FitnessBrowser__pseudo5_N2C3_1:AO356_27515 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)
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: 21:455/457 of query aligns to 10:445/454 of O50131
- T92 (≠ L100) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ E101) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G134) binding
- T125 (≠ S135) binding
- Q267 (= Q272) binding
- K293 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T327) binding
7vo1A Structure of aminotransferase-substrate complex (see paper)
36% identity, 95% coverage: 21:455/457 of query aligns to 8:443/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ V73), S121 (= S133), G122 (= G134), T123 (≠ S135), F149 (≠ Y161), H150 (= H162), R152 (≠ V164), E234 (= E241), D262 (= D269), V264 (= V271), Q265 (= Q272), K291 (= K298), N318 (= N326), T319 (= T327), R417 (= R429)
7vntA Structure of aminotransferase-substrate complex (see paper)
36% identity, 95% coverage: 21:455/457 of query aligns to 8:443/452 of 7vntA
- binding L-ornithine: F149 (≠ Y161), R152 (≠ V164), E234 (= E241), K291 (= K298)
- binding pyridoxal-5'-phosphate: G122 (= G134), T123 (≠ S135), F149 (≠ Y161), H150 (= H162), E229 (= E236), D262 (= D269), V264 (= V271), Q265 (= Q272), K291 (= K298)
7vnoA Structure of aminotransferase (see paper)
36% identity, 95% coverage: 21:455/457 of query aligns to 8:443/452 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)
34% identity, 96% coverage: 13:452/457 of query aligns to 19:458/474 of O58478
- D251 (≠ E241) mutation to A: Loss of activity.
- K308 (= K298) mutation to A: Loss of activity.
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
34% identity, 89% coverage: 48:456/457 of query aligns to 27:433/439 of 5wyaA
- active site: Y140 (= Y161), E215 (= E236), D248 (= D269), N251 (≠ Q272), K278 (= K298), T307 (= T327), R406 (= R429)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ V73), Y82 (vs. gap), S112 (= S133), G113 (= G134), S114 (= S135), Y140 (= Y161), H141 (= H162), E215 (= E236), D248 (= D269), V250 (= V271), N251 (≠ Q272), K278 (= K298), F306 (≠ N326), T307 (= T327), R406 (= R429)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
34% identity, 89% coverage: 48:456/457 of query aligns to 36:442/448 of 4ysnC
- active site: Y149 (= Y161), E224 (= E236), D257 (= D269), N260 (≠ Q272), K287 (= K298), T316 (= T327), R415 (= R429)
- binding pyridoxal-5'-phosphate: S121 (= S133), G122 (= G134), S123 (= S135), Y149 (= Y161), H150 (= H162), E224 (= E236), D257 (= D269), V259 (= V271), K287 (= K298), F315 (≠ N326), T316 (= T327)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
34% identity, 89% coverage: 48:456/457 of query aligns to 29:435/446 of 5wyfA
- active site: Y142 (= Y161), E217 (= E236), D250 (= D269), N253 (≠ Q272), K280 (= K298), T309 (= T327), R408 (= R429)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ V73), Y84 (vs. gap), G115 (= G134), S116 (= S135), Y142 (= Y161), H143 (= H162), D222 (≠ E241), D250 (= D269), V252 (= V271), N253 (≠ Q272), K280 (= K298), F308 (≠ N326), T309 (= T327), R408 (= R429)
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)
35% identity, 92% coverage: 32:453/457 of query aligns to 8:422/426 of P22256
- I50 (≠ V73) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (= GS 134:135) binding
- E211 (= E241) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V271) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q272) binding
- K268 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T327) binding
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
35% identity, 92% coverage: 32:453/457 of query aligns to 7:421/425 of 1sffA
- active site: V18 (≠ G43), Y137 (= Y161), E205 (= E236), D238 (= D269), Q241 (= Q272), K267 (= K298), T296 (= T327), R397 (= R429)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ S104), G110 (= G134), S111 (= S135), Y137 (= Y161), H138 (= H162), R140 (≠ V164), E205 (= E236), D238 (= D269), V240 (= V271), Q241 (= Q272), K267 (= K298), T296 (= T327)
- binding sulfate ion: N152 (≠ T175), Y393 (≠ S425)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
35% identity, 92% coverage: 32:453/457 of query aligns to 7:421/425 of 1sf2A
- active site: V18 (≠ G43), Y137 (= Y161), E205 (= E236), D238 (= D269), Q241 (= Q272), K267 (= K298), T296 (= T327), R397 (= R429)
- binding pyridoxal-5'-phosphate: G110 (= G134), S111 (= S135), Y137 (= Y161), H138 (= H162), E205 (= E236), D238 (= D269), V240 (= V271), Q241 (= Q272), K267 (= K298)
- binding sulfate ion: N152 (≠ T175), Y393 (≠ S425)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
34% identity, 92% coverage: 32:453/457 of query aligns to 7:421/425 of 1szkA
- active site: V18 (≠ G43), Y137 (= Y161), E205 (= E236), D238 (= D269), Q241 (= Q272), K267 (= K298), T296 (= T327), R397 (= R429)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G134), S111 (= S135), Y137 (= Y161), H138 (= H162), E205 (= E236), D238 (= D269), V240 (= V271), Q241 (= Q272), K267 (= K298)
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, 91% coverage: 35:452/457 of query aligns to 10:419/421 of P50457
- K267 (= K298) mutation to A: No GABA-AT activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
34% identity, 95% coverage: 16:448/457 of query aligns to 7:431/439 of 3q8nC
- active site: V32 (≠ G43), Y151 (= Y161), E221 (= E236), D254 (= D269), Q257 (= Q272), K283 (= K298), T312 (= T327), R412 (= R429)
- binding 4-oxobutanoic acid: G124 (= G134), A125 (≠ S135), V256 (= V271), K283 (= K298)
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
33% identity, 90% coverage: 46:455/457 of query aligns to 24:412/412 of 2eo5A
- active site: F139 (≠ Y161), E219 (= E236), D252 (= D269), Q255 (= Q272), K281 (= K298), T303 (= T327), R386 (= R429)
- binding pyridoxal-5'-phosphate: G113 (= G134), T114 (≠ S135), F139 (≠ Y161), H140 (= H162), E219 (= E236), D252 (= D269), V254 (= V271), Q255 (= Q272), K281 (= K298)
Sites not aligning to the query:
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
34% identity, 96% coverage: 16:454/457 of query aligns to 10:443/444 of 4atqF
- active site: V35 (vs. gap), Y154 (= Y161), E226 (= E236), D259 (= D269), Q262 (= Q272), K288 (= K298), T317 (= T327), R418 (= R429)
- binding gamma-amino-butanoic acid: M95 (≠ V102), Y154 (= Y161), R157 (≠ V164), E231 (= E241), K288 (= K298), G316 (≠ N326)
- binding pyridoxal-5'-phosphate: G127 (= G134), A128 (≠ S135), Y154 (= Y161), H155 (= H162), D259 (= D269), V261 (= V271)
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
36% identity, 85% coverage: 52:438/457 of query aligns to 33:380/395 of Q5SHH5
- GT 113:114 (≠ GS 134:135) binding
- K254 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T327) binding
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 85% coverage: 52:438/457 of query aligns to 25:372/387 of 1wkhA
- active site: F132 (≠ Y161), E184 (= E236), D217 (= D269), Q220 (= Q272), K246 (= K298), T275 (= T327), R363 (= R429)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ V73), S104 (= S133), G105 (= G134), T106 (≠ S135), F132 (≠ Y161), S133 (≠ H162), E184 (= E236), E189 (= E241), D217 (= D269), I219 (≠ V271), K246 (= K298), R363 (= R429)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 85% coverage: 52:438/457 of query aligns to 25:372/387 of 1wkgA
- active site: F132 (≠ Y161), E184 (= E236), D217 (= D269), Q220 (= Q272), K246 (= K298), T275 (= T327), R363 (= R429)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ V73), G105 (= G134), T106 (≠ S135), F132 (≠ Y161), S133 (≠ H162), R135 (≠ Q184), E184 (= E236), D217 (= D269), I219 (≠ V271), Q220 (= Q272), K246 (= K298), G273 (≠ P325), T274 (≠ N326), T275 (= T327)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 85% coverage: 52:438/457 of query aligns to 25:372/387 of 1vefA
- active site: F132 (≠ Y161), D217 (= D269), K246 (= K298), T275 (= T327), R363 (= R429)
- binding pyridoxal-5'-phosphate: G105 (= G134), T106 (≠ S135), F132 (≠ Y161), S133 (≠ H162), E184 (= E236), D217 (= D269), I219 (≠ V271), K246 (= K298)
Sites not aligning to the query:
Query Sequence
>AO356_27515 FitnessBrowser__pseudo5_N2C3_1:AO356_27515
MSEAKLEALHFADAPRINSTIPGPRTTEALALSARTESMARGGGRMPVAMDRAFGATFKD
ADDNTYIDLSAGVGVSSVGRCHPKVVQAIREQSEVLMHALEVNSTRRTELAAKLSEIAPD
GLRGDCITFFTQSGSDALEAAIKFAKRVTGRHQIIAFHGGYHGVWNASGALTTGTAYRKG
YGAQMGGVIHAPYPYAYRFPFDTTHKSAEQIAGEYVDYLLNTPYTAADDVAAVIVEPVQG
EGGYVPPSPEFLQLLRKACDRSGTLLIVDEVQSGAGRTGKMWAVEHSGVKPDMLTFGKGI
GSDLPMAGLIMRSDLAAAIPDGSMPNTFAANSLSAAVALTNISILQDPELDLLNRAHTLG
LEAQERIRGFGSPLVGEVRGRGLMIGIELVSDPTTKAPLAPEKIGQLMGYLLSHGVLMIP
CGRYSNVMRVMPSLTISRALFFKALDIFGDALDALDA
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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