SitesBLAST
Comparing HSERO_RS19685 FitnessBrowser__HerbieS:HSERO_RS19685 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)
7vo1A Structure of aminotransferase-substrate complex (see paper)
36% identity, 94% coverage: 23:449/456 of query aligns to 9:436/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ V74), S121 (≠ G134), G122 (= G135), T123 (≠ S136), F149 (≠ Y162), H150 (= H163), R152 (≠ I165), E234 (= E242), D262 (= D270), V264 (= V272), Q265 (= Q273), K291 (= K299), N318 (= N327), T319 (= T328), R417 (= R430)
7vntA Structure of aminotransferase-substrate complex (see paper)
36% identity, 94% coverage: 23:449/456 of query aligns to 9:436/452 of 7vntA
- binding L-ornithine: F149 (≠ Y162), R152 (≠ I165), E234 (= E242), K291 (= K299)
- binding pyridoxal-5'-phosphate: G122 (= G135), T123 (≠ S136), F149 (≠ Y162), H150 (= H163), E229 (= E237), D262 (= D270), V264 (= V272), Q265 (= Q273), K291 (= K299)
7vnoA Structure of aminotransferase (see paper)
36% identity, 94% coverage: 23:449/456 of query aligns to 9:436/452 of 7vnoA
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, 94% coverage: 23:449/456 of query aligns to 11:438/454 of O50131
- T92 (≠ M101) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ E102) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G135) binding
- T125 (≠ S136) binding
- Q267 (= Q273) binding
- K293 (= K299) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T328) binding
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
35% identity, 98% coverage: 10:456/456 of query aligns to 1:438/439 of 3q8nC
- active site: V32 (≠ G44), Y151 (= Y162), E221 (= E237), D254 (= D270), Q257 (= Q273), K283 (= K299), T312 (= T328), R412 (= R430)
- binding 4-oxobutanoic acid: G124 (= G135), A125 (≠ S136), V256 (= V272), K283 (= K299)
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, 96% coverage: 13:448/456 of query aligns to 19:453/474 of O58478
- D251 (≠ E242) mutation to A: Loss of activity.
- K308 (= K299) mutation to A: Loss of activity.
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
35% identity, 91% coverage: 33:449/456 of query aligns to 7:416/425 of 1sffA
- active site: V18 (≠ G44), Y137 (= Y162), E205 (= E237), D238 (= D270), Q241 (= Q273), K267 (= K299), T296 (= T328), R397 (= R430)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ V103), G110 (= G135), S111 (= S136), Y137 (= Y162), H138 (= H163), R140 (≠ I165), E205 (= E237), D238 (= D270), V240 (= V272), Q241 (= Q273), K267 (= K299), T296 (= T328)
- binding sulfate ion: N152 (≠ A177), Y393 (≠ T426)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
35% identity, 91% coverage: 33:449/456 of query aligns to 7:416/425 of 1sf2A
- active site: V18 (≠ G44), Y137 (= Y162), E205 (= E237), D238 (= D270), Q241 (= Q273), K267 (= K299), T296 (= T328), R397 (= R430)
- binding pyridoxal-5'-phosphate: G110 (= G135), S111 (= S136), Y137 (= Y162), H138 (= H163), E205 (= E237), D238 (= D270), V240 (= V272), Q241 (= Q273), K267 (= K299)
- binding sulfate ion: N152 (≠ A177), Y393 (≠ T426)
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, 91% coverage: 33:449/456 of query aligns to 8:417/426 of P22256
- I50 (≠ V74) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (= GS 135:136) binding
- E211 (= E242) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V272) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q273) binding
- K268 (= K299) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T328) binding
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
35% identity, 91% coverage: 33:449/456 of query aligns to 7:416/425 of 1szkA
- active site: V18 (≠ G44), Y137 (= Y162), E205 (= E237), D238 (= D270), Q241 (= Q273), K267 (= K299), T296 (= T328), R397 (= R430)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G135), S111 (= S136), Y137 (= Y162), H138 (= H163), E205 (= E237), D238 (= D270), V240 (= V272), Q241 (= Q273), K267 (= K299)
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
32% identity, 88% coverage: 49:449/456 of query aligns to 27:425/439 of 5wyaA
- active site: Y140 (= Y162), E215 (= E237), D248 (= D270), N251 (≠ Q273), K278 (= K299), T307 (= T328), R406 (= R430)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ V74), Y82 (vs. gap), S112 (≠ G134), G113 (= G135), S114 (= S136), Y140 (= Y162), H141 (= H163), E215 (= E237), D248 (= D270), V250 (= V272), N251 (≠ Q273), K278 (= K299), F306 (≠ N327), T307 (= T328), R406 (= R430)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
32% identity, 88% coverage: 49:449/456 of query aligns to 36:434/448 of 4ysnC
- active site: Y149 (= Y162), E224 (= E237), D257 (= D270), N260 (≠ Q273), K287 (= K299), T316 (= T328), R415 (= R430)
- binding pyridoxal-5'-phosphate: S121 (≠ G134), G122 (= G135), S123 (= S136), Y149 (= Y162), H150 (= H163), E224 (= E237), D257 (= D270), V259 (= V272), K287 (= K299), F315 (≠ N327), T316 (= T328)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
32% identity, 88% coverage: 49:449/456 of query aligns to 29:427/446 of 5wyfA
- active site: Y142 (= Y162), E217 (= E237), D250 (= D270), N253 (≠ Q273), K280 (= K299), T309 (= T328), R408 (= R430)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ V74), Y84 (vs. gap), G115 (= G135), S116 (= S136), Y142 (= Y162), H143 (= H163), D222 (≠ E242), D250 (= D270), V252 (= V272), N253 (≠ Q273), K280 (= K299), F308 (≠ N327), T309 (= T328), R408 (= R430)
Sites not aligning to the query:
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)
35% identity, 92% coverage: 36:454/456 of query aligns to 10:420/421 of P50457
- K267 (= K299) mutation to A: No GABA-AT activity.
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
33% identity, 96% coverage: 16:455/456 of query aligns to 9:443/444 of 4atqF
- active site: V35 (≠ R42), Y154 (= Y162), E226 (= E237), D259 (= D270), Q262 (= Q273), K288 (= K299), T317 (= T328), R418 (= R430)
- binding gamma-amino-butanoic acid: M95 (= M101), Y154 (= Y162), R157 (≠ I165), E231 (= E242), K288 (= K299), G316 (≠ N327)
- binding pyridoxal-5'-phosphate: G127 (= G135), A128 (≠ S136), Y154 (= Y162), H155 (= H163), D259 (= D270), V261 (= V272)
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
33% identity, 88% coverage: 47:449/456 of query aligns to 24:405/412 of 2eo5A
- active site: F139 (≠ Y162), E219 (= E237), D252 (= D270), Q255 (= Q273), K281 (= K299), T303 (= T328), R386 (= R430)
- binding pyridoxal-5'-phosphate: G113 (= G135), T114 (≠ S136), F139 (≠ Y162), H140 (= H163), E219 (= E237), D252 (= D270), V254 (= V272), Q255 (= Q273), K281 (= K299)
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, 88% coverage: 56:454/456 of query aligns to 36:395/395 of Q5SHH5
- GT 113:114 (≠ GS 135:136) binding
- K254 (= K299) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T328) binding
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
35% identity, 88% coverage: 56:454/456 of query aligns to 28:387/387 of 1wkhA
- active site: F132 (≠ Y162), E184 (= E237), D217 (= D270), Q220 (= Q273), K246 (= K299), T275 (= T328), R363 (= R430)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ V74), S104 (≠ G134), G105 (= G135), T106 (≠ S136), F132 (≠ Y162), S133 (≠ H163), E184 (= E237), E189 (= E242), D217 (= D270), I219 (≠ V272), K246 (= K299), R363 (= R430)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
35% identity, 88% coverage: 56:454/456 of query aligns to 28:387/387 of 1wkgA
- active site: F132 (≠ Y162), E184 (= E237), D217 (= D270), Q220 (= Q273), K246 (= K299), T275 (= T328), R363 (= R430)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ V74), G105 (= G135), T106 (≠ S136), F132 (≠ Y162), S133 (≠ H163), R135 (≠ I165), E184 (= E237), D217 (= D270), I219 (≠ V272), Q220 (= Q273), K246 (= K299), G273 (≠ P326), T274 (≠ N327), T275 (= T328)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
35% identity, 88% coverage: 56:454/456 of query aligns to 28:387/387 of 1vefA
- active site: F132 (≠ Y162), D217 (= D270), K246 (= K299), T275 (= T328), R363 (= R430)
- binding pyridoxal-5'-phosphate: G105 (= G135), T106 (≠ S136), F132 (≠ Y162), S133 (≠ H163), E184 (= E237), D217 (= D270), I219 (≠ V272), K246 (= K299)
Sites not aligning to the query:
Query Sequence
>HSERO_RS19685 FitnessBrowser__HerbieS:HSERO_RS19685
MIEAELESLNFTDAPKMVTPTYPGPKTAAALELSARTESMARGGGRMPIAMDQAFGVTFK
DPDGNTFIDLSAGVGVSSVGRCNPRVVEAIRKQSESLMHSMEVNSSKRTELAAKISEIMP
DGLRGDCITFFTQGGSDALEAAVKFAKRVTGRHQIIAFHGGYHGIWNASNALTTGTAYRK
GFGPFMGGVIHAPYPYAYRFPFDTSHKSAEQIAGEYVDYLLNTPYTAADDVAAVIVEPVQ
GEGGYVPPSPEFLQILRKACDRSGALLIVDEVQAGAGRTGKMWAVEHSGVKPDMLTFGKG
IGGDMPMAGLVMRSDLAAKIPDGSQPNTFAANSISAAVALTNISILQDPRLDLVNRAHTL
GLEAQERIRSFNSPWVGEVRGRGLMIGIELVENRETREPLSREKLGKLMDYVVGHGVLMI
PCGRYTNVMRVMPSLTIPRSLMFKGLDIFGAGLASL
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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