SitesBLAST
Comparing WP_028949958.1 NCBI__GCF_000619805.1:WP_028949958.1 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)
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)
32% identity, 99% coverage: 4:457/457 of query aligns to 33:462/474 of O58478
- D251 (≠ T228) mutation to A: Loss of activity.
- K308 (= K285) mutation to A: Loss of activity.
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
30% identity, 98% coverage: 4:449/457 of query aligns to 4:420/425 of 1szkA
- active site: V18 (= V20), Y137 (= Y141), E205 (= E223), D238 (= D256), Q241 (= Q259), K267 (= K285), T296 (= T317), R397 (≠ T426)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G114), S111 (= S115), Y137 (= Y141), H138 (= H142), E205 (= E223), D238 (= D256), V240 (≠ I258), Q241 (= Q259), K267 (= K285)
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)
30% identity, 98% coverage: 4:449/457 of query aligns to 5:421/426 of P22256
- I50 (≠ Y52) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (= GS 114:115) binding
- E211 (≠ T228) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I258) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q259) binding
- K268 (= K285) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T317) binding
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
30% identity, 98% coverage: 4:449/457 of query aligns to 4:420/425 of 1sffA
- active site: V18 (= V20), Y137 (= Y141), E205 (= E223), D238 (= D256), Q241 (= Q259), K267 (= K285), T296 (= T317), R397 (≠ T426)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q81), G110 (= G114), S111 (= S115), Y137 (= Y141), H138 (= H142), R140 (= R144), E205 (= E223), D238 (= D256), V240 (≠ I258), Q241 (= Q259), K267 (= K285), T296 (= T317)
- binding sulfate ion: N152 (≠ R156), Y393 (≠ K422)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
30% identity, 98% coverage: 4:449/457 of query aligns to 4:420/425 of 1sf2A
- active site: V18 (= V20), Y137 (= Y141), E205 (= E223), D238 (= D256), Q241 (= Q259), K267 (= K285), T296 (= T317), R397 (≠ T426)
- binding pyridoxal-5'-phosphate: G110 (= G114), S111 (= S115), Y137 (= Y141), H138 (= H142), E205 (= E223), D238 (= D256), V240 (≠ I258), Q241 (= Q259), K267 (= K285)
- binding sulfate ion: N152 (≠ R156), Y393 (≠ K422)
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)
31% identity, 92% coverage: 28:446/457 of query aligns to 39:439/454 of O50131
- T92 (≠ S80) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ Q81) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G114) binding
- T125 (≠ S115) binding
- Q267 (= Q259) binding
- K293 (= K285) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T317) binding
7vo1A Structure of aminotransferase-substrate complex (see paper)
31% identity, 92% coverage: 28:446/457 of query aligns to 37:437/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ Y52), S121 (≠ G113), G122 (= G114), T123 (≠ S115), F149 (≠ Y141), H150 (= H142), R152 (= R144), E234 (≠ T228), D262 (= D256), V264 (≠ I258), Q265 (= Q259), K291 (= K285), N318 (vs. gap), T319 (= T317), R417 (≠ T426)
7vntA Structure of aminotransferase-substrate complex (see paper)
31% identity, 92% coverage: 28:446/457 of query aligns to 37:437/452 of 7vntA
- binding L-ornithine: F149 (≠ Y141), R152 (= R144), E234 (≠ T228), K291 (= K285)
- binding pyridoxal-5'-phosphate: G122 (= G114), T123 (≠ S115), F149 (≠ Y141), H150 (= H142), E229 (= E223), D262 (= D256), V264 (≠ I258), Q265 (= Q259), K291 (= K285)
7vnoA Structure of aminotransferase (see paper)
31% identity, 92% coverage: 28:446/457 of query aligns to 37:437/452 of 7vnoA
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
31% identity, 92% coverage: 26:445/457 of query aligns to 25:405/412 of 2eo5A
- active site: F139 (≠ Y141), E219 (= E223), D252 (= D256), Q255 (= Q259), K281 (= K285), T303 (= T317), R386 (≠ T426)
- binding pyridoxal-5'-phosphate: G113 (= G114), T114 (≠ S115), F139 (≠ Y141), H140 (= H142), E219 (= E223), D252 (= D256), V254 (≠ I258), Q255 (= Q259), K281 (= K285)
Sites not aligning to the query:
6s54A Transaminase from pseudomonas fluorescens (see paper)
28% identity, 95% coverage: 18:449/457 of query aligns to 12:448/453 of 6s54A
- active site: M20 (vs. gap), Y152 (= Y141), D258 (= D256), K287 (= K285)
- binding pyridoxal-5'-phosphate: G119 (= G114), S120 (= S115), Y152 (= Y141), H153 (= H142), G154 (= G143), E225 (= E223), D258 (= D256), V260 (≠ I258), I261 (≠ Q259), K287 (= K285)
5lh9D Amine transaminase crystal structure from an uncultivated pseudomonas species in the plp-bound (internal aldimine) form
26% identity, 93% coverage: 28:451/457 of query aligns to 29:447/449 of 5lh9D
- active site: Y148 (= Y141), D255 (= D256), K284 (= K285), T321 (= T317)
- binding pyridoxal-5'-phosphate: G115 (= G114), S116 (= S115), Y148 (= Y141), H149 (= H142), G150 (= G143), E222 (= E223), D255 (= D256), V257 (≠ I258), K284 (= K285)
5lhaA Amine transaminase crystal structure from an uncultivated pseudomonas species in the pmp-bound form
26% identity, 93% coverage: 28:451/457 of query aligns to 27:445/447 of 5lhaA
- active site: Y146 (= Y141), D253 (= D256), K282 (= K285), T319 (= T317)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G113 (= G114), S114 (= S115), Y146 (= Y141), H147 (= H142), G148 (= G143), E220 (= E223), D253 (= D256), K282 (= K285), Y318 (vs. gap), T319 (= T317)
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)
28% identity, 92% coverage: 29:450/457 of query aligns to 25:420/421 of P50457
- K267 (= K285) mutation to A: No GABA-AT activity.
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum
29% identity, 93% coverage: 22:445/457 of query aligns to 14:385/390 of 8ht4B
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
28% identity, 99% coverage: 5:457/457 of query aligns to 7:437/439 of 5wyaA
- active site: A20 (≠ D18), Y140 (= Y141), E215 (= E223), D248 (= D256), N251 (≠ Q259), K278 (= K285), T307 (≠ S316), R406 (≠ T426)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ Y52), Y82 (≠ F82), S112 (≠ G113), G113 (= G114), S114 (= S115), Y140 (= Y141), H141 (= H142), E215 (= E223), D248 (= D256), V250 (≠ I258), N251 (≠ Q259), K278 (= K285), F306 (≠ H315), T307 (≠ S316), R406 (≠ T426)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
28% identity, 99% coverage: 5:457/457 of query aligns to 16:446/448 of 4ysnC
- active site: A29 (≠ D18), Y149 (= Y141), E224 (= E223), D257 (= D256), N260 (≠ Q259), K287 (= K285), T316 (≠ S316), R415 (≠ T426)
- binding pyridoxal-5'-phosphate: S121 (≠ G113), G122 (= G114), S123 (= S115), Y149 (= Y141), H150 (= H142), E224 (= E223), D257 (= D256), V259 (≠ I258), K287 (= K285), F315 (≠ H315), T316 (≠ S316)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
28% identity, 99% coverage: 5:457/457 of query aligns to 9:439/446 of 5wyfA
- active site: A22 (≠ D18), Y142 (= Y141), E217 (= E223), D250 (= D256), N253 (≠ Q259), K280 (= K285), T309 (≠ S316), R408 (≠ T426)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ Y52), Y84 (≠ F82), G115 (= G114), S116 (= S115), Y142 (= Y141), H143 (= H142), D222 (≠ T228), D250 (= D256), V252 (≠ I258), N253 (≠ Q259), K280 (= K285), F308 (≠ H315), T309 (≠ S316), R408 (≠ T426)
5kr6B Directed evolution of transaminases by ancestral reconstruction. Using old proteins for new chemistries
28% identity, 95% coverage: 25:457/457 of query aligns to 33:460/460 of 5kr6B
6io1B Crystal structure of a novel thermostable (s)-enantioselective omega- transaminase from thermomicrobium roseum (see paper)
26% identity, 95% coverage: 18:452/457 of query aligns to 12:446/448 of 6io1B
- active site: L20 (vs. gap), Y151 (= Y141), D257 (= D256), K286 (= K285)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G117 (= G113), G118 (= G114), A119 (≠ S115), N122 (≠ I118), Y151 (= Y141), H152 (= H142), D257 (= D256), V259 (≠ I258), I260 (≠ Q259), K286 (= K285)
Query Sequence
>WP_028949958.1 NCBI__GCF_000619805.1:WP_028949958.1
MEEKELLQLESEYCSFGDTVHYLNPPKIFAKSEGSYLYDLEGKQYLDLQMWYSACNFGYN
NKRINDGIKNQMDTLGQLASQFLTKEKILLSYKIAKSVEDRFKVKGRVHFNVGGSQAIED
SLKIVRNYTKKNLNFAFMGGYHGRTIGATNITSSYRYRERYGHFSDRAFFIPFPYCFRCP
YGKDKETCDLYCAKEFEKLFESEYYTVCNPKTKNCEFGAFYIEPIQGTGGYIIPPKDYFK
KIKPVLDEYKVLLVSDEIQMGFYRTGKLWSIEHFGVVPDIIVFGKSLTNGMNPLSGLWAK
EELINPEIFPPGSTHSTFSSNPIGVRAGLEVFKIIEEKDYEKIVKEKGEKFLNYLKDLKK
KYPFIGDVDGLGLALRVEICEKDGYTPSKKLTDKIVEEGLKANLNLNEKTYGLVLDVGGY
YKNVLTLAPSLDITDEEINLAVEFLDIQFSRIAKDEL
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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