SitesBLAST
Comparing WP_050997458.1 NCBI__GCF_000058485.1:WP_050997458.1 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)
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
69% identity, 96% coverage: 14:454/458 of query aligns to 2:438/439 of 3q8nC
- active site: V32 (= V44), Y151 (= Y163), E221 (= E236), D254 (= D269), Q257 (= Q272), K283 (= K298), T312 (= T327), R412 (= R428)
- binding 4-oxobutanoic acid: G124 (= G136), A125 (= A137), V256 (≠ I271), K283 (= K298)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
64% identity, 95% coverage: 14:447/458 of query aligns to 5:437/444 of 4atqF
- active site: V35 (= V44), Y154 (= Y163), E226 (= E236), D259 (= D269), Q262 (= Q272), K288 (= K298), T317 (= T327), R418 (= R428)
- binding gamma-amino-butanoic acid: M95 (= M104), Y154 (= Y163), R157 (= R166), E231 (= E241), K288 (= K298), G316 (= G326)
- binding pyridoxal-5'-phosphate: G127 (= G136), A128 (= A137), Y154 (= Y163), H155 (= H164), D259 (= D269), V261 (≠ I271)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
57% identity, 97% coverage: 14:456/458 of query aligns to 5:440/440 of 6j2vA
- active site: L35 (≠ V44), Y154 (= Y163), D256 (= D269), K285 (= K298)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G136), A128 (= A137), Y154 (= Y163), H155 (= H164), R157 (= R166), E223 (= E236), E228 (= E241), D256 (= D269), I258 (= I271), K285 (= K298), G313 (= G326), T314 (= T327)
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, 93% coverage: 29:453/458 of query aligns to 4:423/426 of P22256
- I50 (= I75) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 136:137) binding pyridoxal 5'-phosphate
- E211 (= E241) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I271) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q272) binding pyridoxal 5'-phosphate
- K268 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T327) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
45% identity, 93% coverage: 29:453/458 of query aligns to 3:422/425 of 1sffA
- active site: V18 (= V44), Y137 (= Y163), E205 (= E236), D238 (= D269), Q241 (= Q272), K267 (= K298), T296 (= T327), R397 (= R428)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ M104), G110 (= G136), S111 (≠ A137), Y137 (= Y163), H138 (= H164), R140 (= R166), E205 (= E236), D238 (= D269), V240 (≠ I271), Q241 (= Q272), K267 (= K298), T296 (= T327)
- binding sulfate ion: N152 (≠ A178), Y393 (≠ G424)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
45% identity, 93% coverage: 29:453/458 of query aligns to 3:422/425 of 1sf2A
- active site: V18 (= V44), Y137 (= Y163), E205 (= E236), D238 (= D269), Q241 (= Q272), K267 (= K298), T296 (= T327), R397 (= R428)
- binding pyridoxal-5'-phosphate: G110 (= G136), S111 (≠ A137), Y137 (= Y163), H138 (= H164), E205 (= E236), D238 (= D269), V240 (≠ I271), Q241 (= Q272), K267 (= K298)
- binding sulfate ion: N152 (≠ A178), Y393 (≠ G424)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
45% identity, 93% coverage: 29:453/458 of query aligns to 3:422/425 of 1szkA
- active site: V18 (= V44), Y137 (= Y163), E205 (= E236), D238 (= D269), Q241 (= Q272), K267 (= K298), T296 (= T327), R397 (= R428)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G136), S111 (≠ A137), Y137 (= Y163), H138 (= H164), E205 (= E236), D238 (= D269), V240 (≠ I271), 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)
43% identity, 91% coverage: 35:453/458 of query aligns to 9:421/421 of P50457
- K267 (= K298) mutation to A: No GABA-AT activity.
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, 96% coverage: 19:458/458 of query aligns to 22:465/474 of O58478
- D251 (≠ E241) mutation to A: Loss of activity.
- K308 (= K298) mutation to A: Loss of activity.
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)
35% identity, 96% coverage: 16:455/458 of query aligns to 2:446/454 of O50131
- T92 (≠ C102) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ F103) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G136) binding pyridoxal 5'-phosphate
- T125 (≠ A137) binding pyridoxal 5'-phosphate
- Q267 (= Q272) binding pyridoxal 5'-phosphate
- K293 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T327) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
35% identity, 95% coverage: 21:455/458 of query aligns to 5:444/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I75), S121 (= S135), G122 (= G136), T123 (≠ A137), F149 (≠ Y163), H150 (= H164), R152 (= R166), E234 (= E241), D262 (= D269), V264 (≠ I271), Q265 (= Q272), K291 (= K298), N318 (≠ G326), T319 (= T327), R417 (= R428)
7vntA Structure of aminotransferase-substrate complex (see paper)
35% identity, 95% coverage: 21:455/458 of query aligns to 5:444/452 of 7vntA
- binding L-ornithine: F149 (≠ Y163), R152 (= R166), E234 (= E241), K291 (= K298)
- binding pyridoxal-5'-phosphate: G122 (= G136), T123 (≠ A137), F149 (≠ Y163), H150 (= H164), E229 (= E236), D262 (= D269), V264 (≠ I271), Q265 (= Q272), K291 (= K298)
7vnoA Structure of aminotransferase (see paper)
35% identity, 95% coverage: 21:455/458 of query aligns to 5:444/452 of 7vnoA
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
33% identity, 88% coverage: 52:454/458 of query aligns to 38:441/448 of 4ysnC
- active site: Y149 (= Y163), E224 (= E236), D257 (= D269), N260 (≠ Q272), K287 (= K298), T316 (= T327), R415 (= R428)
- binding pyridoxal-5'-phosphate: S121 (= S135), G122 (= G136), S123 (≠ A137), Y149 (= Y163), H150 (= H164), E224 (= E236), D257 (= D269), V259 (≠ I271), K287 (= K298), F315 (≠ G326), T316 (= T327)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
33% identity, 88% coverage: 52:454/458 of query aligns to 31:434/446 of 5wyfA
- active site: Y142 (= Y163), E217 (= E236), D250 (= D269), N253 (≠ Q272), K280 (= K298), T309 (= T327), R408 (= R428)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I75), Y84 (≠ I105), G115 (= G136), S116 (≠ A137), Y142 (= Y163), H143 (= H164), D222 (≠ E241), D250 (= D269), V252 (≠ I271), N253 (≠ Q272), K280 (= K298), F308 (≠ G326), T309 (= T327), R408 (= R428)
Sites not aligning to the query:
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
33% identity, 88% coverage: 52:454/458 of query aligns to 29:432/439 of 5wyaA
- active site: Y140 (= Y163), E215 (= E236), D248 (= D269), N251 (≠ Q272), K278 (= K298), T307 (= T327), R406 (= R428)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I75), Y82 (≠ I105), S112 (= S135), G113 (= G136), S114 (≠ A137), Y140 (= Y163), H141 (= H164), E215 (= E236), D248 (= D269), V250 (≠ I271), N251 (≠ Q272), K278 (= K298), F306 (≠ G326), T307 (= T327), R406 (= R428)
Sites not aligning to the query:
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
34% identity, 89% coverage: 46:454/458 of query aligns to 22:412/412 of 2eo5A
- active site: F139 (≠ Y163), E219 (= E236), D252 (= D269), Q255 (= Q272), K281 (= K298), T303 (= T327), R386 (= R428)
- binding pyridoxal-5'-phosphate: G113 (= G136), T114 (≠ A137), F139 (≠ Y163), H140 (= H164), E219 (= E236), D252 (= D269), V254 (≠ I271), Q255 (= Q272), K281 (= K298)
Sites not aligning to the query:
8cplC Yzw2 a scaffold for cryo-em of small proteins of interest
35% identity, 84% coverage: 50:435/458 of query aligns to 58:425/499 of 8cplC
P42588 Putrescine aminotransferase; PAT; PATase; Cadaverine transaminase; Diamine transaminase; Putrescine transaminase; Putrescine--2-oxoglutaric acid transaminase; Putrescine:2-OG aminotransferase; EC 2.6.1.82; EC 2.6.1.29 from Escherichia coli (strain K12) (see paper)
35% identity, 84% coverage: 50:435/458 of query aligns to 66:433/459 of P42588
- GT 150:151 (≠ GA 136:137) binding in other chain
- Q274 (= Q272) binding in other chain
- K300 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T332 (= T327) binding pyridoxal 5'-phosphate
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
37% identity, 85% coverage: 47:435/458 of query aligns to 16:373/390 of 8ht4B
Query Sequence
>WP_050997458.1 NCBI__GCF_000058485.1:WP_050997458.1
MNPPNVPARGGPGLPQIRRLVTEIPGPRSRALAARRAGAVARGVGETLPVYVHAAGGGVV
VDVDGNSLIDFGSGIAVVSVGNAADGVVAAVREQVGRFTHTCFMITPYEGYVAVCEALNR
LTPGDHDKRSALFNSGAEAVENAVKIARSATGRAAIVVFEHAYHGRTNLTLAMTAKSAPY
KAGFGPFAPEVYRVPLAYPYRWPTGREHCGEQAAARVIELVRDEIGAGEVAALVIEPIQG
EGGFIVPGRGFLPRLAEFCADAGILFVADEIQTGFARTGTMFACEDEGVVPDLITTAKGI
AGGMPLAAVTGRAEIMDAPQVGGLGGTYGGNPAACAAALAAIGFIESADLAARARRIGEL
ALPRLRALAARYDVIGDVRGRGAMLALELVRGGGDTRPDRELTGAVAAACHRRGLIVLTA
GTWGNVLRLLPPLVMDPALLLAGLDVLDEAFAEVTAAR
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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