SitesBLAST
Comparing WP_012102402.1 NCBI__GCF_000016505.1:WP_012102402.1 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)
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)
39% identity, 95% coverage: 19:422/426 of query aligns to 23:421/421 of P50457
- K267 (= K269) mutation to A: No GABA-AT activity.
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)
38% identity, 98% coverage: 4:422/426 of query aligns to 9:423/426 of P22256
- I50 (= I45) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 105:106) binding pyridoxal 5'-phosphate
- E211 (= E212) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I242) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q243) binding pyridoxal 5'-phosphate
- K268 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T298) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
38% identity, 98% coverage: 4:422/426 of query aligns to 8:422/425 of 1sffA
- active site: V18 (≠ L14), Y137 (≠ F132), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R397)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ N74), G110 (= G105), S111 (≠ A106), Y137 (≠ F132), H138 (= H133), R140 (= R135), E205 (= E207), D238 (= D240), V240 (≠ I242), Q241 (= Q243), K267 (= K269), T296 (= T298)
- binding sulfate ion: N152 (≠ S147), Y393 (≠ G393)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
38% identity, 98% coverage: 4:422/426 of query aligns to 8:422/425 of 1sf2A
- active site: V18 (≠ L14), Y137 (≠ F132), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R397)
- binding pyridoxal-5'-phosphate: G110 (= G105), S111 (≠ A106), Y137 (≠ F132), H138 (= H133), E205 (= E207), D238 (= D240), V240 (≠ I242), Q241 (= Q243), K267 (= K269)
- binding sulfate ion: N152 (≠ S147), Y393 (≠ G393)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
38% identity, 98% coverage: 4:422/426 of query aligns to 8:422/425 of 1szkA
- active site: V18 (≠ L14), Y137 (≠ F132), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R397)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G105), S111 (≠ A106), Y137 (≠ F132), H138 (= H133), E205 (= E207), D238 (= D240), V240 (≠ I242), Q241 (= Q243), K267 (= K269)
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)
39% identity, 98% coverage: 4:420/426 of query aligns to 20:442/454 of O50131
- T92 (≠ N74) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ L75) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G105) binding pyridoxal 5'-phosphate
- T125 (≠ A106) binding pyridoxal 5'-phosphate
- Q267 (= Q243) binding pyridoxal 5'-phosphate
- K293 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T298) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
39% identity, 98% coverage: 4:420/426 of query aligns to 18:440/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I45), S121 (≠ G104), G122 (= G105), T123 (≠ A106), F149 (= F132), H150 (= H133), R152 (= R135), E234 (= E212), D262 (= D240), V264 (≠ I242), Q265 (= Q243), K291 (= K269), N318 (≠ T297), T319 (= T298), R417 (= R397)
7vntA Structure of aminotransferase-substrate complex (see paper)
39% identity, 98% coverage: 4:420/426 of query aligns to 18:440/452 of 7vntA
- binding L-ornithine: F149 (= F132), R152 (= R135), E234 (= E212), K291 (= K269)
- binding pyridoxal-5'-phosphate: G122 (= G105), T123 (≠ A106), F149 (= F132), H150 (= H133), E229 (= E207), D262 (= D240), V264 (≠ I242), Q265 (= Q243), K291 (= K269)
7vnoA Structure of aminotransferase (see paper)
39% identity, 98% coverage: 4:420/426 of query aligns to 18:440/452 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)
35% identity, 98% coverage: 4:420/426 of query aligns to 37:458/474 of O58478
- D251 (≠ E212) mutation to A: Loss of activity.
- K308 (= K269) mutation to A: Loss of activity.
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
41% identity, 93% coverage: 25:420/426 of query aligns to 25:390/393 of 2ordA
- active site: F134 (= F132), E186 (= E207), D219 (= D240), Q222 (= Q243), K248 (= K269), T276 (= T298), R367 (= R397)
- binding pyridoxal-5'-phosphate: G102 (= G105), T103 (≠ A106), F134 (= F132), H135 (= H133), E186 (= E207), D219 (= D240), V221 (≠ I242), Q222 (= Q243), K248 (= K269)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
41% identity, 93% coverage: 25:420/426 of query aligns to 17:382/385 of Q9X2A5
- GT 94:95 (≠ GA 105:106) binding pyridoxal 5'-phosphate
- T268 (= T298) binding pyridoxal 5'-phosphate
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
37% identity, 93% coverage: 27:423/426 of query aligns to 45:438/439 of 3q8nC
Sites not aligning to the query:
Q9M8M7 Acetylornithine aminotransferase, chloroplastic/mitochondrial; ACOAT; Acetylornithine transaminase; AOTA; Protein HOPW1-1-INTERACTING 1; EC 2.6.1.11 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 94% coverage: 20:420/426 of query aligns to 78:453/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
33% identity, 97% coverage: 4:417/426 of query aligns to 13:428/446 of 5wyfA
- active site: A22 (= A13), Y142 (≠ F132), E217 (= E207), D250 (= D240), N253 (≠ Q243), K280 (= K269), T309 (= T298), R408 (= R397)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I45), Y84 (≠ L75), G115 (= G105), S116 (≠ A106), Y142 (≠ F132), H143 (= H133), D222 (≠ E212), D250 (= D240), V252 (≠ I242), N253 (≠ Q243), K280 (= K269), F308 (≠ T297), T309 (= T298), R408 (= R397)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
33% identity, 97% coverage: 4:417/426 of query aligns to 20:435/448 of 4ysnC
- active site: A29 (= A13), Y149 (≠ F132), E224 (= E207), D257 (= D240), N260 (≠ Q243), K287 (= K269), T316 (= T298), R415 (= R397)
- binding pyridoxal-5'-phosphate: S121 (≠ G104), G122 (= G105), S123 (≠ A106), Y149 (≠ F132), H150 (= H133), E224 (= E207), D257 (= D240), V259 (≠ I242), K287 (= K269), F315 (≠ T297), T316 (= T298)
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
33% identity, 97% coverage: 4:417/426 of query aligns to 11:426/439 of 5wyaA
- active site: A20 (= A13), Y140 (≠ F132), E215 (= E207), D248 (= D240), N251 (≠ Q243), K278 (= K269), T307 (= T298), R406 (= R397)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I45), Y82 (≠ L75), S112 (≠ G104), G113 (= G105), S114 (≠ A106), Y140 (≠ F132), H141 (= H133), E215 (= E207), D248 (= D240), V250 (≠ I242), N251 (≠ Q243), K278 (= K269), F306 (≠ T297), T307 (= T298), R406 (= R397)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
35% identity, 96% coverage: 4:413/426 of query aligns to 6:388/400 of 4addA
- active site: F136 (= F132), E188 (= E207), D221 (= D240), Q224 (= Q243), K250 (= K269), T279 (= T298), R372 (= R397)
- binding pyridoxal-5'-phosphate: G103 (= G105), A104 (= A106), F136 (= F132), H137 (= H133), D221 (= D240), V223 (≠ I242), K250 (= K269)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ L14), F136 (= F132), R139 (= R135)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
35% identity, 96% coverage: 4:413/426 of query aligns to 6:388/401 of 4adbB
- active site: F136 (= F132), E188 (= E207), D221 (= D240), Q224 (= Q243), K250 (= K269), T279 (= T298), R372 (= R397)
- binding pyridoxal-5'-phosphate: S102 (≠ G104), G103 (= G105), A104 (= A106), F136 (= F132), H137 (= H133), D221 (= D240), V223 (≠ I242), Q224 (= Q243), K250 (= K269)
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
37% identity, 94% coverage: 20:420/426 of query aligns to 26:409/412 of 2eo5A
- active site: F139 (= F132), E219 (= E207), D252 (= D240), Q255 (= Q243), K281 (= K269), T303 (= T298), R386 (= R397)
- binding pyridoxal-5'-phosphate: G113 (= G105), T114 (≠ A106), F139 (= F132), H140 (= H133), E219 (= E207), D252 (= D240), V254 (≠ I242), Q255 (= Q243), K281 (= K269)
Sites not aligning to the query:
Query Sequence
>WP_012102402.1 NCBI__GCF_000016505.1:WP_012102402.1
MNYENYKQYLSPALAKATDLIMESGKGCYMTDINGDEYLDFVQGIAVNALGHCHPKVVQA
VVEQTKKLMNGSFNLVNFPTTLKLAKRLSEVTPGNLNSIFFSNGGAEAIDGALKLAKAYT
KRPAIIAFKGSFHGRTLGATTITASNSKYRKYYEPMVGSVYFSTYPSKDLCPKGFDEKQR
TEYCLNELDSLFKYVVAPEMVAAIIMEPVQGEGGYVVPTKEFVQGVRDICTKHGILLIFD
EIQSGYGRTGKMFAGENFDVVPDIMTVGKAIAGGLPMSAVISTPEIMDEWHAGMHGTTFG
GNPVCAAAALAVLEEYKNANILENVNNMGAYLRKKLEVLKEKYSCISDIRGLGLMVAIEF
SYGDGTPAGDLFEKVRDKCFKNKLLTLACGVYGNGLRFAAPLNVTEDEIDKGITIIDKVL
GEIWKK
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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