SitesBLAST
Comparing PP_0214 FitnessBrowser__Putida:PP_0214 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)
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
73% identity, 99% coverage: 3:423/425 of query aligns to 1:422/425 of 1sffA
- active site: V18 (= V20), Y137 (= Y139), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R398)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q80), G110 (= G112), S111 (= S113), Y137 (= Y139), H138 (= H140), R140 (= R142), E205 (= E207), D238 (= D240), V240 (= V242), Q241 (= Q243), K267 (= K269), T296 (= T298)
- binding sulfate ion: N152 (≠ V154), Y393 (≠ G394)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
73% identity, 99% coverage: 3:423/425 of query aligns to 1:422/425 of 1sf2A
- active site: V18 (= V20), Y137 (= Y139), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R398)
- binding pyridoxal-5'-phosphate: G110 (= G112), S111 (= S113), Y137 (= Y139), H138 (= H140), E205 (= E207), D238 (= D240), V240 (= V242), Q241 (= Q243), K267 (= K269)
- binding sulfate ion: N152 (≠ V154), Y393 (≠ G394)
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)
73% identity, 99% coverage: 3:423/425 of query aligns to 2:423/426 of P22256
- I50 (= I51) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (= GS 112:113) binding
- E211 (= E212) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V242) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q243) binding
- K268 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T298) binding
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
73% identity, 99% coverage: 3:423/425 of query aligns to 1:422/425 of 1szkA
- active site: V18 (= V20), Y137 (= Y139), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R398)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G112), S111 (= S113), Y137 (= Y139), H138 (= H140), E205 (= E207), D238 (= D240), V240 (= V242), Q241 (= Q243), K267 (= K269)
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)
55% identity, 99% coverage: 4:423/425 of query aligns to 2:421/421 of P50457
- K267 (= K269) mutation to A: No GABA-AT activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
46% identity, 99% coverage: 5:424/425 of query aligns to 17:438/439 of 3q8nC
- active site: V32 (= V20), Y151 (= Y139), E221 (= E207), D254 (= D240), Q257 (= Q243), K283 (= K269), T312 (= T298), R412 (= R398)
- binding 4-oxobutanoic acid: G124 (= G112), A125 (≠ S113), V256 (= V242), K283 (= K269)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
44% identity, 97% coverage: 5:417/425 of query aligns to 20:437/444 of 4atqF
- active site: V35 (= V20), Y154 (= Y139), E226 (= E207), D259 (= D240), Q262 (= Q243), K288 (= K269), T317 (= T298), R418 (= R398)
- binding gamma-amino-butanoic acid: M95 (≠ Q80), Y154 (= Y139), R157 (= R142), E231 (= E212), K288 (= K269), G316 (= G297)
- binding pyridoxal-5'-phosphate: G127 (= G112), A128 (≠ S113), Y154 (= Y139), H155 (= H140), D259 (= D240), V261 (= V242)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
43% identity, 97% coverage: 5:417/425 of query aligns to 20:431/440 of 6j2vA
- active site: L35 (≠ V20), Y154 (= Y139), D256 (= D240), K285 (= K269)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G112), A128 (≠ S113), Y154 (= Y139), H155 (= H140), R157 (= R142), E223 (= E207), E228 (= E212), D256 (= D240), I258 (≠ V242), K285 (= K269), G313 (= G297), T314 (= T298)
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: 6:423/425 of query aligns to 33:460/474 of O58478
- D251 (≠ E212) mutation to A: Loss of activity.
- K308 (= K269) 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)
38% identity, 93% coverage: 26:420/425 of query aligns to 38:441/454 of O50131
- T92 (≠ V81) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ L82) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G112) binding
- T125 (≠ S113) binding
- Q267 (= Q243) binding
- K293 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T298) binding
7vo1A Structure of aminotransferase-substrate complex (see paper)
38% identity, 93% coverage: 26:420/425 of query aligns to 36:439/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I51), S121 (≠ T111), G122 (= G112), T123 (≠ S113), F149 (≠ Y139), H150 (= H140), R152 (= R142), E234 (= E212), D262 (= D240), V264 (= V242), Q265 (= Q243), K291 (= K269), N318 (≠ G297), T319 (= T298), R417 (= R398)
7vntA Structure of aminotransferase-substrate complex (see paper)
38% identity, 93% coverage: 26:420/425 of query aligns to 36:439/452 of 7vntA
- binding L-ornithine: F149 (≠ Y139), R152 (= R142), E234 (= E212), K291 (= K269)
- binding pyridoxal-5'-phosphate: G122 (= G112), T123 (≠ S113), F149 (≠ Y139), H150 (= H140), E229 (= E207), D262 (= D240), V264 (= V242), Q265 (= Q243), K291 (= K269)
7vnoA Structure of aminotransferase (see paper)
38% identity, 93% coverage: 26:420/425 of query aligns to 36:439/452 of 7vnoA
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
33% identity, 94% coverage: 26:424/425 of query aligns to 27:432/439 of 5wyaA
- active site: Y140 (= Y139), E215 (= E207), D248 (= D240), N251 (≠ Q243), K278 (= K269), T307 (≠ G297), R406 (= R398)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I51), Y82 (≠ V81), S112 (≠ T111), G113 (= G112), S114 (= S113), Y140 (= Y139), H141 (= H140), E215 (= E207), D248 (= D240), V250 (= V242), N251 (≠ Q243), K278 (= K269), F306 (≠ G296), T307 (≠ G297), R406 (= R398)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
33% identity, 94% coverage: 26:424/425 of query aligns to 29:434/446 of 5wyfA
- active site: Y142 (= Y139), E217 (= E207), D250 (= D240), N253 (≠ Q243), K280 (= K269), T309 (≠ G297), R408 (= R398)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I51), Y84 (≠ V81), G115 (= G112), S116 (= S113), Y142 (= Y139), H143 (= H140), D222 (≠ E212), D250 (= D240), V252 (= V242), N253 (≠ Q243), K280 (= K269), F308 (≠ G296), T309 (≠ G297), R408 (= R398)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
33% identity, 94% coverage: 26:424/425 of query aligns to 36:441/448 of 4ysnC
- active site: Y149 (= Y139), E224 (= E207), D257 (= D240), N260 (≠ Q243), K287 (= K269), T316 (≠ G297), R415 (= R398)
- binding pyridoxal-5'-phosphate: S121 (≠ T111), G122 (= G112), S123 (= S113), Y149 (= Y139), H150 (= H140), E224 (= E207), D257 (= D240), V259 (= V242), K287 (= K269), F315 (≠ G296), T316 (≠ G297)
Sites not aligning to the query:
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
34% identity, 89% coverage: 32:411/425 of query aligns to 18:372/385 of Q9X2A5
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
34% identity, 89% coverage: 32:411/425 of query aligns to 26:380/393 of 2ordA
- active site: F134 (≠ Y139), E186 (= E207), D219 (= D240), Q222 (= Q243), K248 (= K269), T276 (= T298), R367 (= R398)
- binding pyridoxal-5'-phosphate: G102 (= G112), T103 (≠ S113), F134 (≠ Y139), H135 (= H140), E186 (= E207), D219 (= D240), V221 (= V242), Q222 (= Q243), K248 (= K269)
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
34% identity, 90% coverage: 32:414/425 of query aligns to 27:388/402 of 4jevB
- active site: F136 (≠ Y139), E188 (= E207), D221 (= D240), Q224 (= Q243), K250 (= K269), T279 (= T298), R372 (= R398)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I51), S102 (≠ T111), G103 (= G112), T104 (≠ S113), F136 (≠ Y139), H137 (= H140), E188 (= E207), E193 (= E212), D221 (= D240), V223 (= V242), Q224 (= Q243), K250 (= K269), R372 (= R398)
P40732 Acetylornithine/succinyldiaminopimelate aminotransferase; ACOAT; DapATase; Succinyldiaminopimelate transferase; EC 2.6.1.11; EC 2.6.1.17 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
34% identity, 90% coverage: 32:414/425 of query aligns to 32:393/405 of P40732
- GT 108:109 (≠ GS 112:113) binding
- K255 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T298) binding
Query Sequence
>PP_0214 FitnessBrowser__Putida:PP_0214
MSKTNESLMQRRVAAVPRGVGQIHPIFVDTAKNSTVIDVEGRELIDFAGGIAVLNTGHLH
PKVVAAVQEQLTKVSHTCFQVLAYEPYVELCEKINKLVPGDFDKKTLLVTTGSEAVENAV
KIARAATGRAGVIAFTGGYHGRTMMTLGLTGKVVPYSAGMGLMPGGIFRALFPSELHGIS
VDDAIASVERIFKNDAEPRDIAAIILEPVQGEGGFLPAPKELMKRLRALCDQHGILLIAD
EVQTGAGRTGTFFAMEQMGVAPDLTTFAKSIAGGFPLAGVCGKAEYMDAIAPGGLGGTYA
GSPIACAAALAVIEVFEEEKLLDRSKAVGERLTAGLREIQKKYPIIGDVRGLGSMIAVEV
FEKGTHTPNAAAVGQVVAKAREKGLILLSCGTYGNVLRILVPLTAEDALLDKGLAIIEEC
FAEIA
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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