SitesBLAST
Comparing 5210744 FitnessBrowser__PV4:5210744 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)
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
55% identity, 99% coverage: 2:422/426 of query aligns to 2:421/425 of 1sffA
- active site: V18 (≠ Q18), Y137 (≠ F137), E205 (= E205), D238 (= D238), Q241 (= Q241), K267 (= K267), T296 (= T296), R397 (= R398)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ M78), G110 (= G110), S111 (≠ A111), Y137 (≠ F137), H138 (= H138), R140 (= R140), E205 (= E205), D238 (= D238), V240 (≠ I240), Q241 (= Q241), K267 (= K267), T296 (= T296)
- binding sulfate ion: N152 (≠ T152), Y393 (≠ G394)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
55% identity, 99% coverage: 2:422/426 of query aligns to 2:421/425 of 1sf2A
- active site: V18 (≠ Q18), Y137 (≠ F137), E205 (= E205), D238 (= D238), Q241 (= Q241), K267 (= K267), T296 (= T296), R397 (= R398)
- binding pyridoxal-5'-phosphate: G110 (= G110), S111 (≠ A111), Y137 (≠ F137), H138 (= H138), E205 (= E205), D238 (= D238), V240 (≠ I240), Q241 (= Q241), K267 (= K267)
- binding sulfate ion: N152 (≠ T152), 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)
55% identity, 99% coverage: 2:422/426 of query aligns to 3:422/426 of P22256
- I50 (= I49) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 110:111) binding
- E211 (= E210) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I240) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q241) binding
- K268 (= K267) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T296) binding
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
54% identity, 99% coverage: 2:422/426 of query aligns to 2:421/425 of 1szkA
- active site: V18 (≠ Q18), Y137 (≠ F137), E205 (= E205), D238 (= D238), Q241 (= Q241), K267 (= K267), T296 (= T296), R397 (= R398)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G110), S111 (≠ A111), Y137 (≠ F137), H138 (= H138), E205 (= E205), D238 (= D238), V240 (≠ I240), Q241 (= Q241), K267 (= K267)
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)
56% identity, 100% coverage: 1:426/426 of query aligns to 1:421/421 of P50457
- K267 (= K267) mutation to A: No GABA-AT activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
52% identity, 98% coverage: 5:421/426 of query aligns to 19:435/439 of 3q8nC
- active site: V32 (≠ Q18), Y151 (≠ F137), E221 (= E205), D254 (= D238), Q257 (= Q241), K283 (= K267), T312 (= T296), R412 (= R398)
- binding 4-oxobutanoic acid: G124 (= G110), A125 (= A111), V256 (≠ I240), K283 (= K267)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
48% identity, 96% coverage: 6:414/426 of query aligns to 23:428/440 of 6j2vA
- active site: L35 (≠ Q18), Y154 (≠ F137), D256 (= D238), K285 (= K267)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G110), A128 (= A111), Y154 (≠ F137), H155 (= H138), R157 (= R140), E223 (= E205), E228 (= E210), D256 (= D238), I258 (= I240), K285 (= K267), G313 (= G295), T314 (= T296)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
47% identity, 96% coverage: 6:414/426 of query aligns to 23:434/444 of 4atqF
- active site: V35 (≠ Q18), Y154 (≠ F137), E226 (= E205), D259 (= D238), Q262 (= Q241), K288 (= K267), T317 (= T296), R418 (= R398)
- binding gamma-amino-butanoic acid: M95 (= M78), Y154 (≠ F137), R157 (= R140), E231 (= E210), K288 (= K267), G316 (= G295)
- binding pyridoxal-5'-phosphate: G127 (= G110), A128 (= A111), Y154 (≠ F137), H155 (= H138), D259 (= D238), V261 (≠ I240)
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, 96% coverage: 5:414/426 of query aligns to 34:451/474 of O58478
- D251 (≠ E210) mutation to A: Loss of activity.
- K308 (= K267) 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, 97% coverage: 7:418/426 of query aligns to 21:439/454 of O50131
- T92 (≠ C76) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ V77) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G110) binding
- T125 (≠ A111) binding
- Q267 (= Q241) binding
- K293 (= K267) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T296) binding
7vo1A Structure of aminotransferase-substrate complex (see paper)
38% identity, 97% coverage: 7:418/426 of query aligns to 19:437/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I49), S121 (≠ T109), G122 (= G110), T123 (≠ A111), F149 (= F137), H150 (= H138), R152 (= R140), E234 (= E210), D262 (= D238), V264 (≠ I240), Q265 (= Q241), K291 (= K267), N318 (≠ G295), T319 (= T296), R417 (= R398)
7vntA Structure of aminotransferase-substrate complex (see paper)
38% identity, 97% coverage: 7:418/426 of query aligns to 19:437/452 of 7vntA
- binding L-ornithine: F149 (= F137), R152 (= R140), E234 (= E210), K291 (= K267)
- binding pyridoxal-5'-phosphate: G122 (= G110), T123 (≠ A111), F149 (= F137), H150 (= H138), E229 (= E205), D262 (= D238), V264 (≠ I240), Q265 (= Q241), K291 (= K267)
7vnoA Structure of aminotransferase (see paper)
38% identity, 97% coverage: 7:418/426 of query aligns to 19:437/452 of 7vnoA
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
34% identity, 95% coverage: 20:424/426 of query aligns to 25:434/446 of 5wyfA
- active site: Y142 (≠ F137), E217 (= E205), D250 (= D238), N253 (≠ Q241), K280 (= K267), T309 (≠ G295), R408 (= R398)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I49), Y84 (≠ V79), G115 (= G110), S116 (≠ A111), Y142 (≠ F137), H143 (= H138), D222 (≠ E210), D250 (= D238), V252 (≠ I240), N253 (≠ Q241), K280 (= K267), F308 (≠ G294), T309 (≠ G295), R408 (= R398)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
34% identity, 95% coverage: 20:424/426 of query aligns to 32:441/448 of 4ysnC
- active site: Y149 (≠ F137), E224 (= E205), D257 (= D238), N260 (≠ Q241), K287 (= K267), T316 (≠ G295), R415 (= R398)
- binding pyridoxal-5'-phosphate: S121 (≠ T109), G122 (= G110), S123 (≠ A111), Y149 (≠ F137), H150 (= H138), E224 (= E205), D257 (= D238), V259 (≠ I240), K287 (= K267), F315 (≠ G294), T316 (≠ G295)
Sites not aligning to the query:
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
34% identity, 95% coverage: 20:424/426 of query aligns to 23:432/439 of 5wyaA
- active site: Y140 (≠ F137), E215 (= E205), D248 (= D238), N251 (≠ Q241), K278 (= K267), T307 (≠ G295), R406 (= R398)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I49), Y82 (≠ V79), S112 (≠ T109), G113 (= G110), S114 (≠ A111), Y140 (≠ F137), H141 (= H138), E215 (= E205), D248 (= D238), V250 (≠ I240), N251 (≠ Q241), K278 (= K267), F306 (≠ G294), T307 (≠ G295), R406 (= R398)
Sites not aligning to the query:
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
36% identity, 97% coverage: 12:425/426 of query aligns to 1:399/401 of 4adbB
- active site: F136 (= F137), E188 (= E205), D221 (= D238), Q224 (= Q241), K250 (= K267), T279 (= T296), R372 (= R398)
- binding pyridoxal-5'-phosphate: S102 (≠ T109), G103 (= G110), A104 (= A111), F136 (= F137), H137 (= H138), D221 (= D238), V223 (≠ I240), Q224 (= Q241), K250 (= K267)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
37% identity, 93% coverage: 28:425/426 of query aligns to 25:399/400 of 4addA
- active site: F136 (= F137), E188 (= E205), D221 (= D238), Q224 (= Q241), K250 (= K267), T279 (= T296), R372 (= R398)
- binding pyridoxal-5'-phosphate: G103 (= G110), A104 (= A111), F136 (= F137), H137 (= H138), D221 (= D238), V223 (≠ I240), K250 (= K267)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: F136 (= F137), R139 (= R140)
Sites not aligning to the query:
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
36% identity, 91% coverage: 32:417/426 of query aligns to 29:391/402 of 4jevB
- active site: F136 (= F137), E188 (= E205), D221 (= D238), Q224 (= Q241), K250 (= K267), T279 (= T296), R372 (= R398)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I49), S102 (≠ T109), G103 (= G110), T104 (≠ A111), F136 (= F137), H137 (= H138), E188 (= E205), E193 (= E210), D221 (= D238), V223 (≠ I240), Q224 (= Q241), K250 (= K267), 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)
36% identity, 91% coverage: 32:417/426 of query aligns to 34:396/405 of P40732
- GT 108:109 (≠ GA 110:111) binding
- K255 (= K267) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T296) binding
Query Sequence
>5210744 FitnessBrowser__PV4:5210744
MSNAELQARKVQAIARGQGNAYPVYVERALNAELWDVEGKRYIDFGTGIAVCNTGHSHPK
VVAAVKAQLDNFSHTCVMVNPYESAVALAEQLNRIAPGGSDKKAIFVTTGAEAVENCVKI
ARAHTGRRGVIAFNGGFHGRTNLTMALTGKITPYKHQFGPFAGDIFHAPYPVAFHGVSVK
DSLKAIEHLFKVDIAPCDVAAIVVEPVQGEGGFYAAPPEFLQALRALCDQHGIVLVMDEI
QTGFGRTGKMFSCEHAGVEPDLMTMAKGIAGGFPLAAVVGKSEIMDAPLPGGLGGTYGGS
PVGCVAALAVLEVMQEEQLVERAVKIGDSFNQALSALKEQYPQLIGEVRNQGAMIAMELV
IDGDIEQPNTALTQAIIANAAAHGLVLLACGFYGNVIRFLPALTISDEIMAEGLAKFKTL
FESLVD
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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