SitesBLAST
Comparing WP_086510803.1 NCBI__GCF_002151265.1:WP_086510803.1 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)
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)
50% identity, 98% coverage: 2:422/430 of query aligns to 3:423/426 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 (= V240) 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
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
50% identity, 98% coverage: 2:422/430 of query aligns to 2:422/425 of 1sffA
- active site: V18 (≠ A18), Y137 (= Y137), E205 (= E205), D238 (= D238), Q241 (= Q241), K267 (= K267), T296 (= T296), R397 (= R397)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ T78), G110 (= G110), S111 (≠ A111), Y137 (= Y137), H138 (= H138), R140 (= R140), E205 (= E205), D238 (= D238), V240 (= V240), Q241 (= Q241), K267 (= K267), T296 (= T296)
- binding sulfate ion: N152 (≠ A152), Y393 (≠ G393)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
50% identity, 98% coverage: 2:422/430 of query aligns to 2:422/425 of 1sf2A
- active site: V18 (≠ A18), Y137 (= Y137), E205 (= E205), D238 (= D238), Q241 (= Q241), K267 (= K267), T296 (= T296), R397 (= R397)
- binding pyridoxal-5'-phosphate: G110 (= G110), S111 (≠ A111), Y137 (= Y137), H138 (= H138), E205 (= E205), D238 (= D238), V240 (= V240), Q241 (= Q241), K267 (= K267)
- binding sulfate ion: N152 (≠ A152), Y393 (≠ G393)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
50% identity, 98% coverage: 2:422/430 of query aligns to 2:422/425 of 1szkA
- active site: V18 (≠ A18), Y137 (= Y137), E205 (= E205), D238 (= D238), Q241 (= Q241), K267 (= K267), T296 (= T296), R397 (= R397)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G110), S111 (≠ A111), Y137 (= Y137), H138 (= H138), E205 (= E205), D238 (= D238), V240 (= V240), 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)
47% identity, 98% coverage: 1:422/430 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)
44% identity, 97% coverage: 5:423/430 of query aligns to 19:438/439 of 3q8nC
- active site: V32 (≠ A18), Y151 (= Y137), E221 (= E205), D254 (= D238), Q257 (= Q241), K283 (= K267), T312 (= T296), R412 (= R397)
- binding 4-oxobutanoic acid: G124 (= G110), A125 (= A111), V256 (= V240), K283 (= K267)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
45% identity, 97% coverage: 6:420/430 of query aligns to 23:435/440 of 6j2vA
- active site: L35 (≠ A18), Y154 (= Y137), 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 (= Y137), H155 (= H138), R157 (= R140), E223 (= E205), E228 (= E210), D256 (= D238), I258 (≠ V240), K285 (= K267), G313 (= G295), T314 (= T296)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
43% identity, 97% coverage: 6:420/430 of query aligns to 23:441/444 of 4atqF
- active site: V35 (≠ A18), Y154 (= Y137), E226 (= E205), D259 (= D238), Q262 (= Q241), K288 (= K267), T317 (= T296), R418 (= R397)
- binding gamma-amino-butanoic acid: M95 (≠ T78), Y154 (= Y137), R157 (= R140), E231 (= E210), K288 (= K267), G316 (= G295)
- binding pyridoxal-5'-phosphate: G127 (= G110), A128 (= A111), Y154 (= Y137), H155 (= H138), D259 (= D238), V261 (= V240)
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)
33% identity, 93% coverage: 28:428/430 of query aligns to 58:466/474 of O58478
- D251 (≠ E210) mutation to A: Loss of activity.
- K308 (= K267) mutation to A: Loss of activity.
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
33% identity, 94% coverage: 27:429/430 of query aligns to 30:438/439 of 5wyaA
- active site: Y140 (= Y137), E215 (= E205), D248 (= D238), N251 (≠ Q241), K278 (= K267), T307 (= T296), R406 (= R397)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I49), Y82 (≠ V79), S112 (= S109), G113 (= G110), S114 (≠ A111), Y140 (= Y137), H141 (= H138), E215 (= E205), D248 (= D238), V250 (= V240), N251 (≠ Q241), K278 (= K267), F306 (≠ G295), T307 (= T296), R406 (= R397)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
33% identity, 94% coverage: 27:429/430 of query aligns to 32:440/446 of 5wyfA
- active site: Y142 (= Y137), E217 (= E205), D250 (= D238), N253 (≠ Q241), K280 (= K267), T309 (= T296), R408 (= R397)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I49), Y84 (≠ V79), G115 (= G110), S116 (≠ A111), Y142 (= Y137), H143 (= H138), D222 (≠ E210), D250 (= D238), V252 (= V240), N253 (≠ Q241), K280 (= K267), F308 (≠ G295), T309 (= T296), R408 (= R397)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
33% identity, 94% coverage: 27:429/430 of query aligns to 39:447/448 of 4ysnC
- active site: Y149 (= Y137), E224 (= E205), D257 (= D238), N260 (≠ Q241), K287 (= K267), T316 (= T296), R415 (= R397)
- binding pyridoxal-5'-phosphate: S121 (= S109), G122 (= G110), S123 (≠ A111), Y149 (= Y137), H150 (= H138), E224 (= E205), D257 (= D238), V259 (= V240), K287 (= K267), F315 (≠ G295), T316 (= T296)
Sites not aligning to the query:
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)
36% identity, 96% coverage: 8:420/430 of query aligns to 20:442/454 of O50131
- T92 (= T78) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (vs. gap) 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)
36% identity, 96% coverage: 8:420/430 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 (= I49), S121 (= S109), G122 (= G110), T123 (≠ A111), F149 (≠ Y137), H150 (= H138), R152 (= R140), E234 (= E210), D262 (= D238), V264 (= V240), Q265 (= Q241), K291 (= K267), N318 (≠ G295), T319 (= T296), R417 (= R397)
7vntA Structure of aminotransferase-substrate complex (see paper)
36% identity, 96% coverage: 8:420/430 of query aligns to 18:440/452 of 7vntA
- binding L-ornithine: F149 (≠ Y137), R152 (= R140), E234 (= E210), K291 (= K267)
- binding pyridoxal-5'-phosphate: G122 (= G110), T123 (≠ A111), F149 (≠ Y137), H150 (= H138), E229 (= E205), D262 (= D238), V264 (= V240), Q265 (= Q241), K291 (= K267)
7vnoA Structure of aminotransferase (see paper)
36% identity, 96% coverage: 8:420/430 of query aligns to 18:440/452 of 7vnoA
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
33% identity, 94% coverage: 20:424/430 of query aligns to 17:399/402 of 4jevB
- active site: F136 (≠ Y137), E188 (= E205), D221 (= D238), Q224 (= Q241), K250 (= K267), T279 (= T296), R372 (= R397)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I49), S102 (= S109), G103 (= G110), T104 (≠ A111), F136 (≠ Y137), H137 (= H138), E188 (= E205), E193 (= E210), D221 (= D238), V223 (= V240), Q224 (= Q241), K250 (= K267), R372 (= R397)
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)
33% identity, 94% coverage: 20:424/430 of query aligns to 22:404/405 of P40732
- GT 108:109 (≠ GA 110:111) binding
- K255 (= K267) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T296) binding
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
35% identity, 96% coverage: 9:420/430 of query aligns to 3:383/390 of A0QYS9
- K304 (≠ D328) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
33% identity, 94% coverage: 20:424/430 of query aligns to 17:394/397 of 4jewA
- active site: F136 (≠ Y137), E188 (= E205), D221 (= D238), Q224 (= Q241), K250 (= K267), T274 (= T296), R367 (= R397)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G110), T104 (≠ A111), F136 (≠ Y137), H137 (= H138), R139 (= R140), E188 (= E205), E193 (= E210), D221 (= D238), V223 (= V240), K250 (= K267)
- binding picric acid: K25 (≠ R28), K27 (≠ E30), W32 (= W35)
Query Sequence
>WP_086510803.1 NCBI__GCF_002151265.1:WP_086510803.1
MNNAQLNELKQRYVANGAASPATQFADRAENALIWDADGNRIIDFAGGIGVLNIGHRHPK
VVEAVKAQLDKVMHTCQTVMPYEGYVKVAEKLSQVTPVRGHAKVMLANSGAEALENAVKI
ARAATGKNNVICFDGGYHGRTFMTMAMNGKVAPYASDFGTMPGNVFRAPYPVPYHGVSED
EAIRGLKMAIKTDANPRDTAAIVLEPVLGEGGFYPAPASFLKAIREICDEHGMLMIVDEV
QSGFGRTGKLFAIEHSGVEPDIITMAKSMADGMPISAVVGTDKVMDASGPNSLGGTYTGN
PLSCAATLAVLDVFEEENILEKSMALGDKLAKRFAQWQRDFDCVDNARNMGAMAALDLVT
DKAKHTPDADLAAALCKKAREKGLILLSCGLYGNTIRFLMPVTIEDEILEEGLDIVEAAL
TELVGSKATA
Or try a new SitesBLAST search
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