SitesBLAST
Comparing WP_012170173.1 NCBI__GCF_000010525.1:WP_012170173.1 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)
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)
31% identity, 94% coverage: 19:464/472 of query aligns to 33:456/474 of O58478
- D251 (≠ T244) mutation to A: Loss of activity.
- K308 (= K301) 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)
33% identity, 92% coverage: 38:472/472 of query aligns to 34:448/454 of O50131
- T92 (≠ S95) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ Q96) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G129) binding pyridoxal 5'-phosphate
- T125 (≠ A130) binding pyridoxal 5'-phosphate
- Q267 (= Q275) binding pyridoxal 5'-phosphate
- K293 (= K301) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T333) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
33% identity, 92% coverage: 38:472/472 of query aligns to 32:446/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ Y67), S121 (≠ G128), G122 (= G129), T123 (≠ A130), F149 (≠ Y157), H150 (= H158), R152 (= R160), E234 (≠ T244), D262 (= D272), V264 (≠ I274), Q265 (= Q275), K291 (= K301), N318 (vs. gap), T319 (= T333), R417 (≠ T443)
7vntA Structure of aminotransferase-substrate complex (see paper)
33% identity, 92% coverage: 38:472/472 of query aligns to 32:446/452 of 7vntA
- binding L-ornithine: F149 (≠ Y157), R152 (= R160), E234 (≠ T244), K291 (= K301)
- binding pyridoxal-5'-phosphate: G122 (= G129), T123 (≠ A130), F149 (≠ Y157), H150 (= H158), E229 (= E239), D262 (= D272), V264 (≠ I274), Q265 (= Q275), K291 (= K301)
7vnoA Structure of aminotransferase (see paper)
33% identity, 92% coverage: 38:472/472 of query aligns to 32:446/452 of 7vnoA
6io1B Crystal structure of a novel thermostable (s)-enantioselective omega- transaminase from thermomicrobium roseum (see paper)
32% identity, 90% coverage: 39:465/472 of query aligns to 29:447/448 of 6io1B
- active site: Y151 (= Y157), D257 (= D272), K286 (= K301)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G117 (= G128), G118 (= G129), A119 (= A130), N122 (≠ I133), Y151 (= Y157), H152 (= H158), D257 (= D272), V259 (≠ I274), I260 (≠ Q275), K286 (= K301)
Sites not aligning to the query:
5lhaA Amine transaminase crystal structure from an uncultivated pseudomonas species in the pmp-bound form
29% identity, 90% coverage: 43:469/472 of query aligns to 27:446/447 of 5lhaA
- active site: Y146 (= Y157), D253 (= D272), K282 (= K301), T319 (= T333)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G113 (= G129), S114 (≠ A130), Y146 (= Y157), H147 (= H158), G148 (= G159), E220 (= E239), D253 (= D272), K282 (= K301), Y318 (vs. gap), T319 (= T333)
5lh9D Amine transaminase crystal structure from an uncultivated pseudomonas species in the plp-bound (internal aldimine) form
29% identity, 90% coverage: 43:469/472 of query aligns to 29:448/449 of 5lh9D
- active site: Y148 (= Y157), D255 (= D272), K284 (= K301), T321 (= T333)
- binding pyridoxal-5'-phosphate: G115 (= G129), S116 (≠ A130), Y148 (= Y157), H149 (= H158), G150 (= G159), E222 (= E239), D255 (= D272), V257 (≠ I274), K284 (= K301)
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
31% identity, 91% coverage: 40:469/472 of query aligns to 24:412/412 of 2eo5A
- active site: F139 (≠ Y157), E219 (= E239), D252 (= D272), Q255 (= Q275), K281 (= K301), T303 (= T333), R386 (≠ T443)
- binding pyridoxal-5'-phosphate: G113 (= G129), T114 (≠ A130), F139 (≠ Y157), H140 (= H158), E219 (= E239), D252 (= D272), V254 (≠ I274), Q255 (= Q275), K281 (= K301)
Sites not aligning to the query:
6s54A Transaminase from pseudomonas fluorescens (see paper)
28% identity, 90% coverage: 41:467/472 of query aligns to 31:449/453 of 6s54A
- active site: Y152 (= Y157), D258 (= D272), K287 (= K301)
- binding pyridoxal-5'-phosphate: G119 (= G129), S120 (≠ A130), Y152 (= Y157), H153 (= H158), G154 (= G159), E225 (= E239), D258 (= D272), V260 (≠ I274), I261 (≠ Q275), K287 (= K301)
Sites not aligning to the query:
5kr6B Directed evolution of transaminases by ancestral reconstruction. Using old proteins for new chemistries
28% identity, 96% coverage: 17:470/472 of query aligns to 5:457/460 of 5kr6B
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
29% identity, 90% coverage: 41:466/472 of query aligns to 23:420/425 of 1szkA
- active site: Y137 (= Y157), E205 (= E239), D238 (= D272), Q241 (= Q275), K267 (= K301), T296 (= T333), R397 (≠ T443)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G129), S111 (≠ A130), Y137 (= Y157), H138 (= H158), E205 (= E239), D238 (= D272), V240 (≠ I274), Q241 (= Q275), K267 (= K301)
Sites not aligning to the query:
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)
29% identity, 90% coverage: 41:466/472 of query aligns to 24:421/426 of P22256
- I50 (≠ Y67) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 129:130) binding pyridoxal 5'-phosphate
- E211 (≠ T244) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I274) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q275) binding pyridoxal 5'-phosphate
- K268 (= K301) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T333) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
29% identity, 90% coverage: 41:466/472 of query aligns to 23:420/425 of 1sffA
- active site: Y137 (= Y157), E205 (= E239), D238 (= D272), Q241 (= Q275), K267 (= K301), T296 (= T333), R397 (≠ T443)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q96), G110 (= G129), S111 (≠ A130), Y137 (= Y157), H138 (= H158), R140 (= R160), E205 (= E239), D238 (= D272), V240 (≠ I274), Q241 (= Q275), K267 (= K301), T296 (= T333)
- binding sulfate ion: N152 (≠ R172), Y393 (≠ K439)
Sites not aligning to the query:
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
29% identity, 90% coverage: 41:466/472 of query aligns to 23:420/425 of 1sf2A
- active site: Y137 (= Y157), E205 (= E239), D238 (= D272), Q241 (= Q275), K267 (= K301), T296 (= T333), R397 (≠ T443)
- binding pyridoxal-5'-phosphate: G110 (= G129), S111 (≠ A130), Y137 (= Y157), H138 (= H158), E205 (= E239), D238 (= D272), V240 (≠ I274), Q241 (= Q275), K267 (= K301)
- binding sulfate ion: N152 (≠ R172), Y393 (≠ K439)
Sites not aligning to the query:
5kr5A Directed evolution of transaminases by ancestral reconstruction. Using old proteins for new chemistries
27% identity, 96% coverage: 19:470/472 of query aligns to 3:453/455 of 5kr5A
- binding calcium ion: E66 (≠ Q77), D70 (= D81), D412 (≠ G419), E447 (≠ Q464)
- binding pyridoxal-5'-phosphate: S117 (≠ G128), G118 (= G129), S119 (≠ A130), Y151 (= Y157), H152 (= H158), G153 (= G159), E224 (= E239), D257 (= D272), V259 (≠ I274), K286 (= K301), W322 (vs. gap), T323 (= T333)
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
27% identity, 95% coverage: 20:469/472 of query aligns to 7:432/439 of 5wyaA
- active site: A20 (≠ D33), Y140 (= Y157), E215 (= E239), D248 (= D272), N251 (≠ Q275), K278 (= K301), T307 (= T333), R406 (≠ T443)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ Y67), Y82 (= Y97), S112 (≠ G128), G113 (= G129), S114 (≠ A130), Y140 (= Y157), H141 (= H158), E215 (= E239), D248 (= D272), V250 (≠ I274), N251 (≠ Q275), K278 (= K301), F306 (≠ S332), T307 (= T333), R406 (≠ T443)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
27% identity, 95% coverage: 20:469/472 of query aligns to 16:441/448 of 4ysnC
- active site: A29 (≠ D33), Y149 (= Y157), E224 (= E239), D257 (= D272), N260 (≠ Q275), K287 (= K301), T316 (= T333), R415 (≠ T443)
- binding pyridoxal-5'-phosphate: S121 (≠ G128), G122 (= G129), S123 (≠ A130), Y149 (= Y157), H150 (= H158), E224 (= E239), D257 (= D272), V259 (≠ I274), K287 (= K301), F315 (≠ S332), T316 (= T333)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
27% identity, 95% coverage: 20:469/472 of query aligns to 9:434/446 of 5wyfA
- active site: A22 (≠ D33), Y142 (= Y157), E217 (= E239), D250 (= D272), N253 (≠ Q275), K280 (= K301), T309 (= T333), R408 (≠ T443)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ Y67), Y84 (= Y97), G115 (= G129), S116 (≠ A130), Y142 (= Y157), H143 (= H158), D222 (≠ T244), D250 (= D272), V252 (≠ I274), N253 (≠ Q275), K280 (= K301), F308 (≠ S332), T309 (= T333), R408 (≠ T443)
3fcrA Crystal structure of putative aminotransferase (yp_614685.1) from silicibacter sp. Tm1040 at 1.80 a resolution
32% identity, 77% coverage: 42:403/472 of query aligns to 34:396/458 of 3fcrA
- active site: Y153 (= Y157), E227 (= E239), D260 (= D272), V263 (≠ Q275), K289 (= K301), T326 (= T333)
- binding pyridoxal-5'-phosphate: G120 (= G129), S121 (≠ A130), Y153 (= Y157), H154 (= H158), E227 (= E239), D260 (= D272), V262 (≠ I274), K289 (= K301)
Sites not aligning to the query:
Query Sequence
>WP_012170173.1 NCBI__GCF_000010525.1:WP_012170173.1
MLDRSLLTGTATTAEAERERLLTLENAYCSHGDTVHYTEFPKIFERCEGSFMYDDEDRPF
LDLQMWYSAVNFGYGNQRLNDAMRRQLERLPQVASQYLHREKIELAAEIAIGAQERFGRK
GRVHFNVGGAQAIEDSLKIVRNACGGKSLMFAFEGGYHGRTLGASAITSSYRYRRRYGHF
GERAQFVEFPYHFRGPRGMSKEEYGLHCVRKFERLFESEYNGVWDPKVGQSEYAAFYVEP
IQGTGGYVIPPANFFPELKRVLDKHGILLVVDEIQMGFFRTGKLWSIEHFGVQPDVLVFG
KALTNGLNPLSGVWAREELINPQIFPAGSTHSTFNANPLGTAVALEAMRMMQEEDFGASV
MEKGAHFLEGIKELKKKHAIVGDVDGLGLALRIEICEPHDSYTPSKKLVDLMADEAMKGD
LVYGGERYGLVLDIGGYHKNVITLAPALTISHAEIDMALALLDQLFTRVTPR
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