SitesBLAST
Comparing WP_012172510.1 NCBI__GCF_000010525.1:WP_012172510.1 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: 22:466/475 of query aligns to 31:455/474 of O58478
- D251 (≠ T247) mutation to A: Loss of activity.
- K308 (= K304) mutation to A: Loss of activity.
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
31% identity, 89% coverage: 45:465/475 of query aligns to 23:416/425 of 1szkA
- active site: Y137 (= Y161), E205 (= E242), D238 (= D275), Q241 (= Q278), K267 (= K304), T296 (= T336), R397 (≠ T446)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G133), S111 (= S134), Y137 (= Y161), H138 (= H162), E205 (= E242), D238 (= D275), V240 (≠ I277), Q241 (= Q278), K267 (= K304)
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)
32% identity, 90% coverage: 47:473/475 of query aligns to 39:446/454 of O50131
- T92 (≠ S99) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ Q100) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G133) binding pyridoxal 5'-phosphate
- T125 (≠ S134) binding pyridoxal 5'-phosphate
- Q267 (= Q278) binding pyridoxal 5'-phosphate
- K293 (= K304) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T336) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
32% identity, 90% coverage: 47:473/475 of query aligns to 37:444/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ Y71), S121 (≠ G132), G122 (= G133), T123 (≠ S134), F149 (≠ Y161), H150 (= H162), R152 (= R164), E234 (≠ T247), D262 (= D275), V264 (≠ I277), Q265 (= Q278), K291 (= K304), N318 (vs. gap), T319 (= T336), R417 (≠ T446)
7vntA Structure of aminotransferase-substrate complex (see paper)
32% identity, 90% coverage: 47:473/475 of query aligns to 37:444/452 of 7vntA
- binding L-ornithine: F149 (≠ Y161), R152 (= R164), E234 (≠ T247), K291 (= K304)
- binding pyridoxal-5'-phosphate: G122 (= G133), T123 (≠ S134), F149 (≠ Y161), H150 (= H162), E229 (= E242), D262 (= D275), V264 (≠ I277), Q265 (= Q278), K291 (= K304)
7vnoA Structure of aminotransferase (see paper)
32% identity, 90% coverage: 47:473/475 of query aligns to 37:444/452 of 7vnoA
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
31% identity, 89% coverage: 45:465/475 of query aligns to 23:416/425 of 1sffA
- active site: Y137 (= Y161), E205 (= E242), D238 (= D275), Q241 (= Q278), K267 (= K304), T296 (= T336), R397 (≠ T446)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q100), G110 (= G133), S111 (= S134), Y137 (= Y161), H138 (= H162), R140 (= R164), E205 (= E242), D238 (= D275), V240 (≠ I277), Q241 (= Q278), K267 (= K304), T296 (= T336)
- binding sulfate ion: N152 (vs. gap), Y393 (≠ K442)
Sites not aligning to the query:
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
31% identity, 89% coverage: 45:465/475 of query aligns to 23:416/425 of 1sf2A
- active site: Y137 (= Y161), E205 (= E242), D238 (= D275), Q241 (= Q278), K267 (= K304), T296 (= T336), R397 (≠ T446)
- binding pyridoxal-5'-phosphate: G110 (= G133), S111 (= S134), Y137 (= Y161), H138 (= H162), E205 (= E242), D238 (= D275), V240 (≠ I277), Q241 (= Q278), K267 (= K304)
- binding sulfate ion: N152 (vs. gap), Y393 (≠ K442)
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)
31% identity, 89% coverage: 45:465/475 of query aligns to 24:417/426 of P22256
- I50 (≠ Y71) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (= GS 133:134) binding pyridoxal 5'-phosphate
- E211 (≠ T247) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I277) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q278) binding pyridoxal 5'-phosphate
- K268 (= K304) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T336) binding pyridoxal 5'-phosphate
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
31% identity, 90% coverage: 45:472/475 of query aligns to 25:412/412 of 2eo5A
- active site: F139 (≠ Y161), E219 (= E242), D252 (= D275), Q255 (= Q278), K281 (= K304), T303 (= T336), R386 (≠ T446)
- binding pyridoxal-5'-phosphate: G113 (= G133), T114 (≠ S134), F139 (≠ Y161), H140 (= H162), E219 (= E242), D252 (= D275), V254 (≠ I277), Q255 (= Q278), K281 (= K304)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
28% identity, 96% coverage: 20:475/475 of query aligns to 11:444/448 of 4ysnC
- active site: A29 (≠ D38), Y149 (= Y161), E224 (= E242), D257 (= D275), N260 (≠ Q278), K287 (= K304), T316 (≠ S335), R415 (≠ T446)
- binding pyridoxal-5'-phosphate: S121 (≠ G132), G122 (= G133), S123 (= S134), Y149 (= Y161), H150 (= H162), E224 (= E242), D257 (= D275), V259 (≠ I277), K287 (= K304), F315 (≠ H334), T316 (≠ S335)
6io1B Crystal structure of a novel thermostable (s)-enantioselective omega- transaminase from thermomicrobium roseum (see paper)
31% identity, 90% coverage: 45:472/475 of query aligns to 31:446/448 of 6io1B
- active site: Y151 (= Y161), D257 (= D275), K286 (= K304)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G117 (= G132), G118 (= G133), A119 (≠ S134), N122 (≠ V137), Y151 (= Y161), H152 (= H162), D257 (= D275), V259 (≠ I277), I260 (≠ Q278), K286 (= K304)
Sites not aligning to the query:
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
28% identity, 96% coverage: 20:475/475 of query aligns to 2:435/439 of 5wyaA
- active site: A20 (≠ D38), Y140 (= Y161), E215 (= E242), D248 (= D275), N251 (≠ Q278), K278 (= K304), T307 (≠ S335), R406 (≠ T446)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ Y71), Y82 (= Y101), S112 (≠ G132), G113 (= G133), S114 (= S134), Y140 (= Y161), H141 (= H162), E215 (= E242), D248 (= D275), V250 (≠ I277), N251 (≠ Q278), K278 (= K304), F306 (≠ H334), T307 (≠ S335), R406 (≠ T446)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
28% identity, 96% coverage: 20:475/475 of query aligns to 4:437/446 of 5wyfA
- active site: A22 (≠ D38), Y142 (= Y161), E217 (= E242), D250 (= D275), N253 (≠ Q278), K280 (= K304), T309 (≠ S335), R408 (≠ T446)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ Y71), Y84 (= Y101), G115 (= G133), S116 (= S134), Y142 (= Y161), H143 (= H162), D222 (≠ T247), D250 (= D275), V252 (≠ I277), N253 (≠ Q278), K280 (= K304), F308 (≠ H334), T309 (≠ S335), R408 (≠ T446)
6s54A Transaminase from pseudomonas fluorescens (see paper)
28% identity, 90% coverage: 39:466/475 of query aligns to 25:445/453 of 6s54A
- active site: Y152 (= Y161), D258 (= D275), K287 (= K304)
- binding pyridoxal-5'-phosphate: G119 (= G133), S120 (= S134), Y152 (= Y161), H153 (= H162), G154 (= G163), E225 (= E242), D258 (= D275), V260 (≠ I277), I261 (≠ Q278), K287 (= K304)
Sites not aligning to the query:
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
31% identity, 89% coverage: 45:465/475 of query aligns to 43:421/429 of P73133
- S125 (≠ G132) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G133) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (≠ S134) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R164) mutation to A: 4100-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 9.5% of N-acetylornithine aminotransferase wild-type activity.
- E223 (≠ T247) mutation to A: 65-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 50% of N-acetylornithine aminotransferase wild-type activity.; mutation to S: 73-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Shows 160% of N-acetylornithine aminotransferase wild-type activity.
- D251 (= D275) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q278) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K304) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T336) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (≠ T446) mutation to A: 2080-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 18% of N-acetylornithine aminotransferase wild-type activity.
Sites not aligning to the query:
- 39 Y→F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
5kr6B Directed evolution of transaminases by ancestral reconstruction. Using old proteins for new chemistries
27% identity, 88% coverage: 46:464/475 of query aligns to 35:448/460 of 5kr6B
5lhaA Amine transaminase crystal structure from an uncultivated pseudomonas species in the pmp-bound form
30% identity, 91% coverage: 41:472/475 of query aligns to 21:446/447 of 5lhaA
- active site: Y146 (= Y161), D253 (= D275), K282 (= K304), T319 (= T336)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G113 (= G133), S114 (= S134), Y146 (= Y161), H147 (= H162), G148 (= G163), E220 (= E242), D253 (= D275), K282 (= K304), Y318 (vs. gap), T319 (= T336)
5lh9D Amine transaminase crystal structure from an uncultivated pseudomonas species in the plp-bound (internal aldimine) form
30% identity, 91% coverage: 41:472/475 of query aligns to 23:448/449 of 5lh9D
- active site: Y148 (= Y161), D255 (= D275), K284 (= K304), T321 (= T336)
- binding pyridoxal-5'-phosphate: G115 (= G133), S116 (= S134), Y148 (= Y161), H149 (= H162), G150 (= G163), E222 (= E242), D255 (= D275), V257 (≠ I277), K284 (= K304)
Q6LFH8 Ornithine aminotransferase; PfOAT; Ornithine--oxo-acid aminotransferase; EC 2.6.1.13 from Plasmodium falciparum (isolate 3D7) (see paper)
27% identity, 89% coverage: 45:465/475 of query aligns to 29:403/414 of Q6LFH8
- C154 (≠ A168) modified: Disulfide link with 163, Reversible; mutation to S: Severe reduction in catalytic activity. Does not affect TRX1-mediated activation. Severe reduction in catalytic activity and loss of TRX1-mediated activation; when associated with S-163.
- C163 (≠ Y177) modified: Disulfide link with 154, Reversible; mutation to S: No effect on catalytic activity. Requires higher concentrations of TRX1 for activation. Severe reduction in catalytic activity and loss of TRX1-mediated activation; when associated with S-154.
- C316 (≠ G361) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C350 (≠ L395) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
- C390 (≠ L452) mutation to S: About 70% reduction in catalytic activity. Does not affect TRX1-mediated activation.
Query Sequence
>WP_012172510.1 NCBI__GCF_000010525.1:WP_012172510.1
MNIPARHLAAGGTRPSAFDVSRETRLLALEQRYCSHGDTVHYSEPKIFDRCQGSYMYDAE
DVPYLDLQMWYSAVNFGYGNQRLNKALTRQLDRLPQVASQYLHAEKIELAATIAQHAEKT
WGAGGRVHFNVGGSQAVEDALKLVRNARRGKGTMFAFEGGYHGRTLGASAITSSYRYRRR
YGHFDRALFVPFPYHFRGPKGMDKEEYGLHCVKQFERLFESEYNGVWDPKAGEAECAAFF
VEPIQGTGGYVIPPHNFFIELKKVLDRHGILLVVDEIQMGVYRTGKLWSIEHFGVTPDVL
VFGKAITNGLNPLSGIWARDALINPEVFPPGSTHSTFASNPLGTAVALETLRMVEEEQDF
GAAVMAKGAYFLEGLQYLQRSHKVVGDVDGLGLALRMEICEEDGHTPNKALVDRMVDIAL
AADLELDGRRHGLVLDIGGYYKNVVTLAPSLLITKSEIDQAIRLLDLLLTRVTRG
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