SitesBLAST
Comparing WP_013011689.1 NCBI__GCF_000025725.1:WP_013011689.1 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)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
53% identity, 97% coverage: 3:472/486 of query aligns to 2:466/478 of 3h0mA
- active site: K72 (= K78), S147 (= S153), S148 (= S154), S166 (= S172), T168 (= T174), G169 (= G175), G170 (= G176), S171 (= S177), Q174 (= Q180)
- binding glutamine: M122 (= M128), G123 (= G129), D167 (= D173), T168 (= T174), G169 (= G175), G170 (= G176), S171 (= S177), F199 (= F205), Y302 (= Y308), R351 (= R356), D418 (= D423)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
53% identity, 97% coverage: 3:472/486 of query aligns to 2:466/478 of 3h0lA
- active site: K72 (= K78), S147 (= S153), S148 (= S154), S166 (= S172), T168 (= T174), G169 (= G175), G170 (= G176), S171 (= S177), Q174 (= Q180)
- binding asparagine: G123 (= G129), S147 (= S153), G169 (= G175), G170 (= G176), S171 (= S177), Y302 (= Y308), R351 (= R356), D418 (= D423)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
50% identity, 100% coverage: 1:484/486 of query aligns to 1:485/485 of 2f2aA
- active site: K79 (= K78), S154 (= S153), S155 (= S154), S173 (= S172), T175 (= T174), G176 (= G175), G177 (= G176), S178 (= S177), Q181 (= Q180)
- binding glutamine: G130 (= G129), S154 (= S153), D174 (= D173), T175 (= T174), G176 (= G175), S178 (= S177), F206 (= F205), Y309 (= Y308), Y310 (= Y309), R358 (= R356), D425 (= D423)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
50% identity, 100% coverage: 1:484/486 of query aligns to 1:485/485 of 2dqnA
- active site: K79 (= K78), S154 (= S153), S155 (= S154), S173 (= S172), T175 (= T174), G176 (= G175), G177 (= G176), S178 (= S177), Q181 (= Q180)
- binding asparagine: M129 (= M128), G130 (= G129), T175 (= T174), G176 (= G175), S178 (= S177), Y309 (= Y308), Y310 (= Y309), R358 (= R356), D425 (= D423)
3kfuE Crystal structure of the transamidosome (see paper)
47% identity, 96% coverage: 9:475/486 of query aligns to 3:457/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 83% coverage: 71:471/486 of query aligns to 31:449/450 of 4n0iA
- active site: K38 (= K78), S116 (= S153), S117 (= S154), T135 (≠ S172), T137 (= T174), G138 (= G175), G139 (= G176), S140 (= S177), L143 (≠ Q180)
- binding glutamine: G89 (= G129), T137 (= T174), G138 (= G175), S140 (= S177), Y168 (≠ F205), Y271 (= Y308), Y272 (= Y309), R320 (= R356), D404 (= D423)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
30% identity, 89% coverage: 50:481/486 of query aligns to 177:597/607 of Q7XJJ7
- K205 (= K78) mutation to A: Loss of activity.
- SS 281:282 (= SS 153:154) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 174:177) binding substrate
- S305 (= S177) mutation to A: Loss of activity.
- R307 (= R179) mutation to A: Loss of activity.
- S360 (≠ H232) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 89% coverage: 50:481/486 of query aligns to 177:597/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A127), T258 (≠ S130), S281 (= S153), G302 (≠ T174), G303 (= G175), S305 (= S177), S472 (≠ T361), I532 (≠ L417), M539 (vs. gap)
Sites not aligning to the query:
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
30% identity, 89% coverage: 50:481/486 of query aligns to 177:597/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A127), G302 (≠ T174), G303 (= G175), G304 (= G176), A305 (≠ S177), V442 (≠ Y309), I475 (≠ L364), M539 (vs. gap)
Sites not aligning to the query:
8ey1D Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with n-(3-oxododecanoyl)-l-homoserine lactone
30% identity, 89% coverage: 50:481/486 of query aligns to 177:597/605 of 8ey1D
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 97% coverage: 10:480/486 of query aligns to 5:455/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
33% identity, 82% coverage: 75:472/486 of query aligns to 92:497/508 of 3a1iA
- active site: K95 (= K78), S170 (= S153), S171 (= S154), G189 (≠ S172), Q191 (≠ T174), G192 (= G175), G193 (= G176), A194 (≠ S177), I197 (≠ Q180)
- binding benzamide: F145 (≠ M128), S146 (≠ G129), G147 (≠ S130), Q191 (≠ T174), G192 (= G175), G193 (= G176), A194 (≠ S177), W327 (≠ Y308)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 99% coverage: 3:482/486 of query aligns to 3:486/487 of 1m21A
- active site: K81 (= K78), S160 (= S153), S161 (= S154), T179 (≠ S172), T181 (= T174), D182 (≠ G175), G183 (= G176), S184 (= S177), C187 (≠ Q180)
- binding : A129 (= A127), N130 (≠ M128), F131 (≠ G129), C158 (≠ G151), G159 (= G152), S160 (= S153), S184 (= S177), C187 (≠ Q180), I212 (≠ F205), R318 (≠ Y309), L321 (≠ A312), L365 (≠ M358), F426 (≠ Y420)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 96% coverage: 7:472/486 of query aligns to 29:487/507 of Q84DC4
- T31 (≠ K9) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K78) mutation to A: Abolishes activity on mandelamide.
- S180 (= S153) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S154) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G175) mutation to A: Increase in KM values for aromatic substrates, but not aliphatic substrates. Active against lactamide but not against mandelamide; when associated with H-207 and E-382.; mutation to V: Increase in KM values for aromatic substrates, but not aliphatic substrates.
- S204 (= S177) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q180) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with E-382. Active against lactamide but not against mandelamide; when associated with A-202 and E-382. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with S-316 and N-437.
- S316 (≠ A304) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- Q382 (≠ D370) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with H-207. Active against lactamide but not against mandelamide; when associated with A-202 and H-207.
- I437 (≠ S428) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with I-31. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-316.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 87% coverage: 48:471/486 of query aligns to 62:460/605 of Q936X2
- K91 (= K78) mutation to A: Loss of activity.
- S165 (= S153) mutation to A: Loss of activity.
- S189 (= S177) mutation to A: Loss of activity.
Q9FR37 Amidase 1; AtAMI1; Translocon at the outer membrane of chloroplasts 64-I; AtTOC64-I; EC 3.5.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 74% coverage: 107:467/486 of query aligns to 67:417/425 of Q9FR37
- S113 (= S153) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S154) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D173) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S177) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C185) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ G261) mutation to T: Slightly reduces catalytic activity.
Sites not aligning to the query:
- 36 active site, Charge relay system; K→A: Loss of catalytic activity.; K→R: Reduces catalytic activity 10-fold.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
26% identity, 98% coverage: 6:479/486 of query aligns to 6:480/490 of 4yjiA
- active site: K79 (= K78), S158 (= S153), S159 (= S154), G179 (≠ T174), G180 (= G175), G181 (= G176), A182 (≠ S177)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L80), G132 (≠ A127), S158 (= S153), G179 (≠ T174), G180 (= G175), A182 (≠ S177)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 92% coverage: 23:468/486 of query aligns to 19:434/461 of 4gysB
- active site: K72 (= K78), S146 (= S153), S147 (= S154), T165 (≠ S172), T167 (= T174), A168 (≠ G175), G169 (= G176), S170 (= S177), V173 (≠ Q180)
- binding malonate ion: A120 (= A127), G122 (= G129), S146 (= S153), T167 (= T174), A168 (≠ G175), S170 (= S177), S193 (≠ F200), G194 (= G201), V195 (≠ L202), R200 (≠ S207), Y297 (= Y308), R305 (≠ A316)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 91% coverage: 33:472/486 of query aligns to 29:407/412 of 1o9oA
- active site: K62 (= K78), A131 (≠ S153), S132 (= S154), T150 (≠ S172), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177), R158 (≠ Q180)
- binding 3-amino-3-oxopropanoic acid: G130 (= G152), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177), R158 (≠ Q180), P359 (= P416)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 91% coverage: 33:472/486 of query aligns to 29:407/412 of 1ocmA
- active site: K62 (= K78), S131 (= S153), S132 (= S154), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177)
- binding pyrophosphate 2-: R113 (≠ S131), S131 (= S153), Q151 (≠ D173), T152 (= T174), G153 (= G175), G154 (= G176), S155 (= S177), R158 (≠ Q180), P359 (= P416)
Query Sequence
>WP_013011689.1 NCBI__GCF_000025725.1:WP_013011689.1
MSFLNKNLKELTDGLAGKDFSSKELVQFYLDRIKKYDSEIQAFNYINENALKQAEAIDAK
RLKGETLPAYAGVPVALKDLLITKDMPTTCSSKFLEGFKPPFNGTAVSLLEEAGFINLGK
LSMDEFAMGSSNENAAFKKTRNPWDTTKVPGGSSGGSAASVAAGLAPVTLGSDTGGSIRQ
PASLCGVVGMKPTYGRVSRFGLVAFASSLDQIGPMGKSAFDLASILSVIGKHDSKDSTSA
NVDQKDYTKDLTDDVRGMKIGIPKEYFAEGLAPDVKSAVADAIKKYTDLGCEMVDISLPH
TDYALATYYIIATAEASSNLGRYDGVRFGRRAEADNLRDMYFNSRTEGFGEEVKRRIMLG
TYVLSAGYYDAYYLKAQRVRTLIKQDFVEAFKTVDAIICPTSPTTAFKAGAKTEDPLQMY
LSDIYTLSLNLFGGCGLSLPCGFDKDGMPIGVQLMGNYFEEGKILNLAHAFELATDISRI
PEKLKI
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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