SitesBLAST
Comparing WP_012760005.1 NCBI__GCF_000023185.1:WP_012760005.1 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)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
53% identity, 99% coverage: 5:598/601 of query aligns to 19:605/605 of Q936X2
- K91 (= K77) mutation to A: Loss of activity.
- S165 (= S151) mutation to A: Loss of activity.
- S189 (= S175) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
57% identity, 76% coverage: 6:460/601 of query aligns to 3:454/461 of 4gysB
- active site: K72 (= K77), S146 (= S151), S147 (= S152), T165 (= T170), T167 (= T172), A168 (= A173), G169 (= G174), S170 (= S175), V173 (= V178)
- binding malonate ion: A120 (= A125), G122 (= G127), S146 (= S151), T167 (= T172), A168 (= A173), S170 (= S175), S193 (≠ T198), G194 (= G199), V195 (≠ A200), R200 (≠ K205), Y297 (= Y302), R305 (= R310)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 72% coverage: 8:439/601 of query aligns to 7:462/478 of 3h0mA
- active site: K72 (= K77), S147 (= S151), S148 (= S152), S166 (≠ T170), T168 (= T172), G169 (≠ A173), G170 (= G174), S171 (= S175), Q174 (≠ V178)
- binding glutamine: M122 (≠ T126), G123 (= G127), D167 (= D171), T168 (= T172), G169 (≠ A173), G170 (= G174), S171 (= S175), F199 (≠ A203), Y302 (≠ D290), R351 (≠ I332), D418 (≠ G391)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 72% coverage: 8:439/601 of query aligns to 7:462/478 of 3h0lA
- active site: K72 (= K77), S147 (= S151), S148 (= S152), S166 (≠ T170), T168 (= T172), G169 (≠ A173), G170 (= G174), S171 (= S175), Q174 (≠ V178)
- binding asparagine: G123 (= G127), S147 (= S151), G169 (≠ A173), G170 (= G174), S171 (= S175), Y302 (≠ D290), R351 (≠ I332), D418 (≠ G391)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
28% identity, 72% coverage: 14:446/601 of query aligns to 137:591/607 of Q7XJJ7
- K205 (= K77) mutation to A: Loss of activity.
- SS 281:282 (= SS 151:152) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 172:175) binding
- S305 (= S175) mutation to A: Loss of activity.
- R307 (= R177) mutation to A: Loss of activity.
- S360 (≠ F230) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 72% coverage: 14:446/601 of query aligns to 137:591/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A125), T258 (≠ L128), S281 (= S151), G302 (≠ T172), G303 (≠ A173), S305 (= S175), S472 (≠ V329), I532 (≠ V387), M539 (≠ G394)
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 63% coverage: 67:447/601 of query aligns to 55:458/468 of 3kfuE
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 47% coverage: 6:290/601 of query aligns to 20:306/487 of 1m21A
- active site: K81 (= K77), S160 (= S151), S161 (= S152), T179 (= T170), T181 (= T172), D182 (≠ A173), G183 (= G174), S184 (= S175), C187 (≠ V178)
- binding : A129 (= A125), N130 (≠ T126), F131 (vs. gap), C158 (≠ G149), G159 (= G150), S160 (= S151), S184 (= S175), C187 (≠ V178), I212 (≠ A203)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 60% coverage: 65:425/601 of query aligns to 88:469/507 of Q84DC4
- K100 (= K77) mutation to A: Abolishes activity on mandelamide.
- S180 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S152) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A173) 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 (= S175) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V178) 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 (≠ A298) 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 (vs. gap) 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 (≠ G394) 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.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 69% coverage: 23:439/601 of query aligns to 31:469/485 of 2f2aA
- active site: K79 (= K77), S154 (= S151), S155 (= S152), S173 (≠ T170), T175 (= T172), G176 (≠ A173), G177 (= G174), S178 (= S175), Q181 (≠ V178)
- binding glutamine: G130 (= G127), S154 (= S151), D174 (= D171), T175 (= T172), G176 (≠ A173), S178 (= S175), F206 (≠ A203), Y309 (≠ D290), Y310 (= Y291), R358 (≠ I332), D425 (≠ G394)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 69% coverage: 23:439/601 of query aligns to 31:469/485 of 2dqnA
- active site: K79 (= K77), S154 (= S151), S155 (= S152), S173 (≠ T170), T175 (= T172), G176 (≠ A173), G177 (= G174), S178 (= S175), Q181 (≠ V178)
- binding asparagine: M129 (≠ T126), G130 (= G127), T175 (= T172), G176 (≠ A173), S178 (= S175), Y309 (≠ D290), Y310 (= Y291), R358 (≠ I332), D425 (≠ G394)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 68% coverage: 23:432/601 of query aligns to 19:437/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 61% coverage: 69:432/601 of query aligns to 87:486/508 of 3a1iA
- active site: K95 (= K77), S170 (= S151), S171 (= S152), G189 (≠ T170), Q191 (≠ T172), G192 (≠ A173), G193 (= G174), A194 (≠ S175), I197 (≠ V178)
- binding benzamide: F145 (≠ T126), S146 (≠ G127), G147 (≠ L128), Q191 (≠ T172), G192 (≠ A173), G193 (= G174), A194 (≠ S175), W327 (≠ A297)
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)
26% identity, 62% coverage: 69:442/601 of query aligns to 28:421/425 of Q9FR37
- K36 (= K77) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S151) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S152) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D171) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S175) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N183) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ A240) mutation to T: Slightly reduces catalytic activity.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
32% identity, 39% coverage: 69:302/601 of query aligns to 30:272/450 of 4n0iA
- active site: K38 (= K77), S116 (= S151), S117 (= S152), T135 (= T170), T137 (= T172), G138 (≠ A173), G139 (= G174), S140 (= S175), L143 (≠ V178)
- binding glutamine: G89 (= G127), T137 (= T172), G138 (≠ A173), S140 (= S175), Y168 (≠ A203), Y271 (≠ L301), Y272 (= Y302)
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 61% coverage: 49:414/601 of query aligns to 44:424/457 of 5h6sC
- active site: K77 (= K77), S152 (= S151), S153 (= S152), L173 (≠ T172), G174 (≠ A173), G175 (= G174), S176 (= S175)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A125), R128 (≠ G127), W129 (≠ L128), S152 (= S151), L173 (≠ T172), G174 (≠ A173), S176 (= S175), W306 (≠ Y291), F338 (= F317)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
33% identity, 37% coverage: 4:226/601 of query aligns to 3:235/564 of 6te4A
Sites not aligning to the query:
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
30% identity, 72% coverage: 5:436/601 of query aligns to 1:399/412 of 1ocmA
- active site: K62 (= K77), S131 (= S151), S132 (= S152), T152 (= T172), G153 (≠ A173), G154 (= G174), S155 (= S175)
- binding pyrophosphate 2-: R113 (= R132), S131 (= S151), Q151 (≠ D171), T152 (= T172), G153 (≠ A173), G154 (= G174), S155 (= S175), R158 (≠ V178), P359 (= P386)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
30% identity, 72% coverage: 5:436/601 of query aligns to 1:399/412 of 1o9oA
- active site: K62 (= K77), A131 (≠ S151), S132 (= S152), T150 (= T170), T152 (= T172), G153 (≠ A173), G154 (= G174), S155 (= S175), R158 (≠ V178)
- binding 3-amino-3-oxopropanoic acid: G130 (= G150), T152 (= T172), G153 (≠ A173), G154 (= G174), S155 (= S175), R158 (≠ V178), P359 (= P386)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
28% identity, 64% coverage: 60:445/601 of query aligns to 52:470/482 of 3a2qA
- active site: K69 (= K77), S147 (= S151), S148 (= S152), N166 (≠ T170), A168 (≠ T172), A169 (= A173), G170 (= G174), A171 (≠ S175), I174 (≠ V178)
- binding 6-aminohexanoic acid: G121 (≠ A125), G121 (≠ A125), N122 (≠ T126), S147 (= S151), A168 (≠ T172), A168 (≠ T172), A169 (= A173), A171 (≠ S175), C313 (≠ R295)
Query Sequence
>WP_012760005.1 NCBI__GCF_000023185.1:WP_012760005.1
MLPTILDLSSLRAAYQSGLTPLDAIEEVIARRAASKDPAIFITPVPDDELRAAAKVLMAR
APEANSLPLWGVPFAVKDNIDAAGLPTTAACPAYEYRPEADATVVARLKAAGAIIIGKTN
LDQFATGLNGTRSPYGAPRSVFDAAYISGGSSSGSSVTVASGLAAFALGTDTAGSGRVPA
AFNNLVGIKPTPGLVPNTGAVPACKSVDCITIFAATVGDGVAIRKVAEGFDGADAFSRHA
KPANLPVSGLRIGVLTDAEREFFGDKEVEALYDQAIERAKALGATIVPFDYAPFREAAAL
LYDGPWVAERLAAVETFLATNAADFDPTVRGIIEGAKGKTAVEAFNGRYRLEELRRKTEA
EWEKADVLLLPTAPTTYTVADMLANPVVLNGRLGRYTNFVNLLDCAAIAVPAGFGKDGLP
GGVTVIAPAFTDDALAPLADALHRAAASGMGIDRQAAIPEASRVVPGDDGFIEIAVVGAH
LTGMPLNHELAGSGGRLVKTCRTSGDYRLFVLPNTMPPKPGLLREPGHRGQGLEVEVWAL
PADAFGRFVQKIPAPLGIGKLTLEDGSSVSGFVCEAHGVKGAEEITALGGWRNYISAKLA
S
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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