SitesBLAST
Comparing WP_015886695.1 NCBI__GCF_000018545.1:WP_015886695.1 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)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
35% identity, 97% coverage: 15:485/486 of query aligns to 21:496/507 of Q84DC4
- T31 (≠ A25) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K93) mutation to A: Abolishes activity on mandelamide.
- S180 (= S168) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S169) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ V190) 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 (= S192) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V195) 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 (≠ T309) 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 (≠ E367) 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 (≠ L426) 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.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 92% coverage: 31:476/486 of query aligns to 14:466/478 of 3h0mA
- active site: K72 (= K93), S147 (= S168), S148 (= S169), S166 (≠ G187), T168 (= T189), G169 (≠ V190), G170 (= G191), S171 (= S192), Q174 (≠ V195)
- binding glutamine: M122 (≠ Y143), G123 (= G144), D167 (= D188), T168 (= T189), G169 (≠ V190), G170 (= G191), S171 (= S192), F199 (≠ I220), Y302 (≠ I316), R351 (≠ A352), D418 (= D423)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 92% coverage: 31:476/486 of query aligns to 14:466/478 of 3h0lA
- active site: K72 (= K93), S147 (= S168), S148 (= S169), S166 (≠ G187), T168 (= T189), G169 (≠ V190), G170 (= G191), S171 (= S192), Q174 (≠ V195)
- binding asparagine: G123 (= G144), S147 (= S168), G169 (≠ V190), G170 (= G191), S171 (= S192), Y302 (≠ I316), R351 (≠ A352), D418 (= D423)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 92% coverage: 31:476/486 of query aligns to 20:473/485 of 2f2aA
- active site: K79 (= K93), S154 (= S168), S155 (= S169), S173 (≠ G187), T175 (= T189), G176 (≠ V190), G177 (= G191), S178 (= S192), Q181 (≠ V195)
- binding glutamine: G130 (= G144), S154 (= S168), D174 (= D188), T175 (= T189), G176 (≠ V190), S178 (= S192), F206 (≠ I220), Y309 (≠ T313), Y310 (≠ W314), R358 (= R350), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 92% coverage: 31:476/486 of query aligns to 20:473/485 of 2dqnA
- active site: K79 (= K93), S154 (= S168), S155 (= S169), S173 (≠ G187), T175 (= T189), G176 (≠ V190), G177 (= G191), S178 (= S192), Q181 (≠ V195)
- binding asparagine: M129 (≠ Y143), G130 (= G144), T175 (= T189), G176 (≠ V190), S178 (= S192), Y309 (≠ T313), Y310 (≠ W314), R358 (= R350), D425 (vs. gap)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
29% identity, 93% coverage: 24:476/486 of query aligns to 8:476/487 of 1m21A
- active site: K81 (= K93), S160 (= S168), S161 (= S169), T179 (≠ G187), T181 (= T189), D182 (≠ V190), G183 (= G191), S184 (= S192), C187 (≠ V195)
- binding : A129 (≠ S142), N130 (≠ Y143), F131 (vs. gap), C158 (≠ G166), G159 (= G167), S160 (= S168), S184 (= S192), C187 (≠ V195), I212 (= I220), R318 (≠ W314), L321 (≠ F317), L365 (≠ V357), F426 (= F414)
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 93% coverage: 29:478/486 of query aligns to 7:456/468 of 3kfuE
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
28% identity, 74% coverage: 116:476/486 of query aligns to 229:588/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ S142), G302 (≠ T189), G303 (≠ V190), G304 (= G191), A305 (≠ S192), V442 (≠ I316), I475 (≠ V357), M539 (≠ A427)
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
28% identity, 74% coverage: 116:476/486 of query aligns to 229:588/605 of 8ey1D
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 83% coverage: 81:485/486 of query aligns to 83:506/508 of 3a1iA
- active site: K95 (= K93), S170 (= S168), S171 (= S169), G189 (= G187), Q191 (≠ T189), G192 (≠ V190), G193 (= G191), A194 (≠ S192), I197 (≠ V195)
- binding benzamide: F145 (≠ Y143), S146 (≠ G144), G147 (≠ L145), Q191 (≠ T189), G192 (≠ V190), G193 (= G191), A194 (≠ S192), W327 (= W314)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 84% coverage: 65:473/486 of query aligns to 63:458/605 of Q936X2
- K91 (= K93) mutation to A: Loss of activity.
- S165 (= S168) mutation to A: Loss of activity.
- S189 (= S192) mutation to A: Loss of activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
31% identity, 55% coverage: 29:293/486 of query aligns to 12:288/457 of 5h6sC
- active site: K77 (= K93), S152 (= S168), S153 (= S169), L173 (≠ T189), G174 (≠ V190), G175 (= G191), S176 (= S192)
- binding 4-oxidanylbenzohydrazide: C126 (≠ S142), R128 (≠ G144), W129 (≠ L145), S152 (= S168), L173 (≠ T189), G174 (≠ V190), S176 (= S192)
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
42% identity, 45% coverage: 23:239/486 of query aligns to 9:221/457 of 6c6gA
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 86% coverage: 67:486/486 of query aligns to 48:456/461 of 4gysB
- active site: K72 (= K93), S146 (= S168), S147 (= S169), T165 (≠ G187), T167 (= T189), A168 (≠ V190), G169 (= G191), S170 (= S192), V173 (= V195)
- binding malonate ion: A120 (≠ S142), G122 (= G144), S146 (= S168), T167 (= T189), A168 (≠ V190), S170 (= S192), S193 (≠ N215), G194 (= G216), V195 (= V217), R200 (≠ H222), Y297 (≠ E310), R305 (≠ T321)
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, 80% coverage: 85:471/486 of query aligns to 28:417/425 of Q9FR37
- K36 (= K93) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S168) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S169) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D188) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S192) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C200) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ Y265) mutation to T: Slightly reduces catalytic activity.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
41% identity, 30% coverage: 116:259/486 of query aligns to 229:369/616 of 6diiH
Sites not aligning to the query:
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
41% identity, 30% coverage: 116:259/486 of query aligns to 229:369/607 of Q7XJJ7
- SS 281:282 (= SS 168:169) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TVGS 189:192) binding substrate
- S305 (= S192) mutation to A: Loss of activity.
- R307 (= R194) mutation to A: Loss of activity.
- S360 (≠ T250) mutation to A: No effect.
Sites not aligning to the query:
- 205 K→A: Loss of activity.
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 84% coverage: 74:479/486 of query aligns to 43:410/412 of 1ocmA
- active site: K62 (= K93), S131 (= S168), S132 (= S169), T152 (= T189), G153 (≠ V190), G154 (= G191), S155 (= S192)
- binding pyrophosphate 2-: R113 (≠ N149), S131 (= S168), Q151 (≠ D188), T152 (= T189), G153 (≠ V190), G154 (= G191), S155 (= S192), R158 (≠ V195), P359 (≠ Q419)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 84% coverage: 74:479/486 of query aligns to 43:410/412 of 1o9oA
- active site: K62 (= K93), A131 (≠ S168), S132 (= S169), T150 (≠ G187), T152 (= T189), G153 (≠ V190), G154 (= G191), S155 (= S192), R158 (≠ V195)
- binding 3-amino-3-oxopropanoic acid: G130 (= G167), T152 (= T189), G153 (≠ V190), G154 (= G191), S155 (= S192), R158 (≠ V195), P359 (≠ Q419)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
39% identity, 36% coverage: 60:234/486 of query aligns to 5:182/450 of 4n0iA
- active site: K38 (= K93), S116 (= S168), S117 (= S169), T135 (≠ G187), T137 (= T189), G138 (≠ V190), G139 (= G191), S140 (= S192), L143 (≠ V195)
- binding glutamine: G89 (= G144), T137 (= T189), G138 (≠ V190), S140 (= S192), Y168 (≠ I220)
Sites not aligning to the query:
Query Sequence
>WP_015886695.1 NCBI__GCF_000018545.1:WP_015886695.1
MHENEAFVRTALELEADGLTGLGVAAAAAAIRNGDISSESYTAALLQRARTHSDLNAFIT
IDETAALAAARNADKARAAGSNASLLGVPLAVKDSYLTKGLRTTLGVRNLEGFVPEEDAV
VVGAIKDAGGVVFGKNNLVEMSYGLTGNNEPYGQVKNPHERNHVTGGSSSGGGASVAARI
VPAALGGDTVGSIRVPASLCGVVGFKPTTGRWPGNGVAPISHTLDTTGVLARNVEDCALI
DQIVTKAEATGRSDRSDLKGVRLAYAPRQYLDLVDPEIEVHFNETVRRLRETGAEIVAID
LGEDFSSITERATWNIFFHETMEAISGFLHHNRVPTSFDAIYDGLKPGLREAWGNVVLPS
GPGYSRETYEAALSLDRPEIQRRFSEAFTRSGAVALLFPTTPCTAPLIEHQSRFSIADQE
VSDLVLAKNTIAASAAGLPGISIPTGLSRNGLPIGLEIDGAHGRDRSLLELARLVEAAVG
ALPSPV
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