SitesBLAST
Comparing WP_012334347.1 NCBI__GCF_000019365.1:WP_012334347.1 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)
30% identity, 96% coverage: 20:471/473 of query aligns to 6:476/478 of 3h0mA
- active site: K72 (= K92), S147 (= S169), S148 (= S170), S166 (≠ T188), T168 (= T190), G169 (= G191), G170 (= G192), S171 (= S193), Q174 (≠ L196)
- binding glutamine: M122 (≠ F142), G123 (= G143), D167 (= D189), T168 (= T190), G169 (= G191), G170 (= G192), S171 (= S193), F199 (≠ L221), Y302 (≠ A324), R351 (= R354), D418 (≠ S412)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 96% coverage: 20:471/473 of query aligns to 6:476/478 of 3h0lA
- active site: K72 (= K92), S147 (= S169), S148 (= S170), S166 (≠ T188), T168 (= T190), G169 (= G191), G170 (= G192), S171 (= S193), Q174 (≠ L196)
- binding asparagine: G123 (= G143), S147 (= S169), G169 (= G191), G170 (= G192), S171 (= S193), Y302 (≠ A324), R351 (= R354), D418 (≠ S412)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 95% coverage: 20:467/473 of query aligns to 7:479/485 of 2f2aA
- active site: K79 (= K92), S154 (= S169), S155 (= S170), S173 (≠ T188), T175 (= T190), G176 (= G191), G177 (= G192), S178 (= S193), Q181 (≠ L196)
- binding glutamine: G130 (= G143), S154 (= S169), D174 (= D189), T175 (= T190), G176 (= G191), S178 (= S193), F206 (≠ L221), Y309 (≠ A324), Y310 (≠ A325), R358 (= R354), D425 (≠ S412)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 95% coverage: 20:467/473 of query aligns to 7:479/485 of 2dqnA
- active site: K79 (= K92), S154 (= S169), S155 (= S170), S173 (≠ T188), T175 (= T190), G176 (= G191), G177 (= G192), S178 (= S193), Q181 (≠ L196)
- binding asparagine: M129 (≠ F142), G130 (= G143), T175 (= T190), G176 (= G191), S178 (= S193), Y309 (≠ A324), Y310 (≠ A325), R358 (= R354), D425 (≠ S412)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 93% coverage: 25:462/473 of query aligns to 135:589/607 of Q7XJJ7
- K205 (= K92) mutation to A: Loss of activity.
- SS 281:282 (= SS 169:170) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 190:193) binding substrate
- S305 (= S193) mutation to A: Loss of activity.
- R307 (= R195) mutation to A: Loss of activity.
- S360 (≠ P248) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 93% coverage: 25:462/473 of query aligns to 135:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A141), T258 (≠ G144), S281 (= S169), G302 (≠ T190), G303 (= G191), S305 (= S193), S472 (≠ R354), I532 (vs. gap), M539 (≠ T415)
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
29% identity, 93% coverage: 25:462/473 of query aligns to 135:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A141), G302 (≠ T190), G303 (= G191), G304 (= G192), A305 (≠ S193), V442 (≠ I327), I475 (≠ S357), M539 (≠ T415)
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
29% identity, 93% coverage: 25:462/473 of query aligns to 135:589/605 of 8ey1D
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 94% coverage: 19:461/473 of query aligns to 1:448/457 of 6c6gA
3kfuE Crystal structure of the transamidosome (see paper)
34% identity, 93% coverage: 24:464/473 of query aligns to 1:457/468 of 3kfuE
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 81% coverage: 82:462/473 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K92), S170 (= S169), S171 (= S170), G189 (≠ T188), Q191 (≠ T190), G192 (= G191), G193 (= G192), A194 (≠ S193), I197 (≠ L196)
- binding benzamide: F145 (= F142), S146 (≠ G143), G147 (= G144), Q191 (≠ T190), G192 (= G191), G193 (= G192), A194 (≠ S193), W327 (vs. gap)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 95% coverage: 22:472/473 of query aligns to 9:485/487 of 1m21A
- active site: K81 (= K92), S160 (= S169), S161 (= S170), T179 (= T188), T181 (= T190), D182 (≠ G191), G183 (= G192), S184 (= S193), C187 (≠ L196)
- binding : A129 (= A141), N130 (vs. gap), F131 (vs. gap), C158 (≠ G167), G159 (= G168), S160 (= S169), S184 (= S193), C187 (≠ L196), I212 (≠ L221), R318 (vs. gap), L321 (vs. gap), L365 (≠ V351), F426 (≠ V410)
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)
45% identity, 36% coverage: 84:253/473 of query aligns to 28:197/425 of Q9FR37
- K36 (= K92) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S169) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S170) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D189) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S193) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C201) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
41% identity, 49% coverage: 18:250/473 of query aligns to 30:261/507 of Q84DC4
- T31 (≠ M19) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K92) mutation to A: Abolishes activity on mandelamide.
- S180 (= S169) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S170) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G191) 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 (= S193) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ L196) 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.
Sites not aligning to the query:
- 316 S→N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- 382 Q→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.
- 437 I→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.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
33% identity, 85% coverage: 73:472/473 of query aligns to 52:443/461 of 4gysB
- active site: K72 (= K92), S146 (= S169), S147 (= S170), T165 (= T188), T167 (= T190), A168 (≠ G191), G169 (= G192), S170 (= S193), V173 (≠ L196)
- binding malonate ion: A120 (= A141), G122 (= G143), S146 (= S169), T167 (= T190), A168 (≠ G191), S170 (= S193), S193 (≠ A216), G194 (= G217), V195 (= V218), R200 (≠ T223), Y297 (≠ N329), R305 (vs. gap)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 90% coverage: 37:462/473 of query aligns to 37:462/605 of Q936X2
- K91 (= K92) mutation to A: Loss of activity.
- S165 (= S169) mutation to A: Loss of activity.
- S189 (= S193) mutation to A: Loss of activity.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 95% coverage: 20:466/473 of query aligns to 7:478/490 of 4yjiA
- active site: K79 (= K92), S158 (= S169), S159 (= S170), G179 (≠ T190), G180 (= G191), G181 (= G192), A182 (≠ S193)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L94), G132 (≠ A141), S158 (= S169), G179 (≠ T190), G180 (= G191), A182 (≠ S193)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 90% coverage: 37:462/473 of query aligns to 23:445/457 of 5h6sC
- active site: K77 (= K92), S152 (= S169), S153 (= S170), L173 (≠ T190), G174 (= G191), G175 (= G192), S176 (= S193)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A141), R128 (≠ G143), W129 (≠ G144), S152 (= S169), L173 (≠ T190), G174 (= G191), S176 (= S193), W306 (≠ G306), F338 (= F343)
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
40% identity, 37% coverage: 90:262/473 of query aligns to 67:240/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
31% identity, 49% coverage: 84:315/473 of query aligns to 30:262/450 of 4n0iA
- active site: K38 (= K92), S116 (= S169), S117 (= S170), T135 (= T188), T137 (= T190), G138 (= G191), G139 (= G192), S140 (= S193), L143 (= L196)
- binding glutamine: G89 (= G143), T137 (= T190), G138 (= G191), S140 (= S193), Y168 (≠ L221)
Sites not aligning to the query:
Query Sequence
>WP_012334347.1 NCBI__GCF_000019365.1:WP_012334347.1
MTDALPTDALPRETDPALMSAASLARAIAARRLSPVDAVEALLARIDRLEPRLHAFVEVY
AADARLAAEGAERAIRSGHAVGPLHGVPVALKDLIDVEGRISTGGSMTRRVQRATASATV
AKRMIAQGMILLGKTHTVEFAFGGWGTNQHMGTPLNPWDPARPRVPGGSSSGSGVAVASR
MAPWAIGTDTGGSVRLPASFCGITGLKVTVGRVSTAGVLPLSTTLDTPGPMARSVEDVAL
LYNVLQGPDPLDPNTRGVVPVDPLPGLERGVRGMRLGRMPAAEREGCAPEMLAAYDRALD
LVDRLGAEIVDTRLPFRFVDFVNAAAIVNAEAYFHNGAIAEDFAAPLDEDVRARILSGAS
VSARDYLRTRRLQQDMKRAFDRAMAGLDALLTPTTETAAIPLDAVDQAVVPSRFTRFGNF
LELCALALPCGFTAEGLPLSLQIACRGYEEATALRIGQAYQQATDWHGRLPPL
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