SitesBLAST
Comparing BWI76_RS21925 FitnessBrowser__Koxy:BWI76_RS21925 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)
Q9I6K2 Guanidinopropionase; EC 3.5.3.17 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
64% identity, 96% coverage: 6:316/323 of query aligns to 2:313/318 of Q9I6K2
- H126 (= H129) binding
- D148 (= D151) binding
- H150 (= H153) binding
- D152 (= D155) binding
- Y157 (= Y160) mutation to M: Reduces substrate affinity 10-fold and catalytic efficiency 3-fold.
- D240 (= D243) binding
- D242 (= D245) binding
3nipB Crystal structure of pseudomonas aeruginosa guanidinopropionase complexed with 1,6-diaminohexane (see paper)
65% identity, 96% coverage: 7:316/323 of query aligns to 1:311/316 of 3nipB
- active site: H124 (= H129), D146 (= D151), H148 (= H153), D150 (= D155), H163 (= H168), D238 (= D243), D240 (= D245), E282 (= E287)
- binding hexane-1,6-diamine: R49 (= R54), P244 (= P249), F246 (≠ Y251), P248 (= P253), A292 (≠ L297), V296 (≠ T301)
3niqA Crystal structure of pseudomonas aeruginosa guanidinopropionase (see paper)
65% identity, 96% coverage: 8:316/323 of query aligns to 1:310/315 of 3niqA
- active site: H123 (= H129), D145 (= D151), H147 (= H153), D149 (= D155), H162 (= H168), D237 (= D243), D239 (= D245), E281 (= E287)
- binding manganese (ii) ion: H123 (= H129), D145 (= D151), D145 (= D151), H147 (= H153), D149 (= D155), D237 (= D243), D237 (= D243), D239 (= D245)
Q9I3S3 Guanidinobutyrase; EC 3.5.3.7 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
47% identity, 95% coverage: 6:313/323 of query aligns to 2:313/319 of Q9I3S3
- H129 (= H129) binding
- D152 (= D151) binding ; binding
- H154 (= H153) binding
- D156 (= D155) binding
- M161 (≠ Y160) mutation to Y: Loss of activity.
- D243 (= D243) binding
- D245 (= D245) binding
3nioA Crystal structure of pseudomonas aeruginosa guanidinobutyrase (see paper)
47% identity, 95% coverage: 8:313/323 of query aligns to 1:310/316 of 3nioA
- active site: H126 (= H129), D149 (= D151), H151 (= H153), D153 (= D155), H165 (= H168), D240 (= D243), D242 (= D245), E284 (= E287)
- binding manganese (ii) ion: H126 (= H129), D149 (= D151), D149 (= D151), H151 (= H153), D153 (= D155), D240 (= D243), D240 (= D243), D242 (= D245)
P0DJQ3 Proclavaminate amidinohydrolase; Proclavaminic acid amidino hydrolase; EC 3.5.3.22 from Streptomyces clavuligerus (see paper)
39% identity, 94% coverage: 18:321/323 of query aligns to 10:313/313 of P0DJQ3
- H121 (= H129) binding
- D144 (= D151) binding ; binding
- H146 (= H153) binding
- D148 (= D155) binding
- D235 (= D243) binding ; binding
- D237 (= D245) binding
1gq6B Proclavaminate amidino hydrolase from streptomyces clavuligerus (see paper)
39% identity, 93% coverage: 18:317/323 of query aligns to 2:301/301 of 1gq6B
- active site: H113 (= H129), D136 (= D151), H138 (= H153), D140 (= D155), H152 (= H168), D227 (= D243), D229 (= D245), E271 (= E287)
- binding manganese (ii) ion: H113 (= H129), D136 (= D151), D136 (= D151), H138 (= H153), D140 (= D155), D227 (= D243), D227 (= D243), D229 (= D245)
7lbaB E. Coli agmatinase (see paper)
41% identity, 88% coverage: 26:310/323 of query aligns to 26:304/310 of 7lbaB
7lolA The structure of agmatinase from e. Coli at 1.8 a displaying urea and agmatine (see paper)
41% identity, 88% coverage: 26:310/323 of query aligns to 9:287/294 of 7lolA
- binding agmatine: Y145 (= Y160), H153 (= H168)
- binding manganese (ii) ion: H116 (= H129), D139 (= D151), D139 (= D151), H141 (= H153), D143 (= D155), D220 (= D243), D220 (= D243), D222 (= D245)
- binding urea: D143 (= D155), H153 (= H168), D220 (= D243), E264 (= E287)
P60651 Agmatinase; Agmatine ureohydrolase; AUH; EC 3.5.3.11 from Escherichia coli (strain K12) (see paper)
41% identity, 88% coverage: 26:310/323 of query aligns to 19:297/306 of P60651
- H163 (= H168) mutation to F: Loss of activity.
7loxA The structure of agmatinase from e. Coli at 3.2 a displaying guanidine in the active site (see paper)
40% identity, 88% coverage: 26:310/323 of query aligns to 5:277/284 of 7loxA
- binding guanidine: H106 (= H129), H131 (= H153), H131 (= H153), D133 (= D155), D133 (= D155), H143 (= H168), D210 (= D243)
- binding manganese (ii) ion: H106 (= H129), D129 (= D151), D129 (= D151), H131 (= H153), D133 (= D155), D210 (= D243), D210 (= D243), D212 (= D245)
4dz4B X-ray crystal structure of a hypothetical agmatinase from burkholderia thailandensis (see paper)
38% identity, 90% coverage: 20:311/323 of query aligns to 28:313/323 of 4dz4B
- active site: H138 (= H129), D162 (= D151), H164 (= H153), D166 (= D155), H178 (= H168), D245 (= D243), D247 (= D245), E289 (= E287)
- binding manganese (ii) ion: H138 (= H129), D162 (= D151), D162 (= D151), H164 (= H153), D166 (= D155), D245 (= D243), D245 (= D243), D247 (= D245)
- binding unknown: H138 (= H129), D166 (= D155), H178 (= H168)
7esrA Crystal structure of synechocystis sp pcc6803 guanidinium hydrolase (r32) (see paper)
31% identity, 96% coverage: 6:314/323 of query aligns to 40:355/378 of 7esrA
1wogA Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily (see paper)
31% identity, 92% coverage: 20:315/323 of query aligns to 7:300/303 of 1wogA
- active site: H119 (= H129), D141 (= D151), H143 (= H153), D145 (= D155), N157 (≠ H168), D227 (= D243), D229 (= D245), E272 (= E287)
- binding hexane-1,6-diamine: H143 (= H153), D145 (= D155), N157 (≠ H168), S158 (≠ G169)
- binding manganese (ii) ion: H119 (= H129), D141 (= D151), D141 (= D151), H143 (= H153), D145 (= D155), D227 (= D243), D227 (= D243), D229 (= D245)
3lhlA Crystal structure of a putative agmatinase from clostridium difficile
27% identity, 86% coverage: 37:315/323 of query aligns to 4:273/276 of 3lhlA
- active site: H95 (= H129), D118 (= D151), H120 (= H153), D122 (= D155), H134 (= H168), D199 (= D243), D201 (= D245), E245 (= E287)
- binding manganese (ii) ion: H95 (= H129), D118 (= D151), D118 (= D151), H120 (= H153), D122 (= D155), D122 (= D155), H134 (= H168), D199 (= D243), D199 (= D243), D201 (= D245)
Q57757 Agmatinase; EC 3.5.3.11 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
30% identity, 84% coverage: 42:313/323 of query aligns to 25:283/284 of Q57757
- C71 (≠ G89) mutation to S: 24% of wild-type activity in the presence of DTT.
- C136 (≠ S154) mutation to A: 89% of wild-type activity in the presence of DTT.
- C151 (≠ T170) mutation to S: 5% of wild-type activity in the presence of DTT.
- C229 (≠ G261) mutation to A: 96% of wild-type activity in the presence of DTT.
1cevA Arginase from bacillus caldovelox, native structure at ph 5.6 (see paper)
31% identity, 85% coverage: 40:312/323 of query aligns to 4:296/299 of 1cevA
- active site: H99 (= H129), D122 (= D151), H124 (= H153), D126 (= D155), H139 (= H168), D226 (= D243), D228 (= D245), E271 (= E287)
- binding manganese (ii) ion: H99 (= H129), D122 (= D151), D122 (= D151), H124 (= H153), D126 (= D155), D226 (= D243), D226 (= D243), D228 (= D245)
P53608 Arginase; EC 3.5.3.1 from Bacillus caldovelox (see paper)
31% identity, 85% coverage: 40:312/323 of query aligns to 4:296/299 of P53608
5cevA Arginase from bacillus caldevelox, l-lysine complex (see paper)
31% identity, 85% coverage: 40:312/323 of query aligns to 3:295/298 of 5cevA
- active site: H98 (= H129), D121 (= D151), H123 (= H153), D125 (= D155), H138 (= H168), D225 (= D243), D227 (= D245), E270 (= E287)
- binding guanidine: H251 (≠ Q269), E255 (≠ R273)
- binding lysine: S134 (≠ E164), H138 (= H168), E270 (= E287)
- binding manganese (ii) ion: H98 (= H129), D121 (= D151), D121 (= D151), H123 (= H153), D125 (= D155), D225 (= D243), D225 (= D243), D227 (= D245)
4cevA Arginase from bacillus caldevelox, l-ornithine complex (see paper)
31% identity, 85% coverage: 40:312/323 of query aligns to 3:295/298 of 4cevA
- active site: H98 (= H129), D121 (= D151), H123 (= H153), D125 (= D155), H138 (= H168), D225 (= D243), D227 (= D245), E270 (= E287)
- binding guanidine: H251 (≠ Q269), E255 (≠ R273)
- binding manganese (ii) ion: H98 (= H129), D121 (= D151), D121 (= D151), H123 (= H153), D125 (= D155), D225 (= D243), D225 (= D243), D227 (= D245)
- binding L-ornithine: H123 (= H153), D125 (= D155), S134 (≠ E164), H138 (= H168), D177 (≠ S197)
Query Sequence
>BWI76_RS21925 FitnessBrowser__Koxy:BWI76_RS21925
MTTATEKNYPQPQDGEIPRFSGLPTFFRLPFAPQAAELDIGIVGVPWDGGTTNRAGTRHG
PRELRNASSLVRRIHQTTRRSPYDYARVGDLGDVRINPVDMQDSLARIEAWYRALAEQQV
MPLTAGGDHLTTLPILRALGRDKPLGMIHFDAHSDTNDSYFGGERFTHGTPFRRAVEEGV
LDPRRTVQIGIRGALFSADEHCWAEENGITIIRMEQVDELGIDKVMQRARAIVGEQPTYI
SFDIDVLDPVYAPGTGTPEIGGMTTLQAQRCVRQLAGLNLIGADVVEVSPPFDQGNLTSL
TGATMMFELLCQLADAHHWRISL
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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