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Comparing BWI76_RS24025 FitnessBrowser__Koxy:BWI76_RS24025 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)
P60651 Agmatinase; Agmatine ureohydrolase; AUH; EC 3.5.3.11 from Escherichia coli (strain K12) (see paper)
99% identity, 100% coverage: 1:306/306 of query aligns to 1:306/306 of P60651
- H163 (= H163) mutation to F: Loss of activity.
7lbaB E. Coli agmatinase (see paper)
99% identity, 99% coverage: 1:303/306 of query aligns to 8:310/310 of 7lbaB
7lolA The structure of agmatinase from e. Coli at 1.8 a displaying urea and agmatine (see paper)
99% identity, 96% coverage: 11:304/306 of query aligns to 1:294/294 of 7lolA
- binding agmatine: Y145 (= Y155), H153 (= H163)
- binding manganese (ii) ion: H116 (= H126), D139 (= D149), D139 (= D149), H141 (= H151), D143 (= D153), D220 (= D230), D220 (= D230), D222 (= D232)
- binding urea: D143 (= D153), H153 (= H163), D220 (= D230), E264 (= E274)
7loxA The structure of agmatinase from e. Coli at 3.2 a displaying guanidine in the active site (see paper)
97% identity, 95% coverage: 15:304/306 of query aligns to 1:284/284 of 7loxA
- binding guanidine: H106 (= H126), H131 (= H151), H131 (= H151), D133 (= D153), D133 (= D153), H143 (= H163), D210 (= D230)
- binding manganese (ii) ion: H106 (= H126), D129 (= D149), D129 (= D149), H131 (= H151), D133 (= D153), D210 (= D230), D210 (= D230), D212 (= D232)
4dz4B X-ray crystal structure of a hypothetical agmatinase from burkholderia thailandensis (see paper)
51% identity, 86% coverage: 41:304/306 of query aligns to 54:319/323 of 4dz4B
- active site: H138 (= H126), D162 (= D149), H164 (= H151), D166 (= D153), H178 (= H163), D245 (= D230), D247 (= D232), E289 (= E274)
- binding manganese (ii) ion: H138 (= H126), D162 (= D149), D162 (= D149), H164 (= H151), D166 (= D153), D245 (= D230), D245 (= D230), D247 (= D232)
- binding unknown: H138 (= H126), D166 (= D153), H178 (= H163)
3nioA Crystal structure of pseudomonas aeruginosa guanidinobutyrase (see paper)
40% identity, 92% coverage: 19:299/306 of query aligns to 20:309/316 of 3nioA
- active site: H126 (= H126), D149 (= D149), H151 (= H151), D153 (= D153), H165 (= H163), D240 (= D230), D242 (= D232), E284 (= E274)
- binding manganese (ii) ion: H126 (= H126), D149 (= D149), D149 (= D149), H151 (= H151), D153 (= D153), D240 (= D230), D240 (= D230), D242 (= D232)
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)
40% identity, 92% coverage: 19:299/306 of query aligns to 23:312/319 of Q9I3S3
- H129 (= H126) binding
- D152 (= D149) binding ; binding
- H154 (= H151) binding
- D156 (= D153) binding
- M161 (≠ A156) mutation to Y: Loss of activity.
- D243 (= D230) binding
- D245 (= D232) binding
3niqA Crystal structure of pseudomonas aeruginosa guanidinopropionase (see paper)
40% identity, 92% coverage: 19:301/306 of query aligns to 20:308/315 of 3niqA
- active site: H123 (= H126), D145 (= D149), H147 (= H151), D149 (= D153), H162 (= H163), D237 (= D230), D239 (= D232), E281 (= E274)
- binding manganese (ii) ion: H123 (= H126), D145 (= D149), D145 (= D149), H147 (= H151), D149 (= D153), D237 (= D230), D237 (= D230), D239 (= D232)
3nipB Crystal structure of pseudomonas aeruginosa guanidinopropionase complexed with 1,6-diaminohexane (see paper)
40% identity, 92% coverage: 19:301/306 of query aligns to 21:309/316 of 3nipB
- active site: H124 (= H126), D146 (= D149), H148 (= H151), D150 (= D153), H163 (= H163), D238 (= D230), D240 (= D232), E282 (= E274)
- binding hexane-1,6-diamine: R49 (= R49), P244 (= P236), F246 (= F238), P248 (= P240), A292 (≠ I284), V296 (≠ A288)
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)
40% identity, 92% coverage: 19:301/306 of query aligns to 23:311/318 of Q9I6K2
- H126 (= H126) binding
- D148 (= D149) binding
- H150 (= H151) binding
- D152 (= D153) binding
- Y157 (= Y155) mutation to M: Reduces substrate affinity 10-fold and catalytic efficiency 3-fold.
- D240 (= D230) binding
- D242 (= D232) binding
1gq6B Proclavaminate amidino hydrolase from streptomyces clavuligerus (see paper)
40% identity, 92% coverage: 19:298/306 of query aligns to 10:295/301 of 1gq6B
- active site: H113 (= H126), D136 (= D149), H138 (= H151), D140 (= D153), H152 (= H163), D227 (= D230), D229 (= D232), E271 (= E274)
- binding manganese (ii) ion: H113 (= H126), D136 (= D149), D136 (= D149), H138 (= H151), D140 (= D153), D227 (= D230), D227 (= D230), D229 (= D232)
P0DJQ3 Proclavaminate amidinohydrolase; Proclavaminic acid amidino hydrolase; EC 3.5.3.22 from Streptomyces clavuligerus (see paper)
40% identity, 92% coverage: 19:298/306 of query aligns to 18:303/313 of P0DJQ3
- H121 (= H126) binding
- D144 (= D149) binding ; binding
- H146 (= H151) binding
- D148 (= D153) binding
- D235 (= D230) binding ; binding
- D237 (= D232) binding
7esrA Crystal structure of synechocystis sp pcc6803 guanidinium hydrolase (r32) (see paper)
30% identity, 86% coverage: 34:297/306 of query aligns to 76:351/378 of 7esrA
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)
31% identity, 91% coverage: 21:297/306 of query aligns to 10:280/284 of Q57757
- C71 (≠ V86) mutation to S: 24% of wild-type activity in the presence of DTT.
- C136 (≠ T152) mutation to A: 89% of wild-type activity in the presence of DTT.
- C151 (≠ T165) mutation to S: 5% of wild-type activity in the presence of DTT.
- C229 (≠ G248) mutation to A: 96% of wild-type activity in the presence of DTT.
3lhlA Crystal structure of a putative agmatinase from clostridium difficile
28% identity, 89% coverage: 31:303/306 of query aligns to 3:274/276 of 3lhlA
- active site: H95 (= H126), D118 (= D149), H120 (= H151), D122 (= D153), H134 (= H163), D199 (= D230), D201 (= D232), E245 (= E274)
- binding manganese (ii) ion: H95 (= H126), D118 (= D149), D118 (= D149), H120 (= H151), D122 (= D153), D122 (= D153), H134 (= H163), D199 (= D230), D199 (= D230), D201 (= D232)
1wogA Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily (see paper)
31% identity, 91% coverage: 19:297/306 of query aligns to 13:295/303 of 1wogA
- active site: H119 (= H126), D141 (= D149), H143 (= H151), D145 (vs. gap), N157 (≠ H163), D227 (= D230), D229 (= D232), E272 (= E274)
- binding hexane-1,6-diamine: H143 (= H151), D145 (vs. gap), N157 (≠ H163), S158 (≠ G164)
- binding manganese (ii) ion: H119 (= H126), D141 (= D149), D141 (= D149), H143 (= H151), D145 (vs. gap), D227 (= D230), D227 (= D230), D229 (= D232)
1cevA Arginase from bacillus caldovelox, native structure at ph 5.6 (see paper)
29% identity, 84% coverage: 37:292/306 of query aligns to 6:289/299 of 1cevA
- active site: H99 (= H126), D122 (= D149), H124 (= H151), D126 (= D153), H139 (vs. gap), D226 (= D230), D228 (= D232), E271 (= E274)
- binding manganese (ii) ion: H99 (= H126), D122 (= D149), D122 (= D149), H124 (= H151), D126 (= D153), D226 (= D230), D226 (= D230), D228 (= D232)
P53608 Arginase; EC 3.5.3.1 from Bacillus caldovelox (see paper)
29% identity, 84% coverage: 37:292/306 of query aligns to 6:289/299 of P53608
- H99 (= H126) binding
- D122 (= D149) binding ; binding
- H124 (= H151) binding
- HGDVN 124:128 (≠ HTDT- 151:154) binding
- D126 (= D153) binding
- SGN 135:137 (vs. gap) binding
- D178 (vs. gap) binding
- D226 (= D230) binding ; binding
- D228 (= D232) binding
- T240 (= T244) binding
- E271 (= E274) binding
5cevA Arginase from bacillus caldevelox, l-lysine complex (see paper)
29% identity, 84% coverage: 37:292/306 of query aligns to 5:288/298 of 5cevA
- active site: H98 (= H126), D121 (= D149), H123 (= H151), D125 (= D153), H138 (vs. gap), D225 (= D230), D227 (= D232), E270 (= E274)
- binding guanidine: H251 (≠ I256), E255 (≠ R260)
- binding lysine: S134 (vs. gap), H138 (vs. gap), E270 (= E274)
- binding manganese (ii) ion: H98 (= H126), D121 (= D149), D121 (= D149), H123 (= H151), D125 (= D153), D225 (= D230), D225 (= D230), D227 (= D232)
4cevA Arginase from bacillus caldevelox, l-ornithine complex (see paper)
29% identity, 84% coverage: 37:292/306 of query aligns to 5:288/298 of 4cevA
- active site: H98 (= H126), D121 (= D149), H123 (= H151), D125 (= D153), H138 (vs. gap), D225 (= D230), D227 (= D232), E270 (= E274)
- binding guanidine: H251 (≠ I256), E255 (≠ R260)
- binding manganese (ii) ion: H98 (= H126), D121 (= D149), D121 (= D149), H123 (= H151), D125 (= D153), D225 (= D230), D225 (= D230), D227 (= D232)
- binding L-ornithine: H123 (= H151), D125 (= D153), S134 (vs. gap), H138 (vs. gap), D177 (vs. gap)
Query Sequence
>BWI76_RS24025 FitnessBrowser__Koxy:BWI76_RS24025
MSTLGHQYDNSLVSNAFGFLRLPMNFMPYDSDADWVITGVPFDMATSGRAGGRHGPAAIR
QVSTNLAWEHNRFPWNFDMRERLNVVDCGDLVYAFGDAREMSEKLQAHAEKLLAAGKRML
SFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYANGCEFDHGTMFYTAPNEGLIDPHH
SVQIGIRTEFDKDNGFTVLDAGQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAP
GTGTPVIGGLTSDRAIKLVRGLKDLNIVGMDVVEVAPAYDQSEITALAAATLALEMLYIQ
AAKKGE
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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