SitesBLAST
Comparing WP_013011785.1 NCBI__GCF_000025725.1:WP_013011785.1 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)
A8B2U2 Fructose-bisphosphate aldolase; Glfba; glFBPA; Fructose-1,6-bisphosphate aldolase; EC 4.1.2.13 from Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) (see 4 papers)
49% identity, 97% coverage: 10:322/322 of query aligns to 3:307/323 of A8B2U2
- S50 (= S57) binding beta-D-fructose 1,6-bisphosphate
- D83 (= D94) active site, Proton donor; mutation to A: Severe loss of catalytic activity.
- H84 (= H95) binding Zn(2+)
- H178 (= H190) binding beta-D-fructose 1,6-bisphosphate; binding Zn(2+)
- G179 (= G191) binding beta-D-fructose 1,6-bisphosphate
- K182 (= K194) binding beta-D-fructose 1,6-bisphosphate
- H210 (= H224) binding Zn(2+)
- G211 (= G225) binding beta-D-fructose 1,6-bisphosphate
- S213 (= S227) binding beta-D-fructose 1,6-bisphosphate
- N253 (= N267) binding beta-D-fructose 1,6-bisphosphate
- D255 (= D269) binding beta-D-fructose 1,6-bisphosphate; mutation to A: 9.4-fold reduction in substrate affinity and 50-fold reduction in catalytic affinity. Has some activity towards tagatose-1,6-bisphosphate.
- S256 (= S270) binding beta-D-fructose 1,6-bisphosphate
- R259 (= R273) binding beta-D-fructose 1,6-bisphosphate; mutation to A: 1.8-fold reduction in substrate affinity and 2.8-fold reduction in catalytic efficiency. 6-fold reduction in substrate affinity and 24-fold reduction in catalytic efficiency; when associated with A-278.
- D278 (= D292) mutation to A: 159-fold reduction in substrate affinity and 2770-fold reduction in catalytic efficiency. 6-fold reduction in substrate affinity and 24-fold reduction in catalytic efficiency; when associated with A-259.
- R280 (= R294) binding beta-D-fructose 1,6-bisphosphate
3ohiA Structure of giardia fructose-1,6-biphosphate aldolase in complex with 3-hydroxy-2-pyridone (see paper)
48% identity, 97% coverage: 10:322/322 of query aligns to 2:303/319 of 3ohiA
- binding ({3-hydroxy-2-oxo-4-[2-(phosphonooxy)ethyl]pyridin-1(2H)-yl}methyl)phosphonic acid: S49 (= S57), D82 (= D94), H83 (= H95), H174 (= H190), G175 (= G191), K178 (= K194), G207 (= G225), S209 (= S227), N249 (= N267), D251 (= D269), S252 (= S270), R255 (= R273)
- binding zinc ion: H83 (= H95), H174 (= H190), H206 (= H224)
3gayA Structure of giardia fructose-1,6-biphosphate aldolase in complex with tagatose-1,6-biphosphate (see paper)
48% identity, 97% coverage: 10:322/322 of query aligns to 2:303/319 of 3gayA
- binding 1,6-di-O-phosphono-D-tagatose: N23 (= N31), S49 (= S57), D82 (= D94), H174 (= H190), G175 (= G191), K178 (= K194), H206 (= H224), G207 (= G225), S209 (= S227), N249 (= N267), D251 (= D269), S252 (= S270), R255 (= R273)
- binding zinc ion: H83 (= H95), H174 (= H190), H206 (= H224)
3gb6A Structure of giardia fructose-1,6-biphosphate aldolase d83a mutant in complex with fructose-1,6-bisphosphate (see paper)
48% identity, 97% coverage: 10:322/322 of query aligns to 2:302/318 of 3gb6A
- binding 1,6-di-O-phosphono-D-fructose: N23 (= N31), S49 (= S57), H173 (= H190), G174 (= G191), K177 (= K194), H205 (= H224), G206 (= G225), S208 (= S227), N248 (= N267), D250 (= D269), S251 (= S270), R254 (= R273)
2isvB Structure of giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
46% identity, 97% coverage: 10:322/322 of query aligns to 2:292/307 of 2isvB
- binding phosphoglycolohydroxamic acid: D82 (= D94), H168 (= H190), G169 (= G191), K172 (= K194), H195 (= H224), G196 (= G225), S198 (= S227), N238 (= N267), D240 (= D269), S241 (= S270)
- binding zinc ion: H83 (= H95), H168 (= H190), H195 (= H224)
2isvA Structure of giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
46% identity, 97% coverage: 10:322/322 of query aligns to 2:283/298 of 2isvA
1rv8B Class ii fructose-1,6-bisphosphate aldolase from thermus aquaticus in complex with cobalt (see paper)
45% identity, 97% coverage: 10:322/322 of query aligns to 2:305/305 of 1rv8B
- active site: D80 (= D94), H81 (= H95), E140 (= E154), H178 (= H190), H208 (= H224), N251 (= N267)
- binding cobalt (ii) ion: H81 (= H95), E132 (= E146), H178 (= H190), H208 (= H224)
- binding sulfate ion: R116 (≠ K130), H123 (= H137), S211 (= S227), D253 (= D269), T254 (≠ S270)
3n9sA Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with n-(4-hydroxybutyl)- glycolohydroxamic acid bis- phosphate, a competitive inhibitor (see paper)
44% identity, 97% coverage: 10:321/322 of query aligns to 2:306/307 of 3n9sA
- active site: C69 (≠ K81), E70 (= E82), G136 (= G148), H180 (= H190), A226 (≠ Y240), N253 (= N267)
- binding calcium ion: D104 (= D116), S106 (= S118), E134 (= E146)
- binding 4-{hydroxy[(phosphonooxy)acetyl]amino}butyl dihydrogen phosphate: N23 (= N31), S49 (= S57), D82 (= D94), H83 (= H95), H180 (= H190), G181 (= G191), K184 (= K194), H210 (= H224), G211 (= G225), S213 (= S227), N253 (= N267), D255 (= D269), T256 (≠ S270)
- binding zinc ion: H83 (= H95), H180 (= H190), H210 (= H224)
3q94A The crystal structure of fructose 1,6-bisphosphate aldolase from bacillus anthracis str. 'Ames ancestor'
41% identity, 97% coverage: 10:322/322 of query aligns to 3:285/285 of 3q94A
- active site: D85 (= D94), H86 (= H95), E145 (= E154), H181 (= H190), H209 (= H224), N231 (= N267)
- binding zinc ion: H86 (= H95), E114 (= E123), H163 (≠ E172), H181 (= H190), H209 (= H224), E235 (≠ D271), E239 (≠ A275)
3n9rA Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with n-(4-hydroxybutyl)-phosphoglycolohydroxamic acid, a competitive inhibitor (see paper)
42% identity, 97% coverage: 10:321/322 of query aligns to 2:296/297 of 3n9rA
- active site: C69 (≠ K81), E70 (= E82), G136 (= G148), H170 (= H190), A216 (≠ Y240), N243 (= N267)
- binding 2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate: H83 (= H95), H170 (= H190), G171 (= G191), K174 (= K194), H200 (= H224), G201 (= G225), S203 (= S227), N243 (= N267), D245 (= D269), T246 (≠ S270)
- binding zinc ion: H83 (= H95), H170 (= H190), H200 (= H224)
3c56A Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with n-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate, a competitive inhibitor (see paper)
42% identity, 97% coverage: 10:321/322 of query aligns to 2:296/297 of 3c56A
- active site: C69 (≠ K81), E70 (= E82), G136 (= G148), H170 (= H190), A216 (≠ Y240), N243 (= N267)
- binding 3-{hydroxy[(phosphonooxy)acetyl]amino}propyl dihydrogen phosphate: N23 (= N31), S49 (= S57), D82 (= D94), H170 (= H190), K174 (= K194), G201 (= G225), S203 (= S227), N243 (= N267), D245 (= D269), T246 (≠ S270), R249 (= R273)
- binding zinc ion: H83 (= H95), H170 (= H190), H200 (= H224)
3c52A Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with phosphoglycolohydroxamic acid, a competitive inhibitor (see paper)
42% identity, 97% coverage: 10:321/322 of query aligns to 2:295/296 of 3c52A
- active site: C69 (≠ K81), E70 (= E82), G136 (= G148), H169 (= H190), A215 (≠ Y240), N242 (= N267)
- binding calcium ion: D104 (= D116), S106 (= S118), E134 (= E146)
- binding phosphoglycolohydroxamic acid: D82 (= D94), H83 (= H95), H169 (= H190), K173 (= K194), H199 (= H224), G200 (= G225), S202 (= S227), N242 (= N267), D244 (= D269), T245 (≠ S270)
- binding zinc ion: H83 (= H95), H169 (= H190), H199 (= H224)
5uckA Class ii fructose-1,6-bisphosphate aldolase of helicobacter pylori with cleavage products (see paper)
42% identity, 97% coverage: 10:321/322 of query aligns to 2:290/291 of 5uckA
- binding glyceraldehyde-3-phosphate: S49 (= S57), D82 (= D94), H83 (= H95), H164 (= H190), D239 (= D269), R243 (= R273)
- binding zinc ion: H83 (= H95), H83 (= H95), E134 (= E146), H164 (= H190), H194 (= H224), H194 (= H224)
5ucpA Class ii fructose-1,6-bisphosphate aldolase e142a variant of helicobacter pylori with fbp and cleavage products (see paper)
41% identity, 97% coverage: 10:321/322 of query aligns to 2:291/292 of 5ucpA
- binding 1,6-di-O-phosphono-D-fructose: S49 (= S57), D82 (= D94), H83 (= H95), H165 (= H190), K169 (= K194), G196 (= G225), S198 (= S227), N238 (= N267), D240 (= D269), T241 (≠ S270), R244 (= R273)
- binding zinc ion: H83 (= H95), H83 (= H95), H83 (= H95), E134 (= E146), H165 (= H190), H165 (= H190), H165 (= H190), H195 (= H224), H195 (= H224)
4to8A Methicillin-resistant staphylococcus aureus class iib fructose 1,6- bisphosphate aldolase (see paper)
41% identity, 97% coverage: 10:322/322 of query aligns to 2:277/279 of 4to8A
5ud4A Class ii fructose-1,6-bisphosphate aldolase h180q variant of helicobacter pylori with tbp (see paper)
41% identity, 97% coverage: 10:321/322 of query aligns to 2:292/293 of 5ud4A
- binding 1,6-di-O-phosphono-D-tagatose: S49 (= S57), D82 (= D94), Q166 (≠ H190), G167 (= G191), K170 (= K194), G197 (= G225), S199 (= S227), N239 (= N267), D241 (= D269), T242 (≠ S270), R245 (= R273)
- binding zinc ion: H83 (= H95), H83 (= H95), E134 (= E146), H196 (= H224), H196 (= H224)
P13243 Probable fructose-bisphosphate aldolase; FBP aldolase; FBPA; Fructose-1,6-bisphosphate aldolase; EC 4.1.2.13 from Bacillus subtilis (strain 168) (see paper)
40% identity, 97% coverage: 10:322/322 of query aligns to 3:285/285 of P13243
- T212 (≠ S227) modified: Phosphothreonine
- T234 (≠ S270) modified: Phosphothreonine
5ud0A Class ii fructose-1,6-bisphosphate aldolase e149a variant of helicobacter pylori with cleavage products (see paper)
39% identity, 97% coverage: 10:321/322 of query aligns to 2:281/282 of 5ud0A
P0AB74 D-tagatose-1,6-bisphosphate aldolase subunit KbaY; TBPA; TagBP aldolase; D-tagatose-bisphosphate aldolase class II; Ketose 1,6-bisphosphate aldolase class II; Tagatose-bisphosphate aldolase; EC 4.1.2.40 from Escherichia coli (strain K12) (see paper)
35% identity, 98% coverage: 8:321/322 of query aligns to 1:283/286 of P0AB74
- D82 (= D94) active site, Proton donor
- H83 (= H95) binding Zn(2+)
- H180 (= H190) binding Zn(2+)
- H208 (= H224) binding Zn(2+)
1gvfB Structure of tagatose-1,6-bisphosphate aldolase (see paper)
34% identity, 97% coverage: 10:321/322 of query aligns to 2:274/275 of 1gvfB
- active site: D81 (= D94), H82 (= H95), H171 (= H190), H199 (= H224), N221 (= N267)
- binding phosphoglycolohydroxamic acid: D81 (= D94), H82 (= H95), H171 (= H190), G172 (= G191), H199 (= H224), G200 (= G225), S202 (= S227), N221 (= N267), V222 (≠ I268), A223 (≠ D269), T224 (≠ S270)
- binding zinc ion: H82 (= H95), H171 (= H190), H199 (= H224)
Query Sequence
>WP_013011785.1 NCBI__GCF_000025725.1:WP_013011785.1
MGVSYKDIGLVNTKEMFAKAMEGKYAIPAYNFNNLEQLQAIVTACVESKSPVILQVSKGA
REYANATMLRYMAMGAVQYAKELGCEIPIALHLDHGDSFETAKSCIDSGFSSVMIDGSHL
PFEENITLTKKVVDYAHSLDVTVEGELGVLAGIEDDVVAEKSTYTNPDQVVEFVEKTGCD
SLAISIGTSHGAFKFKAGQPVPPLRFDILKECEVRLPGFPIVLHGASSVVQEYVEMINQY
GGKLEGALGVPEEQLRQAAASAVCKINIDSDGRLALTAKIREFLAEHPEEFDPRKYLKPA
RTELVKMYKAKNVNVLGSAGKA
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