SitesBLAST
Comparing NP_661944.1 NCBI__GCF_000006985.1:NP_661944.1 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)
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)
48% identity, 97% coverage: 10:323/323 of query aligns to 1:307/323 of A8B2U2
- S50 (= S59) binding beta-D-fructose 1,6-bisphosphate
- D83 (= D96) active site, Proton donor; mutation to A: Severe loss of catalytic activity.
- H84 (= H97) binding Zn(2+)
- H178 (= H192) binding beta-D-fructose 1,6-bisphosphate; binding Zn(2+)
- G179 (= G193) binding beta-D-fructose 1,6-bisphosphate
- K182 (= K196) binding beta-D-fructose 1,6-bisphosphate
- H210 (= H225) binding Zn(2+)
- G211 (= G226) binding beta-D-fructose 1,6-bisphosphate
- S213 (= S228) binding beta-D-fructose 1,6-bisphosphate
- N253 (= N268) binding beta-D-fructose 1,6-bisphosphate
- D255 (= D270) 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 (= S271) binding beta-D-fructose 1,6-bisphosphate
- R259 (= R274) 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 (= D293) 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 (= R295) 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: 12:323/323 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 (= S59), D82 (= D96), H83 (= H97), H174 (= H192), G175 (= G193), K178 (= K196), G207 (= G226), S209 (= S228), N249 (= N268), D251 (= D270), S252 (= S271), R255 (= R274)
- binding zinc ion: H83 (= H97), H174 (= H192), H206 (= H225)
3gb6A Structure of giardia fructose-1,6-biphosphate aldolase d83a mutant in complex with fructose-1,6-bisphosphate (see paper)
48% identity, 97% coverage: 12:323/323 of query aligns to 2:302/318 of 3gb6A
- binding 1,6-di-O-phosphono-D-fructose: N23 (= N33), S49 (= S59), H173 (= H192), G174 (= G193), K177 (= K196), H205 (= H225), G206 (= G226), S208 (= S228), N248 (= N268), D250 (= D270), S251 (= S271), R254 (= R274)
3gayA Structure of giardia fructose-1,6-biphosphate aldolase in complex with tagatose-1,6-biphosphate (see paper)
48% identity, 97% coverage: 12:323/323 of query aligns to 2:303/319 of 3gayA
- binding 1,6-di-O-phosphono-D-tagatose: N23 (= N33), S49 (= S59), D82 (= D96), H174 (= H192), G175 (= G193), K178 (= K196), H206 (= H225), G207 (= G226), S209 (= S228), N249 (= N268), D251 (= D270), S252 (= S271), R255 (= R274)
- binding zinc ion: H83 (= H97), H174 (= H192), H206 (= H225)
2isvB Structure of giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
47% identity, 97% coverage: 12:323/323 of query aligns to 2:292/307 of 2isvB
- binding phosphoglycolohydroxamic acid: D82 (= D96), H168 (= H192), G169 (= G193), K172 (= K196), H195 (= H225), G196 (= G226), S198 (= S228), N238 (= N268), D240 (= D270), S241 (= S271)
- binding zinc ion: H83 (= H97), H168 (= H192), H195 (= H225)
2isvA Structure of giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate (see paper)
46% identity, 97% coverage: 12:323/323 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)
47% identity, 97% coverage: 12:323/323 of query aligns to 2:305/305 of 1rv8B
- active site: D80 (= D96), H81 (= H97), E140 (= E156), H178 (= H192), H208 (= H225), N251 (= N268)
- binding cobalt (ii) ion: H81 (= H97), E132 (= E148), H178 (= H192), H208 (= H225)
- binding sulfate ion: R116 (= R132), H123 (= H139), S211 (= S228), D253 (= D270), T254 (≠ S271)
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)
43% identity, 96% coverage: 12:322/323 of query aligns to 2:306/307 of 3n9sA
- active site: C69 (≠ A83), E70 (= E84), G136 (= G150), H180 (= H192), A226 (≠ H241), N253 (= N268)
- binding calcium ion: D104 (= D118), S106 (= S120), E134 (= E148)
- binding 4-{hydroxy[(phosphonooxy)acetyl]amino}butyl dihydrogen phosphate: N23 (= N33), S49 (= S59), D82 (= D96), H83 (= H97), H180 (= H192), G181 (= G193), K184 (= K196), H210 (= H225), G211 (= G226), S213 (= S228), N253 (= N268), D255 (= D270), T256 (≠ S271)
- binding zinc ion: H83 (= H97), H180 (= H192), H210 (= H225)
3c52A Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with phosphoglycolohydroxamic acid, a competitive inhibitor (see paper)
43% identity, 96% coverage: 12:322/323 of query aligns to 2:295/296 of 3c52A
- active site: C69 (≠ A83), E70 (= E84), G136 (= G150), H169 (= H192), A215 (≠ H241), N242 (= N268)
- binding calcium ion: D104 (= D118), S106 (= S120), E134 (= E148)
- binding phosphoglycolohydroxamic acid: D82 (= D96), H83 (= H97), H169 (= H192), K173 (= K196), H199 (= H225), G200 (= G226), S202 (= S228), N242 (= N268), D244 (= D270), T245 (≠ S271)
- binding zinc ion: H83 (= H97), H169 (= H192), H199 (= H225)
3n9rA Class ii fructose-1,6-bisphosphate aldolase from helicobacter pylori in complex with n-(4-hydroxybutyl)-phosphoglycolohydroxamic acid, a competitive inhibitor (see paper)
43% identity, 96% coverage: 12:322/323 of query aligns to 2:296/297 of 3n9rA
- active site: C69 (≠ A83), E70 (= E84), G136 (= G150), H170 (= H192), A216 (≠ H241), N243 (= N268)
- binding 2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate: H83 (= H97), H170 (= H192), G171 (= G193), K174 (= K196), H200 (= H225), G201 (= G226), S203 (= S228), N243 (= N268), D245 (= D270), T246 (≠ S271)
- binding zinc ion: H83 (= H97), H170 (= H192), H200 (= H225)
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)
43% identity, 96% coverage: 12:322/323 of query aligns to 2:296/297 of 3c56A
- active site: C69 (≠ A83), E70 (= E84), G136 (= G150), H170 (= H192), A216 (≠ H241), N243 (= N268)
- binding 3-{hydroxy[(phosphonooxy)acetyl]amino}propyl dihydrogen phosphate: N23 (= N33), S49 (= S59), D82 (= D96), H170 (= H192), K174 (= K196), G201 (= G226), S203 (= S228), N243 (= N268), D245 (= D270), T246 (≠ S271), R249 (= R274)
- binding zinc ion: H83 (= H97), H170 (= H192), H200 (= H225)
3q94A The crystal structure of fructose 1,6-bisphosphate aldolase from bacillus anthracis str. 'Ames ancestor'
40% identity, 97% coverage: 10:323/323 of query aligns to 1:285/285 of 3q94A
- active site: D85 (= D96), H86 (= H97), E145 (= E156), H181 (= H192), H209 (= H225), N231 (= N268)
- binding zinc ion: H86 (= H97), E114 (= E125), H163 (≠ D174), H181 (= H192), H209 (= H225), E235 (≠ D272), E239 (≠ A276)
5uckA Class ii fructose-1,6-bisphosphate aldolase of helicobacter pylori with cleavage products (see paper)
42% identity, 96% coverage: 12:322/323 of query aligns to 2:290/291 of 5uckA
- binding glyceraldehyde-3-phosphate: S49 (= S59), D82 (= D96), H83 (= H97), H164 (= H192), D239 (= D270), R243 (= R274)
- binding zinc ion: H83 (= H97), H83 (= H97), E134 (= E148), H164 (= H192), H194 (= H225), H194 (= H225)
5ucpA Class ii fructose-1,6-bisphosphate aldolase e142a variant of helicobacter pylori with fbp and cleavage products (see paper)
42% identity, 96% coverage: 12:322/323 of query aligns to 2:291/292 of 5ucpA
- binding 1,6-di-O-phosphono-D-fructose: S49 (= S59), D82 (= D96), H83 (= H97), H165 (= H192), K169 (= K196), G196 (= G226), S198 (= S228), N238 (= N268), D240 (= D270), T241 (≠ S271), R244 (= R274)
- binding zinc ion: H83 (= H97), H83 (= H97), H83 (= H97), E134 (= E148), H165 (= H192), H165 (= H192), H165 (= H192), H195 (= H225), H195 (= H225)
5ud4A Class ii fructose-1,6-bisphosphate aldolase h180q variant of helicobacter pylori with tbp (see paper)
42% identity, 96% coverage: 12:322/323 of query aligns to 2:292/293 of 5ud4A
- binding 1,6-di-O-phosphono-D-tagatose: S49 (= S59), D82 (= D96), Q166 (≠ H192), G167 (= G193), K170 (= K196), G197 (= G226), S199 (= S228), N239 (= N268), D241 (= D270), T242 (≠ S271), R245 (= R274)
- binding zinc ion: H83 (= H97), H83 (= H97), E134 (= E148), H196 (= H225), H196 (= H225)
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, 96% coverage: 10:320/323 of query aligns to 1:283/285 of P13243
- T212 (≠ S228) modified: Phosphothreonine
- T234 (≠ S271) modified: Phosphothreonine
5ud0A Class ii fructose-1,6-bisphosphate aldolase e149a variant of helicobacter pylori with cleavage products (see paper)
40% identity, 96% coverage: 12:322/323 of query aligns to 2:281/282 of 5ud0A
4to8A Methicillin-resistant staphylococcus aureus class iib fructose 1,6- bisphosphate aldolase (see paper)
40% identity, 96% coverage: 12:320/323 of query aligns to 2:275/279 of 4to8A
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)
36% identity, 97% coverage: 10:322/323 of query aligns to 1:283/286 of P0AB74
- D82 (= D96) active site, Proton donor
- H83 (= H97) binding Zn(2+)
- H180 (= H192) binding Zn(2+)
- H208 (= H225) binding Zn(2+)
1gvfB Structure of tagatose-1,6-bisphosphate aldolase (see paper)
36% identity, 97% coverage: 11:322/323 of query aligns to 1:274/275 of 1gvfB
- active site: D81 (= D96), H82 (= H97), H171 (= H192), H199 (= H225), N221 (= N268)
- binding phosphoglycolohydroxamic acid: D81 (= D96), H82 (= H97), H171 (= H192), G172 (= G193), H199 (= H225), G200 (= G226), S202 (= S228), N221 (= N268), V222 (≠ I269), A223 (≠ D270), T224 (≠ S271)
- binding zinc ion: H82 (= H97), H171 (= H192), H199 (= H225)
Query Sequence
>NP_661944.1 NCBI__GCF_000006985.1:NP_661944.1
MKKITGYKELGLVNSRELFAKAISGGYAIPAYNFNNLEQLQAIIMACVETASPVILQVSK
GARSYANQTLLRHLAAGAVEYAAELGREIPIVLHLDHGDSFELCKDCIETGFSSVMIDGS
HLSYEDNVSLTRKVVEFAHQHDVTVEGELGVLAGIEDEVHATKHTYTEPDQVEDFVGKTG
VDSLAIAIGTSHGAFKFKPGEDHKIRLDILAEIEKRIPGFPIVLHGASSVPQDLVQMINA
HGGKLKDAVGIGEDQLREAARSAVCKINIDSDGRLAMTAAVRKVLDEKPEEFDPRKYLGP
ARDALKQLYMHKIINVLGSNGKA
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