SitesBLAST
Comparing WP_014450362.1 NCBI__GCF_000284315.1:WP_014450362.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 16 hits to proteins with known functional sites (download)
Q9FK51 ADP-glucose phosphorylase; ADP-glucose:phosphate adenylyltransferase; EC 2.7.7.- from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
38% identity, 98% coverage: 2:333/340 of query aligns to 23:351/351 of Q9FK51
- RAKR 41:44 (≠ RGLR 20:23) binding ADP-alpha-D-glucose
- C63 (= C39) binding Zn(2+)
- C66 (= C42) binding Zn(2+)
- ECA 72:74 (≠ KTP 48:50) binding ADP-alpha-D-glucose
- N94 (= N75) binding ADP-alpha-D-glucose
- H133 (= H112) binding Zn(2+)
- N173 (= N152) binding ADP-alpha-D-glucose
- GASM 179:182 (≠ GASL 158:161) binding ADP-alpha-D-glucose
- H184 (= H163) binding Zn(2+)
- H186 (= H165) active site, Tele-AMP-histidine intermediate
- Q188 (= Q167) binding ADP-alpha-D-glucose
- C216 (= C195) binding Zn(2+)
- C219 (= C198) binding Zn(2+)
- H255 (= H239) binding Zn(2+)
- H310 (= H292) binding Zn(2+)
- G321 (≠ R303) binding ADP-alpha-D-glucose
- FE 325:326 (= FE 307:308) binding ADP-alpha-D-glucose
2h39B Crystal structure of an adp-glucose phosphorylase from arabidopsis thaliana with bound adp-glucose
39% identity, 98% coverage: 2:333/340 of query aligns to 3:313/313 of 2h39B
- active site: C32 (= C39), C35 (= C42), H95 (= H112), N135 (= N152), S143 (= S160), H146 (= H163), G148 (≠ H165), Q150 (= Q167)
- binding adenosine-5'-diphosphate-glucose: R21 (= R20), R24 (= R23), F34 (≠ L41), C42 (≠ T49), N63 (= N75), L64 (≠ K76), Y65 (≠ F77), F133 (= F150), N135 (= N152), G141 (= G158), A142 (= A159), S143 (= S160), M144 (≠ L161), Q150 (= Q167), G285 (≠ A305), F287 (= F307), E288 (= E308)
- binding zinc ion: C32 (= C39), H95 (= H112), H146 (= H163), C178 (= C195), C181 (= C198), H217 (= H239), H272 (= H292)
1z84A X-ray structure of galt-like protein from arabidopsis thaliana at5g18200 (see paper)
39% identity, 98% coverage: 2:333/340 of query aligns to 2:311/311 of 1z84A
- active site: C31 (= C39), C34 (= C42), H93 (= H112), N133 (= N152), S141 (= S160), H144 (= H163), H146 (= H165), Q148 (= Q167)
- binding adenosine monophosphate: F33 (≠ L41), N62 (= N75), L63 (≠ K76), Y64 (≠ F77), N133 (= N152), A140 (= A159), S141 (= S160), M142 (≠ L161), H146 (= H165), Q148 (= Q167)
- binding zinc ion: C31 (= C39), C34 (= C42), H93 (= H112), H144 (= H163), C176 (= C195), C179 (= C198), H215 (= H239), H270 (= H292)
6k5zB Structure of uridylyltransferase (see paper)
32% identity, 95% coverage: 3:326/340 of query aligns to 2:305/314 of 6k5zB
- active site: C30 (= C39), C33 (= C42), H86 (= H112), N127 (= N152), S135 (= S160), H138 (= H163), H140 (= H165), Q142 (= Q167)
- binding fe (iii) ion: E156 (= E181), H252 (= H279), H266 (= H294), E268 (= E296)
- binding phosphate ion: V134 (≠ A159), S135 (= S160), L136 (= L161), H140 (= H165)
- binding zinc ion: C30 (= C39), C33 (= C42), H86 (= H112), H138 (= H163), C170 (= C195), C173 (= C198), H211 (= H239), H264 (= H292)
6k9zA Structure of uridylyltransferase mutant (see paper)
30% identity, 95% coverage: 3:326/340 of query aligns to 2:298/309 of 6k9zA
- active site: C23 (= C39), C26 (= C42), H79 (= H112), N120 (= N152), S128 (= S160), H131 (= H163), F133 (≠ H165), Q135 (= Q167)
- binding fe (iii) ion: E149 (= E181), H245 (= H279), H259 (= H294), E261 (= E296)
- binding uridine-5'-diphosphate: P24 (= P40), N43 (= N75), R44 (≠ K76), Y45 (≠ F77), L129 (= L161), Q135 (= Q167), Y137 (≠ I169)
- binding zinc ion: C23 (= C39), C26 (= C42), H79 (= H112), H131 (= H163), C163 (= C195), C166 (= C198), H204 (= H239), H257 (= H292)
1hxpA Nucleotide transferase (see paper)
25% identity, 89% coverage: 2:305/340 of query aligns to 9:299/340 of 1hxpA
- active site: C44 (= C39), C47 (= C42), H107 (= H112), N145 (= N152), S153 (= S160), H156 (= H163), H158 (= H165), Q160 (= Q167)
- binding beta-mercaptoethanol: N145 (= N152), C152 (≠ A159), Q160 (= Q167), C264 (≠ K270), S265 (≠ D271), L295 (= L301), A299 (= A305)
- binding fe (iii) ion: E174 (= E181), H273 (= H279), H288 (= H294), H290 (≠ E296)
- binding uridine-5'-monophosphate: F45 (≠ P40), V53 (≠ Q58), N69 (= N75), D70 (≠ K76)
- binding zinc ion: C44 (= C39), C47 (= C42), H107 (= H112), H156 (= H163)
P09148 Galactose-1-phosphate uridylyltransferase; Gal-1-P uridylyltransferase; UDP-glucose--hexose-1-phosphate uridylyltransferase; EC 2.7.7.12 from Escherichia coli (strain K12) (see 4 papers)
25% identity, 89% coverage: 2:305/340 of query aligns to 10:307/348 of P09148
- RAKR 28:31 (≠ RGLR 20:23) binding UDP-alpha-D-glucose
- C52 (= C39) binding Zn(2+); mutation to S: Decreases enzyme activity 3000-fold.
- C55 (= C42) binding Zn(2+); mutation to S: Decreases enzyme activity 600-fold.
- V61 (≠ Q58) binding in other chain
- ND 77:78 (≠ NK 75:76) binding in other chain
- H115 (= H112) binding Zn(2+); mutation to N: Decreases enzyme activity by 98%.
- N153 (= N152) binding in other chain
- GCS 159:161 (≠ GAS 158:160) binding in other chain
- C160 (≠ A159) mutation C->S,A: Slight inhibition of enzymatic activity.
- S161 (= S160) mutation to A: 7000-fold reduction in specific activity.
- H164 (= H163) binding Zn(2+); mutation to N: Decreases enzyme activity 10000-fold.
- H166 (= H165) active site, Tele-UMP-histidine intermediate; mutation to G: Abolishes enzymatic activity.
- Q168 (= Q167) binding in other chain
- E182 (= E181) binding Fe cation; mutation to A: Decreases enzyme activity by about 50%. Abolishes iron binding, but has no effect on zinc binding.
- H281 (= H279) binding Fe cation
- H296 (= H294) binding Fe cation
- H298 (≠ E296) binding Fe cation
Sites not aligning to the query:
- 311:312 binding UDP-alpha-D-glucose
- 316:317 binding UDP-alpha-D-glucose
- 323 binding in other chain
1guqA Structure of nucleotidyltransferase complexed with udp-glucose (see paper)
25% identity, 89% coverage: 2:305/340 of query aligns to 9:306/347 of 1guqA
- active site: C51 (= C39), C54 (= C42), H114 (= H112), N152 (= N152), S160 (= S160), H163 (= H163), G165 (≠ H165), Q167 (= Q167)
- binding fe (iii) ion: E181 (= E181), H280 (= H279), H295 (= H294), H297 (≠ E296)
- binding potassium ion: E151 (≠ K151), N152 (= N152), K153 (≠ Y153), G165 (≠ H165)
- binding uridine-5'-diphosphate-glucose: R27 (= R20), R30 (= R23), W32 (vs. gap), F52 (≠ P40), V60 (≠ Q58), N76 (= N75), D77 (≠ K76), F150 (= F150), N152 (= N152), G158 (= G158), C159 (≠ A159), S160 (= S160), Q167 (= Q167)
- binding zinc ion: C51 (= C39), C54 (= C42), H114 (= H112), H163 (= H163)
Sites not aligning to the query:
1gupA Structure of nucleotidyltransferase complexed with udp-galactose (see paper)
25% identity, 89% coverage: 2:305/340 of query aligns to 9:306/347 of 1gupA
- active site: C51 (= C39), C54 (= C42), H114 (= H112), N152 (= N152), S160 (= S160), H163 (= H163), G165 (≠ H165), Q167 (= Q167)
- binding fe (iii) ion: E181 (= E181), H280 (= H279), H295 (= H294), H297 (≠ E296)
- binding galactose-uridine-5'-diphosphate: R27 (= R20), R30 (= R23), F52 (≠ P40), R59 (= R57), V60 (≠ Q58), N76 (= N75), D77 (≠ K76), F78 (= F77), F150 (= F150), N152 (= N152), G158 (= G158), C159 (≠ A159), S160 (= S160), Q167 (= Q167), W169 (≠ I169)
- binding potassium ion: N152 (= N152), K153 (≠ Y153), G165 (≠ H165)
- binding zinc ion: C51 (= C39), C54 (= C42), H114 (= H112), H163 (= H163)
Sites not aligning to the query:
1hxpB Nucleotide transferase (see paper)
25% identity, 89% coverage: 2:305/340 of query aligns to 9:290/329 of 1hxpB
- active site: C35 (= C39), C38 (= C42), H98 (= H112), N136 (= N152), S144 (= S160), H147 (= H163), H149 (= H165), Q151 (= Q167)
- binding beta-mercaptoethanol: H10 (≠ E3), N136 (= N152), C143 (≠ A159), Q151 (= Q167), Y208 (≠ F224)
- binding fe (iii) ion: E165 (= E181), H264 (= H279), H279 (= H294), H281 (≠ E296)
- binding uridine-5'-diphosphate: R43 (= R57), V44 (≠ Q58), F58 (≠ V73), N60 (= N75), D61 (≠ K76), S144 (= S160), N145 (≠ L161)
- binding zinc ion: C35 (= C39), C38 (= C42), H98 (= H112), H147 (= H163)
Sites not aligning to the query:
6gqdA Structure of human galactose-1-phosphate uridylyltransferase (galt), with crystallization epitope mutations a21y:a22t:t23p:r25l
23% identity, 89% coverage: 3:305/340 of query aligns to 11:306/344 of 6gqdA
- active site: N48 (vs. gap), C51 (= C42), S111 (≠ H112), N149 (= N152), S157 (= S160), H160 (= H163), H162 (= H165), Q164 (= Q167)
- binding 5,6-dihydrouridine-5'-monophosphate: P49 (= P40), A57 (≠ Q58), N73 (= N75), D74 (≠ K76), H162 (= H165), Q164 (= Q167)
- binding zinc ion: E178 (= E181), H277 (= H279), H295 (= H294), H297 (≠ E296)
P07902 Galactose-1-phosphate uridylyltransferase; Gal-1-P uridylyltransferase; UDP-glucose--hexose-1-phosphate uridylyltransferase; EC 2.7.7.12 from Homo sapiens (Human) (see 22 papers)
24% identity, 96% coverage: 4:330/340 of query aligns to 32:361/379 of P07902
- I32 (≠ L4) to N: in GALAC1; mild; dbSNP:rs111033644
- Y34 (≠ K6) to N: in GALAC1; affects protein stability; dbSNP:rs111033836
- V44 (≠ I16) to M: in GALAC1; reduced enzyme activity; dbSNP:rs111033647
- L62 (≠ Y36) to M: in dbSNP:rs1800461
- L74 (= L41) to P: in GALAC1; reduced enzyme activity; dbSNP:rs111033663
- H132 (≠ T109) to Q: in GALAC1; affects protein stability; dbSNP:rs367543256
- S135 (≠ H112) to L: in GALAC1; about 5% of normal galactose uridylyltransferase activity; dbSNP:rs111033690
- T138 (≠ A115) to M: in GALAC1; mild; dbSNP:rs111033686
- M142 (≠ F119) to K: in GALAC1; 4% of normal activity; dbSNP:rs111033695
- R148 (≠ E125) to W: in GALAC1; unstable protein; dbSNP:rs111033693
- V151 (≠ L128) to A: in GALAC1; approximately 3% of normal activity; dbSNP:rs111033701
- V168 (≠ I147) to L: in GALAC1; loss of activity; dbSNP:rs367543258
- I170 (= I149) to T: in GALAC1; loss of activity; dbSNP:rs111033839
- F171 (= F150) to S: in GALAC1; reduced enzyme activity; dbSNP:rs111033715
- G175 (= G154) to D: in GALAC1; strongly reduces galactose uridylyltransferase activity; dbSNP:rs111033718
- P185 (≠ S164) to H: in GALAC1; loss of activity; dbSNP:rs111033722
- H186 (= H165) active site, Tele-UMP-histidine intermediate
- Q188 (= Q167) to R: in GALAC1; most common mutation; 10% of normal galactose uridylyltransferase activity; impairs protein folding; dbSNP:rs75391579
- L195 (≠ I174) to P: in GALAC1; no enzymatic activity; dbSNP:rs111033728
- R201 (≠ E180) to C: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033739
- E202 (= E181) binding Zn(2+)
- E220 (≠ D199) to K: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033747
- R223 (= R202) to S: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033750
- L227 (≠ S206) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033846
- R231 (= R210) to H: in GALAC1; 15% of normal activity; dbSNP:rs111033754
- R259 (≠ K238) to Q: in GALAC1; loss of activity; dbSNP:rs886042070; to W: in GALAC1; mild; dbSNP:rs786204763
- I278 (= I257) to N: in GALAC1; 18-fold decrease in activity; dbSNP:rs111033778
- K285 (≠ R264) to N: in GALAC1; severe; impairs protein folding; nearly abolishes enzyme activity; dbSNP:rs111033773
- L289 (≠ V267) to F: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033774
- E291 (≠ L269) to V: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033841
- H301 (= H279) binding Zn(2+)
- N314 (≠ Y291) to D: in GALAC1; allele Duarte; exists as allelic variants Duarte-1 and Duarte-2; Duarte-1 has normal or increased activity; Duarte-2 has activity reduced to about 35-45% of normal; dbSNP:rs2070074
- H319 (= H294) binding Zn(2+)
- H321 (≠ E296) binding Zn(2+)
- L327 (≠ T302) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033832
- A330 (= A305) to V: in GALAC1; mild; dbSNP:rs111033804
- R333 (vs. gap) to W: in GALAC1; no enzymatic activity; dbSNP:rs111033800
- T350 (= T318) to A: in GALAC1; mild; dbSNP:rs111033817
5in3A Crystal structure of glucose-1-phosphate bound nucleotidylated human galactose-1-phosphate uridylyltransferase (see paper)
23% identity, 96% coverage: 3:330/340 of query aligns to 4:319/324 of 5in3A
- active site: N30 (≠ C39), C33 (= C42), S93 (≠ H112), N131 (= N152), S139 (= S160), H142 (= H163), H144 (= H165), Q146 (= Q167)
- binding 1-O-phosphono-alpha-D-glucopyranose: F129 (= F150), N131 (= N152), Q146 (= Q167), V295 (vs. gap), G296 (= G306), E298 (= E308)
- binding 5,6-dihydrouridine-5'-monophosphate: P31 (= P40), A39 (≠ Q58), F53 (≠ V73), N55 (= N75), D56 (≠ K76), V86 (= V105), H144 (= H165), Q146 (= Q167)
- binding zinc ion: E160 (= E181), H259 (= H279), H277 (= H294), H279 (≠ E296)
5uvmB Hit family hydrolase from clostridium thermocellum cth-393
26% identity, 30% coverage: 193:295/340 of query aligns to 3:104/115 of 5uvmB
5uvmA Hit family hydrolase from clostridium thermocellum cth-393
26% identity, 30% coverage: 193:295/340 of query aligns to 3:104/115 of 5uvmA
4qvuA Crystal structure of a duf4931 family protein (bce0241) from bacillus cereus atcc 10987 at 2.65 a resolution
30% identity, 21% coverage: 105:174/340 of query aligns to 26:95/217 of 4qvuA
Sites not aligning to the query:
Query Sequence
>WP_014450362.1 NCBI__GCF_000284315.1:WP_014450362.1
MPELRKDPIIGRWVIIATSRGLRPKDYQAEKVRYLYQSCPLCPGQEEKTPPEVLAYRQSG
SLPNTPGWTLRVVPNKFPALEVEGTLDREGVGLYDRMNGIGAHEVVIETPEHKKALSKFT
EKEFENLLWAYRDRILDLRKDTRFRYIMIFKNYGEAAGASLEHSHSQLIALPIIPTAVVE
ELVGAKSHYEEKERCIFCDIIRQELSDGSRIVQENQEFLAITPFAPKFPFEVWILPKKHA
SSFDQGQKSQYEALSRIFLDVLRRLNVALKDPPYNFILHSSPLQERAEDYYHWHFEIMPT
LTRVAGFEWGTGFYINPTPPEDAARFLREIDLTIESEEIP
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