SitesBLAST
Comparing WP_035135395.1 NCBI__GCF_000769915.1:WP_035135395.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
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)
52% identity, 99% coverage: 4:340/340 of query aligns to 5:339/348 of P09148
- RAKR 28:31 (≠ RSKR 27:30) binding UDP-alpha-D-glucose
- C52 (= C51) binding Zn(2+); mutation to S: Decreases enzyme activity 3000-fold.
- C55 (= C54) binding Zn(2+); mutation to S: Decreases enzyme activity 600-fold.
- V61 (≠ S60) binding in other chain
- ND 77:78 (= ND 76:77) binding in other chain
- H115 (= H114) binding Zn(2+); mutation to N: Decreases enzyme activity by 98%.
- N153 (= N154) binding in other chain
- GCS 159:161 (= GCS 160:162) binding in other chain
- C160 (= C161) mutation C->S,A: Slight inhibition of enzymatic activity.
- S161 (= S162) mutation to A: 7000-fold reduction in specific activity.
- H164 (= H165) binding Zn(2+); mutation to N: Decreases enzyme activity 10000-fold.
- H166 (= H167) active site, Tele-UMP-histidine intermediate; mutation to G: Abolishes enzymatic activity.
- Q168 (= Q169) binding in other chain
- E182 (≠ K183) binding Fe cation; mutation to A: Decreases enzyme activity by about 50%. Abolishes iron binding, but has no effect on zinc binding.
- H281 (= H282) binding Fe cation
- H296 (= H297) binding Fe cation
- H298 (≠ A299) binding Fe cation
- KF 311:312 (= KF 312:313) binding UDP-alpha-D-glucose
- YE 316:317 (= YE 317:318) binding UDP-alpha-D-glucose
- Q323 (= Q324) binding in other chain
1guqA Structure of nucleotidyltransferase complexed with udp-glucose (see paper)
51% identity, 99% coverage: 4:340/340 of query aligns to 4:338/347 of 1guqA
- active site: C51 (= C51), C54 (= C54), H114 (= H114), N152 (= N154), S160 (= S162), H163 (= H165), G165 (≠ H167), Q167 (= Q169)
- binding fe (iii) ion: E181 (≠ K183), H280 (= H282), H295 (= H297), H297 (≠ A299)
- binding potassium ion: E151 (= E153), N152 (= N154), K153 (= K155), G165 (≠ H167)
- binding uridine-5'-diphosphate-glucose: R27 (= R27), R30 (= R30), W32 (= W32), F52 (≠ Y52), V60 (≠ S60), N76 (= N76), D77 (= D77), F150 (= F152), N152 (= N154), G158 (= G160), C159 (= C161), S160 (= S162), Q167 (= Q169), K310 (= K312), F311 (= F313), Y315 (= Y317), E316 (= E318)
- binding zinc ion: C51 (= C51), C54 (= C54), H114 (= H114), H163 (= H165)
1gupA Structure of nucleotidyltransferase complexed with udp-galactose (see paper)
51% identity, 99% coverage: 4:340/340 of query aligns to 4:338/347 of 1gupA
- active site: C51 (= C51), C54 (= C54), H114 (= H114), N152 (= N154), S160 (= S162), H163 (= H165), G165 (≠ H167), Q167 (= Q169)
- binding fe (iii) ion: E181 (≠ K183), H280 (= H282), H295 (= H297), H297 (≠ A299)
- binding galactose-uridine-5'-diphosphate: R27 (= R27), R30 (= R30), F52 (≠ Y52), R59 (= R59), V60 (≠ S60), N76 (= N76), D77 (= D77), F78 (= F78), F150 (= F152), N152 (= N154), G158 (= G160), C159 (= C161), S160 (= S162), Q167 (= Q169), W169 (= W171), K310 (= K312), F311 (= F313), V313 (= V315), G314 (= G316), E316 (= E318)
- binding potassium ion: N152 (= N154), K153 (= K155), G165 (≠ H167)
- binding zinc ion: C51 (= C51), C54 (= C54), H114 (= H114), H163 (= H165)
1hxpA Nucleotide transferase (see paper)
51% identity, 99% coverage: 4:340/340 of query aligns to 4:331/340 of 1hxpA
- active site: C44 (= C51), C47 (= C54), H107 (= H114), N145 (= N154), S153 (= S162), H156 (= H165), H158 (= H167), Q160 (= Q169)
- binding beta-mercaptoethanol: N145 (= N154), C152 (= C161), Q160 (= Q169), C264 (≠ V273), S265 (= S274), L295 (= L304), A299 (= A308)
- binding fe (iii) ion: E174 (≠ K183), H273 (= H282), H288 (= H297), H290 (≠ A299)
- binding uridine-5'-monophosphate: F45 (≠ Y52), V53 (≠ S60), N69 (= N76), D70 (= D77)
- binding zinc ion: C44 (= C51), C47 (= C54), H107 (= H114), H156 (= H165)
1hxpB Nucleotide transferase (see paper)
49% identity, 99% coverage: 4:340/340 of query aligns to 4:322/329 of 1hxpB
- active site: C35 (= C51), C38 (= C54), H98 (= H114), N136 (= N154), S144 (= S162), H147 (= H165), H149 (= H167), Q151 (= Q169)
- binding beta-mercaptoethanol: P5 (≠ L5), H10 (= H10), N136 (= N154), C143 (= C161), Q151 (= Q169), Y208 (≠ F226)
- binding fe (iii) ion: E165 (≠ K183), H264 (= H282), H279 (= H297), H281 (≠ A299)
- binding uridine-5'-diphosphate: R43 (= R59), V44 (≠ S60), F58 (= F74), N60 (= N76), D61 (= D77), S144 (= S162), N145 (= N163)
- binding zinc ion: C35 (= C51), C38 (= C54), H98 (= H114), H147 (= H165)
Sites not aligning to the query:
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)
49% identity, 98% coverage: 6:339/340 of query aligns to 27:361/379 of P07902
- I32 (≠ R11) to N: in GALAC1; mild; dbSNP:rs111033644
- Y34 (= Y13) to N: in GALAC1; affects protein stability; dbSNP:rs111033836
- V44 (= V23) to M: in GALAC1; reduced enzyme activity; dbSNP:rs111033647
- L62 (≠ A41) to M: in dbSNP:rs1800461
- L74 (= L53) to P: in GALAC1; reduced enzyme activity; dbSNP:rs111033663
- H132 (≠ S111) to Q: in GALAC1; affects protein stability; dbSNP:rs367543256
- S135 (≠ H114) to L: in GALAC1; about 5% of normal galactose uridylyltransferase activity; dbSNP:rs111033690
- T138 (= T117) to M: in GALAC1; mild; dbSNP:rs111033686
- M142 (= M121) to K: in GALAC1; 4% of normal activity; dbSNP:rs111033695
- R148 (= R127) to W: in GALAC1; unstable protein; dbSNP:rs111033693
- V151 (= V130) to A: in GALAC1; approximately 3% of normal activity; dbSNP:rs111033701
- V168 (= V149) to L: in GALAC1; loss of activity; dbSNP:rs367543258
- I170 (= I151) to T: in GALAC1; loss of activity; dbSNP:rs111033839
- F171 (= F152) to S: in GALAC1; reduced enzyme activity; dbSNP:rs111033715
- G175 (= G156) to D: in GALAC1; strongly reduces galactose uridylyltransferase activity; dbSNP:rs111033718
- P185 (= P166) to H: in GALAC1; loss of activity; dbSNP:rs111033722
- H186 (= H167) active site, Tele-UMP-histidine intermediate
- Q188 (= Q169) to R: in GALAC1; most common mutation; 10% of normal galactose uridylyltransferase activity; impairs protein folding; dbSNP:rs75391579
- L195 (= L176) to P: in GALAC1; no enzymatic activity; dbSNP:rs111033728
- R201 (≠ K182) to C: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033739
- E202 (≠ K183) binding Zn(2+)
- E220 (≠ D201) to K: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033747
- R223 (≠ Q204) to S: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033750
- L227 (≠ Q208) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033846
- R231 (= R212) to H: in GALAC1; 15% of normal activity; dbSNP:rs111033754
- R259 (= R240) to Q: in GALAC1; loss of activity; dbSNP:rs886042070; to W: in GALAC1; mild; dbSNP:rs786204763
- I278 (≠ T259) to N: in GALAC1; 18-fold decrease in activity; dbSNP:rs111033778
- K285 (≠ I266) to N: in GALAC1; severe; impairs protein folding; nearly abolishes enzyme activity; dbSNP:rs111033773
- L289 (≠ V270) to F: in GALAC1; 3-fold decrease in activity; dbSNP:rs111033774
- E291 (≠ D272) to V: in GALAC1; 2-fold decrease in activity; dbSNP:rs111033841
- H301 (= H282) binding Zn(2+)
- N314 (= N292) 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 (= H297) binding Zn(2+)
- H321 (≠ A299) binding Zn(2+)
- L327 (= L305) to P: in GALAC1; results in no detectable protein in the soluble fraction; dbSNP:rs111033832
- A330 (= A308) to V: in GALAC1; mild; dbSNP:rs111033804
- R333 (≠ K311) to W: in GALAC1; no enzymatic activity; dbSNP:rs111033800
- T350 (= T328) to A: in GALAC1; mild; dbSNP:rs111033817
6gqdA Structure of human galactose-1-phosphate uridylyltransferase (galt), with crystallization epitope mutations a21y:a22t:t23p:r25l
49% identity, 98% coverage: 6:339/340 of query aligns to 7:337/344 of 6gqdA
- active site: N48 (≠ C51), C51 (= C54), S111 (≠ H114), N149 (= N154), S157 (= S162), H160 (= H165), H162 (= H167), Q164 (= Q169)
- binding 5,6-dihydrouridine-5'-monophosphate: P49 (≠ Y52), A57 (≠ S60), N73 (= N76), D74 (= D77), H162 (= H167), Q164 (= Q169)
- binding zinc ion: E178 (≠ K183), H277 (= H282), H295 (= H297), H297 (≠ A299)
5in3A Crystal structure of glucose-1-phosphate bound nucleotidylated human galactose-1-phosphate uridylyltransferase (see paper)
47% identity, 97% coverage: 10:339/340 of query aligns to 4:319/324 of 5in3A
- active site: N30 (≠ C51), C33 (= C54), S93 (≠ H114), N131 (= N154), S139 (= S162), H142 (= H165), H144 (= H167), Q146 (= Q169)
- binding 1-O-phosphono-alpha-D-glucopyranose: F129 (= F152), N131 (= N154), Q146 (= Q169), V295 (= V315), G296 (= G316), E298 (= E318)
- binding 5,6-dihydrouridine-5'-monophosphate: P31 (≠ Y52), A39 (≠ S60), F53 (= F74), N55 (= N76), D56 (= D77), V86 (= V107), H144 (= H167), Q146 (= Q169)
- binding zinc ion: E160 (≠ K183), H259 (= H282), H277 (= H297), H279 (≠ A299)
6k5zB Structure of uridylyltransferase (see paper)
29% identity, 96% coverage: 12:337/340 of query aligns to 4:306/314 of 6k5zB
- active site: C30 (= C51), C33 (= C54), H86 (= H114), N127 (= N154), S135 (= S162), H138 (= H165), H140 (= H167), Q142 (= Q169)
- binding fe (iii) ion: E156 (≠ K183), H252 (= H282), H266 (= H297), E268 (≠ A299)
- binding phosphate ion: V134 (≠ C161), S135 (= S162), L136 (≠ N163), H140 (= H167)
- binding zinc ion: C30 (= C51), C33 (= C54), H86 (= H114), H138 (= H165), C170 (≠ T197), C173 (≠ S200), H211 (≠ A241), H264 (= H295)
6k9zA Structure of uridylyltransferase mutant (see paper)
27% identity, 96% coverage: 12:337/340 of query aligns to 4:299/309 of 6k9zA
- active site: C23 (= C51), C26 (= C54), H79 (= H114), N120 (= N154), S128 (= S162), H131 (= H165), F133 (≠ H167), Q135 (= Q169)
- binding fe (iii) ion: E149 (≠ K183), H245 (= H282), H259 (= H297), E261 (≠ A299)
- binding uridine-5'-diphosphate: P24 (≠ Y52), N43 (= N76), R44 (≠ D77), Y45 (≠ F78), L129 (≠ N163), Q135 (= Q169), Y137 (≠ W171)
- binding zinc ion: C23 (= C51), C26 (= C54), H79 (= H114), H131 (= H165), C163 (≠ T197), C166 (≠ S200), H204 (≠ A241), H257 (= H295)
Q9FK51 ADP-glucose phosphorylase; ADP-glucose:phosphate adenylyltransferase; EC 2.7.7.- from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
25% identity, 99% coverage: 6:340/340 of query aligns to 20:349/351 of Q9FK51
- RAKR 41:44 (≠ RSKR 27:30) binding ADP-alpha-D-glucose
- C63 (= C51) binding Zn(2+)
- C66 (= C54) binding Zn(2+)
- ECA 72:74 (≠ SGG 60:62) binding ADP-alpha-D-glucose
- N94 (= N76) binding ADP-alpha-D-glucose
- H133 (= H114) binding Zn(2+)
- N173 (= N154) binding ADP-alpha-D-glucose
- GASM 179:182 (≠ GCSN 160:163) binding ADP-alpha-D-glucose
- H184 (= H165) binding Zn(2+)
- H186 (= H167) active site, Tele-AMP-histidine intermediate
- Q188 (= Q169) binding ADP-alpha-D-glucose
- C216 (≠ T197) binding Zn(2+)
- C219 (≠ S200) binding Zn(2+)
- H255 (≠ A241) binding Zn(2+)
- H310 (= H295) binding Zn(2+)
- G321 (≠ T309) binding ADP-alpha-D-glucose
- FE 325:326 (≠ FM 313:314) binding ADP-alpha-D-glucose
2h39B Crystal structure of an adp-glucose phosphorylase from arabidopsis thaliana with bound adp-glucose
24% identity, 98% coverage: 7:340/340 of query aligns to 1:311/313 of 2h39B
- active site: C32 (= C51), C35 (= C54), H95 (= H114), N135 (= N154), S143 (= S162), H146 (= H165), G148 (≠ H167), Q150 (= Q169)
- binding adenosine-5'-diphosphate-glucose: R21 (= R27), R24 (= R30), F34 (≠ L53), C42 (≠ G61), N63 (= N76), L64 (≠ D77), Y65 (≠ F78), F133 (= F152), N135 (= N154), G141 (= G160), A142 (≠ C161), S143 (= S162), M144 (≠ N163), Q150 (= Q169), G285 (≠ K311), F287 (= F313), E288 (≠ M314)
- binding zinc ion: C32 (= C51), H95 (= H114), H146 (= H165), C178 (≠ T197), C181 (≠ S200), H217 (≠ A241), H272 (= H295)
1z84A X-ray structure of galt-like protein from arabidopsis thaliana at5g18200 (see paper)
24% identity, 98% coverage: 9:340/340 of query aligns to 2:309/311 of 1z84A
- active site: C31 (= C51), C34 (= C54), H93 (= H114), N133 (= N154), S141 (= S162), H144 (= H165), H146 (= H167), Q148 (= Q169)
- binding adenosine monophosphate: F33 (≠ L53), N62 (= N76), L63 (≠ D77), Y64 (≠ F78), N133 (= N154), A140 (≠ C161), S141 (= S162), M142 (≠ N163), H146 (= H167), Q148 (= Q169)
- binding zinc ion: C31 (= C51), C34 (= C54), H93 (= H114), H144 (= H165), C176 (≠ T197), C179 (≠ S200), H215 (≠ A241), H270 (= H295)
Query Sequence
>WP_035135395.1 NCBI__GCF_000769915.1:WP_035135395.1
MDKNLNEYPHRRYNALTGEWVLVSPHRSKRPWQGQVEKHSAEVRPQYDPGCYLCPGNSRS
GGEQNPDYKDVYVFINDFSALLKDSPDFDVVEDDIFKAESEKGICRVICFSPDHSLTIPQ
MKVEDIRKVVDLWIEEYHTLGSDPEINYVQIFENKGEIMGCSNPHPHGQIWASQKLPVEP
SKKQHYQLEYFQKHGDTLLSDYLQKELQKDERIIFENNHFAAIVPFWATWPYEAMIIPKR
AMARITDMTDDEKTALADTYKRLTMIYDKVFDVSFPYSAGIHQAPTDGKEHNEWHWHMAF
YPPLLRSATVKKFMVGYEMLATPQRDITPESAAQILKNLN
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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