SitesBLAST
Comparing WP_041456752.1 NCBI__GCF_000204075.1:WP_041456752.1 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)
2qm1B Crystal structure of glucokinase from enterococcus faecalis
34% identity, 98% coverage: 3:293/298 of query aligns to 5:321/325 of 2qm1B
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
34% identity, 96% coverage: 7:291/298 of query aligns to 4:309/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (= G12), T11 (= T14), K12 (≠ A15), G130 (= G136), T131 (= T137), G180 (≠ I186), G214 (≠ P197), S218 (≠ G201), G260 (= G243), V261 (= V244), E264 (≠ S247)
- binding beta-D-glucopyranose: G65 (= G70), P78 (≠ I83), N103 (= N109), D104 (= D110), L133 (≠ V139), G134 (= G140), E153 (= E159), H156 (≠ L162), E175 (= E181)
- binding zinc ion: H156 (≠ L162), C166 (= C172), C168 (≠ S174), C173 (≠ S179)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
34% identity, 96% coverage: 7:291/298 of query aligns to 4:309/312 of 3vgkB
Q93LQ8 Beta-glucoside kinase; EC 2.7.1.85 from Klebsiella pneumoniae (see paper)
30% identity, 95% coverage: 5:287/298 of query aligns to 2:281/297 of Q93LQ8
- D7 (= D10) mutation to G: Loss of catalytic activity.
- G9 (= G12) mutation to A: Loss of catalytic activity.
- D103 (= D110) mutation to G: Loss of catalytic activity.
- G131 (= G138) mutation to A: Loss of catalytic activity.
- G133 (= G140) mutation to A: Loss of catalytic activity.
4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
30% identity, 98% coverage: 3:293/298 of query aligns to 7:310/311 of 4db3A
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
29% identity, 96% coverage: 4:290/298 of query aligns to 2:302/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G11 (= G13), T12 (= T14), K13 (≠ A15), G133 (= G136), T134 (= T137), G194 (≠ I186), E198 (≠ R190), A211 (≠ P197), G256 (= G242), G257 (= G243), N260 (≠ S247)
- binding zinc ion: H159 (≠ L162), C180 (= C172), C182 (≠ S174), C187 (≠ S179), E213 (= E199), H217 (≠ L203)
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
29% identity, 96% coverage: 4:290/298 of query aligns to 4:304/306 of 7p7wBBB
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
29% identity, 96% coverage: 4:290/298 of query aligns to 1:301/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P69), G67 (= G70), S79 (≠ I83), N105 (= N109), D106 (= D110), G132 (= G136), T133 (= T137), G134 (= G138), V135 (= V139), G136 (= G140), E155 (= E159), H158 (≠ L162), D188 (≠ E181)
- binding zinc ion: H158 (≠ L162), C179 (= C172), C181 (≠ S174), C186 (≠ S179), E212 (= E199), H216 (≠ L203)
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
34% identity, 99% coverage: 5:298/298 of query aligns to 2:298/298 of 3vovB
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
27% identity, 79% coverage: 53:288/298 of query aligns to 131:378/396 of 1z05A
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
26% identity, 94% coverage: 12:291/298 of query aligns to 68:385/396 of 5f7qE
- binding zinc ion: H243 (≠ L162), C253 (= C172), C255 (≠ S174), C260 (≠ S179)
- binding : G68 (= G12), G68 (= G12), G69 (= G13), G69 (= G13), R70 (≠ T14), R70 (≠ T14), R71 (≠ A15), A72 (≠ I16), K73 (= K17)
Sites not aligning to the query:
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
28% identity, 78% coverage: 59:290/298 of query aligns to 59:300/306 of 5f7rA
- binding alpha-D-glucopyranose: G70 (= G70), N110 (≠ D110), N110 (≠ D110), S134 (≠ T134), V135 (≠ L135), G138 (= G138), L139 (≠ V139), G140 (= G140), E159 (= E159), H162 (≠ L162), E181 (= E181), E253 (≠ G243), W293 (≠ G283)
- binding zinc ion: H162 (≠ L162), C172 (= C172), C174 (≠ S174), C179 (≠ S179)
Sites not aligning to the query:
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
29% identity, 88% coverage: 2:264/298 of query aligns to 1:279/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G12), T13 (= T14), N14 (≠ A15), R16 (≠ K17), T140 (= T137), G189 (≠ I186), L216 (vs. gap), V261 (= V244)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G13), G71 (≠ P69), G72 (= G70), R73 (≠ P71), S84 (≠ A82), T85 (≠ I83), L87 (= L85), N112 (= N109), D113 (= D110), G139 (= G136), T140 (= T137), G141 (= G138), I142 (≠ V139), E162 (= E159), H165 (≠ L162), E184 (= E181)
- binding calcium ion: N112 (= N109), N115 (= N112), G144 (= G141), A161 (≠ G158)
- binding zinc ion: H165 (≠ L162), C175 (= C172), C177 (≠ S174), C182 (≠ S179)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
29% identity, 88% coverage: 2:264/298 of query aligns to 1:279/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G12), G12 (= G13), T13 (= T14), N14 (≠ A15), R16 (≠ K17), T140 (= T137), G189 (≠ I186), L216 (vs. gap), V261 (= V244)
- binding calcium ion: N112 (= N109), N115 (= N112), G144 (= G141), A161 (≠ G158)
- binding zinc ion: H165 (≠ L162), C175 (= C172), C177 (≠ S174), C182 (≠ S179)
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
28% identity, 88% coverage: 2:264/298 of query aligns to 1:280/309 of 2yhwA
O35826 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase; UDP-GlcNAc-2-epimerase/ManAc kinase; EC 3.2.1.183; EC 2.7.1.60 from Rattus norvegicus (Rat) (see paper)
28% identity, 87% coverage: 7:264/298 of query aligns to 410:688/722 of O35826
- D413 (= D10) mutation D->K,N: No effect on UDP-N-acetylglucosamine 2-epimerase activity. Does not affect feedback inhibition by CMP-Neu5Ac. Loss of N-acylmannosamine kinase activity. Does not interfere with oligomerization.
- R420 (≠ K17) mutation to M: No effect on UDP-N-acetylglucosamine 2-epimerase activity. Does not affect feedback inhibition by CMP-Neu5Ac. Loss of N-acylmannosamine kinase activity. Does not interfere with oligomerization.
Sites not aligning to the query:
- 1 UDP-N-acetylglucosamine 2-epimerase
- 49 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Does not interfere with enzyme oligomerization.
- 110 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Partial reduction of the dimerization process.
- 132 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Partial reduction of the dimerization process.
- 155 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Strong reduction of the dimerization process.
- 157 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Strong reduction of the dimerization process.
- 406:722 N-acetylmannosamine kinase
Q9Y223 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase; UDP-GlcNAc-2-epimerase/ManAc kinase; EC 3.2.1.183; EC 2.7.1.60 from Homo sapiens (Human) (see 18 papers)
28% identity, 87% coverage: 7:264/298 of query aligns to 410:688/722 of Q9Y223
- D413 (= D10) binding Mg(2+)
- G416 (= G13) binding an N-acyl-D-mannosamine 6-phosphate
- T417 (= T14) binding ADP
- N418 (≠ A15) binding ADP
- R420 (≠ K17) binding ADP
- I472 (≠ V66) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 50% of the wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to less than 10% of wild-type activity
- G476 (= G70) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (≠ P71) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- T489 (≠ I83) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (= N109) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (= D110) active site; binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; mutation D->A,N: Loss of N-acylmannosamine kinase activity. Decreased affinity for N-acyl-D-mannosamine. No effect on structure.
- N519 (= N112) to S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs1554658910; mutation to S: Decreased N-acylmannosamine kinase activity.
- A524 (= A117) to V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 10% of wild-type activity; decreased N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs764698870
- F528 (≠ L121) to C: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70% of wild-type activity; decreased N-acylmannosamine kinase activity; dbSNP:rs986773986; mutation to C: Decreased N-acylmannosamine kinase activity.
- G545 (= G138) binding an N-acyl-D-mannosamine 6-phosphate
- E566 (= E159) binding an N-acyl-D-mannosamine
- H569 (≠ L162) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (≠ L165) to L: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70-80% of wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to less than 10% of wild-type activity; does not affect homohexamers formation; dbSNP:rs121908632
- G576 (= G169) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C172) binding Zn(2+)
- C581 (≠ S174) binding Zn(2+)
- C586 (≠ S179) binding Zn(2+)
- I587 (≠ L180) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs748949603; mutation to T: Decreased N-acylmannosamine kinase activity.
- E588 (= E181) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- A630 (vs. gap) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A204) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 80% of wild-type activity; decreased N-acylmannosamine kinase activity; retains 75% of wild-type activity; dbSNP:rs121908626; to V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70% of wild-type activity; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs62541771; mutation A->V,T: Decreased N-acylmannosamine kinase activity.
Sites not aligning to the query:
- 13 C → S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; dbSNP:rs1209266607
- 19 binding UDP
- 23 binding UDP
- 113 binding UDP
- 132 H → Q: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 10% of wild-type activity; impaired homohexamers formation
- 176 D → V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs139425890
- 177 R → C: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs539332585
- 200 I → F: in NM; uncertain significance; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 90% of wild-type activity; decreased N-acylmannosamine kinase activity; retains 75% of wild-type activity; dbSNP:rs369328625
- 206 G → S: in NM; moderate phenotype with unusual involvement of quadriceps; dbSNP:rs766266918
- 220 binding UDP
- 253 binding UDP
- 259 binding CMP-N-acetyl-beta-neuraminate
- 263 R → L: in SIALURIA; strong reduction of feedback inhibition by CMP-Neu5Ac; dbSNP:rs121908623
- 266 R → Q: in SIALURIA; abolishes feedback inhibition by CMP-Neu5Ac; dbSNP:rs121908622; R → W: in sialuria; dbSNP:rs121908621
- 271 binding CMP-N-acetyl-beta-neuraminate
- 280 binding CMP-N-acetyl-beta-neuraminate
- 281 binding CMP-N-acetyl-beta-neuraminate
- 282 binding UDP
- 301 binding UDP
- 302 binding UDP
- 303 C → V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 80% of wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to 60% of wild-type activity; requires 2 nucleotide substitutions; dbSNP:rs121908633
- 307 binding UDP
- 321 binding UDP
- 331 V → A: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation
- 378 D → Y: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 10-30% of wild-type activity; decreased N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs199877522
- 708 G → S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; severely decreased; dbSNP:rs1554657922
- 712 M→T: Decreased N-acylmannosamine kinase activity.
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
26% identity, 76% coverage: 63:288/298 of query aligns to 148:388/406 of P50456
- H247 (≠ L162) binding Zn(2+)
- C257 (= C172) binding Zn(2+); mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
- C259 (≠ S174) binding Zn(2+); mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
- C264 (≠ S179) binding Zn(2+)
- R306 (vs. gap) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ E210) mutation to G: Forms dimers but not tetramers; when associated with G-306.
Sites not aligning to the query:
- 52 R→H: Shows increased expression and forms larger colonies.
- 86 H→R: Can be bound and inactivated by MtfA.
- 136 F→A: Decreases association with PtsG EIIB domain.
P32718 D-allose kinase; Allokinase; EC 2.7.1.55 from Escherichia coli (strain K12) (see paper)
27% identity, 97% coverage: 6:295/298 of query aligns to 8:300/309 of P32718
- A73 (≠ T68) mutation to G: 60-fold increase in catalytic efficiency for glucose phosphorylation. 45-fold increase in D-glucose affinity. No change in catalytic efficiency for D-allose phosphorylation.
- F145 (≠ G141) mutation to L: 10-fold increase in catalytic efficiency for glucose phosphorylation. Slight increase in catalytic efficiency for D-allose phosphorylation.
1z6rA Crystal structure of mlc from escherichia coli (see paper)
26% identity, 76% coverage: 63:288/298 of query aligns to 124:364/382 of 1z6rA
Query Sequence
>WP_041456752.1 NCBI__GCF_000204075.1:WP_041456752.1
MGNSQVIGIDLGGTAIKLGRFSEDGTCSQSLTVETPQPATPEAVFLVMVDAIAQIDPDNE
TIAIGVGTPGPADAQGRIAQIAINLPQWENVPLADWLETKTNKPTVIENDANCAGIAEAW
LGAGRHYQNFIMLTLGTGVGGAIFLDGKLFVGHRGAAGELGLITLQPDGPMCKSGNPGSL
EQYTSIKAIRRLTGKEPAELGMLAQAGDIEALQFWQEYGQNLGIGLTSLIYVLTPQAIVL
GGGVSASHEFFLPTLKAEIEQRVMSTSRAGLQILPAELGNSAGMVGAARLAWKKFGNG
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