SitesBLAST
Comparing BWI76_RS22415 FitnessBrowser__Koxy:BWI76_RS22415 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)
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
40% identity, 96% coverage: 2:293/304 of query aligns to 2:301/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P66), G67 (= G67), S79 (≠ C79), N105 (= N105), D106 (= D106), G132 (= G132), T133 (= T133), G134 (= G134), V135 (≠ C135), G136 (= G136), E155 (= E155), H158 (= H158), D188 (≠ E184)
- binding zinc ion: H158 (= H158), C179 (= C175), C181 (= C177), C186 (= C182), E212 (≠ A204), H216 (≠ A208)
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
40% identity, 96% coverage: 2:293/304 of query aligns to 3:302/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G11 (= G10), T12 (= T11), K13 (= K12), G133 (= G132), T134 (= T133), G194 (= G189), E198 (≠ A193), A211 (≠ S202), G256 (= G247), G257 (= G248), N260 (= N251)
- binding zinc ion: H159 (= H158), C180 (= C175), C182 (= C177), C187 (= C182), E213 (≠ A204), H217 (≠ A208)
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
40% identity, 96% coverage: 2:293/304 of query aligns to 5:304/306 of 7p7wBBB
4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
37% identity, 97% coverage: 2:295/304 of query aligns to 9:309/311 of 4db3A
Q8ZPZ9 N-acetyl-D-glucosamine kinase; GlcNAc kinase; EC 2.7.1.59 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
36% identity, 97% coverage: 2:297/304 of query aligns to 1:303/303 of Q8ZPZ9
- H157 (= H158) binding
- C177 (= C175) binding
- C179 (= C177) binding
- C184 (= C182) binding
2ap1A Crystal structure of the putative regulatory protein
36% identity, 97% coverage: 2:297/304 of query aligns to 3:305/305 of 2ap1A
Q93LQ8 Beta-glucoside kinase; EC 2.7.1.85 from Klebsiella pneumoniae (see paper)
28% identity, 80% coverage: 6:249/304 of query aligns to 6:244/297 of Q93LQ8
- D7 (= D7) mutation to G: Loss of catalytic activity.
- G9 (= G9) mutation to A: Loss of catalytic activity.
- D103 (= D106) mutation to G: Loss of catalytic activity.
- G131 (= G134) mutation to A: Loss of catalytic activity.
- G133 (= G136) mutation to A: Loss of catalytic activity.
2qm1B Crystal structure of glucokinase from enterococcus faecalis
27% identity, 98% coverage: 4:300/304 of query aligns to 9:325/325 of 2qm1B
P32718 D-allose kinase; Allokinase; EC 2.7.1.55 from Escherichia coli (strain K12) (see paper)
26% identity, 95% coverage: 5:293/304 of query aligns to 10:295/309 of P32718
- A73 (≠ G67) 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 (≠ G137) mutation to L: 10-fold increase in catalytic efficiency for glucose phosphorylation. Slight increase in catalytic efficiency for D-allose phosphorylation.
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
23% identity, 95% coverage: 4:293/304 of query aligns to 78:380/396 of 1z05A
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
27% identity, 82% coverage: 4:251/304 of query aligns to 6:264/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G9), T13 (= T11), N14 (≠ K12), R16 (≠ E14), T140 (= T133), G189 (= G189), L216 (vs. gap), V261 (≠ G248)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G10), G71 (≠ P66), G72 (= G67), R73 (≠ A68), S84 (≠ C79), T85 (≠ N80), L87 (= L82), N112 (= N105), D113 (= D106), G139 (= G132), T140 (= T133), G141 (= G134), I142 (≠ C135), E162 (= E155), H165 (= H158), E184 (= E184)
- binding calcium ion: N112 (= N105), N115 (≠ D108), G144 (= G137), A161 (≠ G154)
- binding zinc ion: H165 (= H158), C175 (= C175), C177 (= C177), C182 (= C182)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
27% identity, 82% coverage: 4:251/304 of query aligns to 6:264/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G9), G12 (= G10), T13 (= T11), N14 (≠ K12), R16 (≠ E14), T140 (= T133), G189 (= G189), L216 (vs. gap), V261 (≠ G248)
- binding calcium ion: N112 (= N105), N115 (≠ D108), G144 (= G137), A161 (≠ G154)
- binding zinc ion: H165 (= H158), C175 (= C175), C177 (= C177), C182 (= C182)
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, 82% coverage: 4:251/304 of query aligns to 410:673/722 of Q9Y223
- D413 (= D7) binding
- G416 (= G10) binding
- T417 (= T11) binding
- N418 (≠ K12) binding
- R420 (≠ E14) binding
- I472 (= I63) 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 (= G67) binding ; binding
- R477 (≠ A68) binding ; binding
- T489 (≠ N80) binding ; binding
- N516 (= N105) binding ; binding
- D517 (= D106) active site; binding ; binding ; mutation D->A,N: Loss of N-acylmannosamine kinase activity. Decreased affinity for N-acyl-D-mannosamine. No effect on structure.
- N519 (≠ D108) 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 (≠ S113) 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 (≠ D117) 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 (= G134) binding
- E566 (= E155) binding
- H569 (= H158) binding ; binding ; binding
- V572 (≠ L161) 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 (= G170) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C175) binding
- C581 (= C177) binding
- C586 (= C182) binding
- I587 (= I183) 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 (= E184) binding ; binding
- A630 (= A208) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A209) 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
- 23 binding
- 113 binding
- 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
- 253 binding
- 259 binding
- 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
- 280 binding
- 281 binding
- 282 binding
- 301 binding
- 302 binding
- 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
- 321 binding
- 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.
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, 82% coverage: 4:251/304 of query aligns to 410:673/722 of O35826
- D413 (= D7) 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 (≠ E14) 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
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
28% identity, 82% coverage: 4:251/304 of query aligns to 6:265/309 of 2yhwA
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
27% identity, 78% coverage: 56:293/304 of query aligns to 144:390/406 of P50456
- H247 (= H158) binding
- C257 (= C175) binding ; mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
- C259 (= C177) binding ; mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
- C264 (= C182) binding
- R306 (= R221) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ D225) 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.
1z6rA Crystal structure of mlc from escherichia coli (see paper)
27% identity, 78% coverage: 56:293/304 of query aligns to 120:366/382 of 1z6rA
6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
28% identity, 96% coverage: 1:292/304 of query aligns to 1:263/269 of 6jdcA
6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
27% identity, 96% coverage: 1:292/304 of query aligns to 1:283/290 of 6jdbA
- binding adenosine-5'-diphosphate: K12 (= K12), S129 (≠ G132), T130 (= T133), P195 (≠ S202), K196 (≠ E203), S241 (≠ G248)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: T62 (≠ P66), G63 (= G67), A72 (≠ N78), L73 (≠ C79), N74 (= N80), N77 (≠ V83), N102 (= N105), D103 (= D106), S129 (≠ G132), T130 (= T133), H152 (≠ E155), H155 (= H158), E174 (= E184)
- binding zinc ion: H155 (= H158), C165 (= C175), C167 (= C177), C172 (= C182)
6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
25% identity, 96% coverage: 1:292/304 of query aligns to 1:284/293 of 6jdoA
Query Sequence
>BWI76_RS22415 FitnessBrowser__Koxy:BWI76_RS22415
MLHLGLDIGGTKMEAVLLNAAGECVYRQRRPTHKESYDAFMQQLLGLIESVRAWSERPFT
LGIGLPGAIDPQSGLIKNCNCLVLNGHDLRHDLMRELGQSVWMANDADCFTLSEAVDGAG
AGATTVFGVIIGTGCGGGVAVNQRLLSGPNAIAGEWGHNPLPGYRPERDGPAQPCYCGKE
NCIESFISGTGFARRYGAQARSEAIIAAAQNGAPLALAHWRHFIDAFARSLASVINILDP
QVIVLGGGLSNVGQIYEQLPSAIVPYLFSDSCRTQIKQARFGDASGVRGAAWLPVLDSAE
GRRR
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