SitesBLAST
Comparing BWI76_RS27555 FitnessBrowser__Koxy:BWI76_RS27555 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)
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
37% identity, 95% coverage: 3:297/310 of query aligns to 3:301/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P66), G67 (= G67), S79 (≠ A79), 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 (≠ A208), H216 (≠ R212)
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
37% identity, 95% coverage: 3:297/310 of query aligns to 4:302/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G11 (= G10), T12 (≠ S11), K13 (= K12), G133 (= G132), T134 (= T133), G194 (= G189), E198 (≠ S193), A211 (≠ S206), G256 (= G251), G257 (= G252), N260 (= N255)
- binding zinc ion: H159 (= H158), C180 (= C175), C182 (= C177), C187 (= C182), E213 (≠ A208), H217 (≠ R212)
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
37% identity, 95% coverage: 3:297/310 of query aligns to 6:304/306 of 7p7wBBB
4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
34% identity, 96% coverage: 3:300/310 of query aligns to 10:310/311 of 4db3A
2ap1A Crystal structure of the putative regulatory protein
36% identity, 95% coverage: 3:297/310 of query aligns to 4:301/305 of 2ap1A
Q8ZPZ9 N-acetyl-D-glucosamine kinase; GlcNAc kinase; EC 2.7.1.59 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
36% identity, 95% coverage: 3:297/310 of query aligns to 2:299/303 of Q8ZPZ9
- H157 (= H158) binding
- C177 (= C175) binding
- C179 (= C177) binding
- C184 (= C182) binding
2qm1B Crystal structure of glucokinase from enterococcus faecalis
28% identity, 98% coverage: 2:304/310 of query aligns to 7:325/325 of 2qm1B
Q93LQ8 Beta-glucoside kinase; EC 2.7.1.85 from Klebsiella pneumoniae (see paper)
26% identity, 95% coverage: 1:296/310 of query aligns to 1:283/297 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.
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
26% identity, 81% coverage: 46:297/310 of query aligns to 124:380/396 of 1z05A
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
35% identity, 84% coverage: 4:262/310 of query aligns to 4:270/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (= G9), T11 (≠ S11), K12 (= K12), G130 (= G132), T131 (= T133), G180 (= G189), G214 (= G216), S218 (vs. gap), G260 (= G252), V261 (≠ L253), E264 (≠ V256)
- binding beta-D-glucopyranose: G65 (= G67), P78 (≠ N80), N103 (= N105), D104 (= D106), L133 (≠ C135), G134 (= G136), E153 (= E155), H156 (= H158), E175 (= E184)
- binding zinc ion: H156 (= H158), C166 (= C175), C168 (= C177), C173 (= C182)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
35% identity, 84% coverage: 4:262/310 of query aligns to 4:270/312 of 3vgkB
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
25% identity, 88% coverage: 28:300/310 of query aligns to 113:387/396 of 5f7qE
Sites not aligning to the query:
- binding : 5, 8, 12, 15, 32, 43, 44, 67, 68, 68, 69, 69, 70, 70, 71, 72, 73
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
25% identity, 88% coverage: 28:300/310 of query aligns to 32:303/306 of 5f7rA
- binding alpha-D-glucopyranose: G70 (= G67), N110 (≠ D106), N110 (≠ D106), S134 (≠ T130), V135 (≠ L131), G138 (= G134), L139 (≠ C135), G140 (= G136), E159 (= E155), H162 (= H158), E181 (= E184), E253 (≠ G251), W293 (≠ G290)
- binding zinc ion: H162 (= H158), C172 (= C175), C174 (= C177), C179 (= C182)
Sites not aligning to the query:
6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
28% identity, 95% coverage: 1:296/310 of query aligns to 1:284/293 of 6jdoA
6jdhA Crystal structure of n-acetyl mannosmaine kinase from pasteurella multocida
28% identity, 95% coverage: 1:296/310 of query aligns to 1:284/293 of 6jdhA
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
26% identity, 66% coverage: 54:257/310 of query aligns to 142:348/406 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 (≠ E215) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ A219) 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.
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
26% identity, 82% coverage: 1:255/310 of query aligns to 3:264/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G9), T13 (≠ S11), N14 (≠ K12), R16 (≠ A14), T140 (= T133), G189 (= G189), L216 (≠ Q207), V261 (≠ G252)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G10), G71 (≠ P66), G72 (= G67), R73 (≠ S68), S84 (≠ A79), T85 (≠ N80), L87 (vs. gap), N112 (= N105), D113 (= D106), G139 (= G132), T140 (= T133), G141 (= G134), I142 (≠ C135), E162 (= E155), H165 (= H158), E184 (= E184)
- binding calcium ion: N112 (= N105), N115 (= N108), G144 (= G137), A161 (= A154)
- 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)
26% identity, 82% coverage: 1:255/310 of query aligns to 3:264/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G9), G12 (= G10), T13 (≠ S11), N14 (≠ K12), R16 (≠ A14), T140 (= T133), G189 (= G189), L216 (≠ Q207), V261 (≠ G252)
- binding calcium ion: N112 (= N105), N115 (= N108), G144 (= G137), A161 (= A154)
- binding zinc ion: H165 (= H158), C175 (= C175), C177 (= C177), C182 (= C182)
1z6rA Crystal structure of mlc from escherichia coli (see paper)
26% identity, 66% coverage: 54:257/310 of query aligns to 118:324/382 of 1z6rA
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)
29% identity, 65% coverage: 4:204/310 of query aligns to 410:608/722 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 (≠ A14) 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
Query Sequence
>BWI76_RS27555 FitnessBrowser__Koxy:BWI76_RS27555
MKYLGLDIGGSKIAAVVMDEQGHEWRRFRVETRKQTRQQFIATLVELITAIGDELAQPLA
IGIALPGSISPQSGKIRNANIQVINGCRLQDELEQRLGQSVVLANDGNCFALSEACDGAG
ADYSLVFGMTLGTGCGGGIALNRQIFPGASGIAAECGHITLPGYQEVNDGPPARCYCGKY
NCVESFISGTGLSARYRLLTQEALSSQAIIARALEGEHAACEQVLRFRQQLARTLATVVN
LIDPGVIILGGGLSNVALLVNDLEADVAPLVFTDHFITPIVPARHGDSSGMRGAAWLAVR
SGVENETFTD
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