SitesBLAST
Comparing 209647 MicrobesOnline__882:209647 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 19 hits to proteins with known functional sites (download)
P78753 Probable asparagine synthetase [glutamine-hydrolyzing]; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
25% identity, 49% coverage: 1:438/889 of query aligns to 1:401/557 of P78753
- S391 (≠ W428) modified: Phosphoserine
Sites not aligning to the query:
- 489 modified: Phosphoserine
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
25% identity, 41% coverage: 70:437/889 of query aligns to 45:376/497 of 1ct9A
- active site: L50 (= L75), N74 (= N98), G75 (= G99), T305 (≠ S370), R308 (≠ W373), E332 (≠ H397), M366 (≠ I427)
- binding adenosine monophosphate: L232 (≠ C294), L233 (= L295), S234 (= S296), S239 (= S301), A255 (≠ S319), V256 (≠ I320), D263 (≠ L333), M316 (≠ L381), S330 (= S395), G331 (= G396), E332 (≠ H397)
- binding glutamine: R49 (= R74), L50 (= L75), I52 (= I77), V53 (≠ L78), N74 (= N98), G75 (= G99), E76 (= E100), D98 (= D123)
Sites not aligning to the query:
P22106 Asparagine synthetase B [glutamine-hydrolyzing]; AS-B; EC 6.3.5.4 from Escherichia coli (strain K12) (see 2 papers)
25% identity, 49% coverage: 1:437/889 of query aligns to 1:393/554 of P22106
- M1 (= M1) modified: Initiator methionine, Removed
- C2 (= C2) mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.
- H30 (= H29) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y104) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (= A129) mutation to H: Little effect on the kinetic properties.
- E349 (≠ H397) mutation E->A,Q: Loss of glutamine- and ammonia-dependent synthetase activity, but still exhibits glutaminase activity.; mutation to D: 5-fold increase in affinity for aspartate when assaying both the glutamine- and ammonia-dependent synthetase reactions, and 2-fold decrease in kcat for these reactions. Modifies the product glutamate/asparagine stoichiometry.
P08243 Asparagine synthetase [glutamine-hydrolyzing]; Cell cycle control protein TS11; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Homo sapiens (Human) (see 7 papers)
25% identity, 46% coverage: 1:412/889 of query aligns to 1:380/561 of P08243
- C2 (= C2) active site, For GATase activity; mutation to A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
- A6 (≠ G6) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ L242) to E: in dbSNP:rs1049674
- F362 (≠ M394) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973
Sites not aligning to the query:
- 550 R → C: in ASNSD; increases level of protein abundance; dbSNP:rs398122974
6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
24% identity, 46% coverage: 2:412/889 of query aligns to 1:367/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L75), N74 (= N98), G75 (= G99), T324 (≠ S370), R327 (≠ W373)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R74), V51 (≠ I77), V52 (≠ L78), Y73 (≠ F97), N74 (= N98), G75 (= G99), E76 (= E100), V95 (≠ G122), D96 (= D123)
Q9L9F2 Demethyldecarbamoylnovobiocin O-methyltransferase; Novobiocin biosynthesis protein P; EC 2.1.1.285 from Streptomyces niveus (Streptomyces spheroides) (see paper)
28% identity, 20% coverage: 679:854/889 of query aligns to 71:238/262 of Q9L9F2
Sites not aligning to the query:
2wk1A Structure of the o-methyltransferase novp (see paper)
28% identity, 20% coverage: 679:854/889 of query aligns to 51:218/242 of 2wk1A
- binding s-adenosyl-l-homocysteine: E72 (= E700), G74 (= G702), V75 (≠ C703), W76 (≠ A704), D102 (= D726), S103 (≠ V727), G106 (≠ C730), P108 (= P732), W157 (≠ L795), F158 (≠ Y796), D176 (= D812), G177 (≠ C813), S182 (= S818)
Sites not aligning to the query:
4x7uA Mycf mycinamicin iii 3'-o-methyltransferase in complex with mg, sah and mycinamicin iii (substrate) (see paper)
30% identity, 19% coverage: 689:854/889 of query aligns to 67:228/252 of 4x7uA
- binding magnesium ion: D187 (= D812), D214 (= D839), D215 (= D840)
- binding s-adenosyl-l-homocysteine: E81 (= E700), G83 (= G702), V84 (≠ C703), W85 (≠ A704), D111 (= D726), S112 (≠ V727), G115 (≠ C730), L141 (= L757), W168 (≠ L795), F169 (≠ Y796), D187 (= D812)
- binding mycinamicin iii: L132 (≠ V748), Y135 (≠ A751), D189 (= D814), D215 (= D840)
Sites not aligning to the query:
4x7xA Mycf mycinamicin iii 3'-o-methyltransferase (e35q, e139a variant) in complex with mg, sah and macrocin (see paper)
30% identity, 19% coverage: 689:854/889 of query aligns to 66:227/250 of 4x7xA
- binding 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-6-[(2R,3R,4R,5S,6R)-4-(dimethylamino)-5-[(2S,4R,5S,6S)-4,6-dimethyl-4,5-bis(oxidanyl)oxan-2-yl]oxy-6-methyl-3-oxidanyl-oxan-2-yl]oxy-16-ethyl-15-[[(2R,3R,4R,5S,6R)-3-methoxy-6-methyl-4,5-bis(oxidanyl)oxan-2-yl]oxymethyl]-5,9,13-trimethyl-4-oxidanyl-2,10-bis(oxidanylidene)-1-oxacyclohexadeca-11,13-dien-7-yl]ethanal: L131 (≠ V748), Y134 (≠ A751), D188 (= D814), D214 (= D840)
- binding magnesium ion: D186 (= D812), D213 (= D839), D214 (= D840)
- binding s-adenosyl-l-homocysteine: E80 (= E700), G82 (= G702), V83 (≠ C703), W84 (≠ A704), D110 (= D726), S111 (≠ V727), G114 (≠ C730), F115 (≠ I731), W167 (≠ L795), F168 (≠ Y796), D186 (= D812)
Sites not aligning to the query:
- binding 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-6-[(2R,3R,4R,5S,6R)-4-(dimethylamino)-5-[(2S,4R,5S,6S)-4,6-dimethyl-4,5-bis(oxidanyl)oxan-2-yl]oxy-6-methyl-3-oxidanyl-oxan-2-yl]oxy-16-ethyl-15-[[(2R,3R,4R,5S,6R)-3-methoxy-6-methyl-4,5-bis(oxidanyl)oxan-2-yl]oxymethyl]-5,9,13-trimethyl-4-oxidanyl-2,10-bis(oxidanylidene)-1-oxacyclohexadeca-11,13-dien-7-yl]ethanal: 46, 53, 243
- binding s-adenosyl-l-homocysteine: 52, 53, 54
4x7wA Mycf mycinamicin iii 3'-o-methyltransferase (e35q, e139a variant) in complex with mg, sah and mycinamicin vi (myce substrate) (see paper)
30% identity, 19% coverage: 689:854/889 of query aligns to 66:227/250 of 4x7wA
- binding magnesium ion: D186 (= D812), D213 (= D839), D214 (= D840)
- binding Mycinamicin VI: L131 (≠ V748), Y134 (≠ A751), D188 (= D814), D214 (= D840)
- binding s-adenosyl-l-homocysteine: E80 (= E700), G82 (= G702), V83 (≠ C703), W84 (≠ A704), D110 (= D726), S111 (≠ V727), G114 (≠ C730), F115 (≠ I731), L140 (= L757), W167 (≠ L795), F168 (≠ Y796), D186 (= D812)
Sites not aligning to the query:
4x7vA Mycf mycinamicin iii 3'-o-methyltransferase (e35q, e139a variant) in complex with mg, sah and mycinamicin iv (product) (see paper)
30% identity, 19% coverage: 689:854/889 of query aligns to 67:228/252 of 4x7vA
- binding magnesium ion: D187 (= D812), D214 (= D839), D215 (= D840)
- binding mycinamicin iv: L132 (≠ V748), Y135 (≠ A751), D187 (= D812), D189 (= D814), D215 (= D840)
- binding s-adenosyl-l-homocysteine: E81 (= E700), G83 (= G702), V84 (≠ C703), W85 (≠ A704), D111 (= D726), S112 (≠ V727), G115 (≠ C730), L141 (= L757), W168 (≠ L795), F169 (≠ Y796), D187 (= D812)
Sites not aligning to the query:
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
27% identity, 22% coverage: 2:195/889 of query aligns to 1:199/460 of 6lbpA
Sites not aligning to the query:
- active site: 243, 301, 306, 316, 424
- binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437
Q9STG9 Amidophosphoribosyltransferase 2, chloroplastic; AtATase2; AtPURF2; PRPP2; Glutamine phosphoribosylpyrophosphate amidotransferase 2; AtGPRAT2; Protein CHLOROPLAST IMPORT APPARATUS 1; Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS; EC 2.4.2.14 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 22% coverage: 2:195/889 of query aligns to 87:285/561 of Q9STG9
- H187 (≠ F97) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K168) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P169) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494.
Sites not aligning to the query:
- 371 G→S: Low resistance to the bleaching herbicides DAS073 and DAS734.
- 476 P→S: Resistance to the bleaching herbicides DAS073 and DAS734.
- 494 Y→F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265.
4ce0A Crystal structure of sah-bound spinosyn rhamnosyl 4'-o- methyltransferase spnh from saccharopolyspora spinosa
28% identity, 20% coverage: 679:854/889 of query aligns to 34:190/213 of 4ce0A
- binding magnesium ion: D149 (= D812), D176 (= D839), D177 (= D840)
- binding s-adenosyl-l-homocysteine: E55 (= E700), G57 (= G702), W59 (≠ A704), D85 (= D726), S86 (≠ V727), G89 (≠ C730), M90 (≠ I731), W130 (≠ L795), F131 (≠ Y796), D149 (= D812), S155 (= S818)
Sites not aligning to the query:
5i10A Crystal structure of spinosyn rhamnosyl 4'-o-methyltransferase spnh mutant t242q from saccharopolyspora spinosa
33% identity, 12% coverage: 750:854/889 of query aligns to 65:168/192 of 5i10A
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
30% identity, 14% coverage: 83:207/889 of query aligns to 93:222/476 of P00497
Sites not aligning to the query:
- 1:11 modified: propeptide
- 12 active site, Nucleophile; C→F: Loss of enzyme activity and N-terminal processing.
- 247 binding
- 294 binding
- 356 binding
- 357 binding
- 393 binding
- 394 F→V: Partial loss of activity.
- 442 D→S: Partial loss of activity.
- 448 binding ; C→S: Loss of activity.
- 451 binding ; C→S: Loss of activity.
- 452 F→C: Lethal.
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
30% identity, 14% coverage: 83:207/889 of query aligns to 82:211/465 of 1gph1
Sites not aligning to the query:
- active site: 300, 305, 315, 423
- binding adenosine monophosphate: 242, 242, 244, 245, 246, 282, 283, 283, 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
- binding iron/sulfur cluster: 236, 237, 382, 384, 388, 437, 440
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
30% identity, 14% coverage: 83:207/889 of query aligns to 78:207/455 of 1ao0A
Sites not aligning to the query:
- active site: 1, 27, 238, 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 25, 238, 240, 241, 242, 277, 278, 279, 300, 301, 301, 303
- binding magnesium ion: 279, 341, 342
- binding iron/sulfur cluster: 232, 233, 234, 378, 380, 433, 436
4xvzC Mycf mycinamicin iii 3'-o-methyltransferase in complex with mg (see paper)
28% identity, 19% coverage: 689:854/889 of query aligns to 43:176/203 of 4xvzC
Query Sequence
>209647 MicrobesOnline__882:209647
MCGIAGIISRKDRNVSSQPLNRMLTSQEHRGPDAGYGVSFRRQSTGAFAAGRRHSADALA
AGLEPAPVWLGHRRLSILDLSDKSAQPLRRGDLHIVFNGELFNYIELRSELTALGEHFET
SGDTEVLLASYRHWGAGCLERFNGIFAFAIFDASRGSLFAARDPFGVKPFHYGVKPFHYA
VTHDFLIFASEIKAISASGLVLRKWDPDVASAYLSYALTTAPQGRTFFENIRQIPPGHCL
TLASPDDEPSVTRYYAPRITETPRSLHELVDEGAGLIRQSCRIRMRSDRDVGLCLSSGID
SANVAAALVAEGIAPECYSIDAASSSMLDEFPLITALADKLGLHVNPIRHPDAIPTADIV
RYMLFNDEPSLFWGSYNQFHLYREMRKLGVIVSMSGHGGDELFCGYQRYYPAVVRDMLAQ
RRIMSLIWWCLRQSRHLMQDRRTIRSTWDSYSHPLGWANDYAHDIAALHLKHTIADPEEW
ISTFVGASSWGEQQQKSLFTYELQYLLRDADRNSMAHGIEERVPLLDTRLYEFCASVPLK
DLCQDGYLKGLARQLFPAIPESLRFHQIKRGLYTDISSKLPQLQADLMPLVHRSPLLREL
VDLQKLPQQLPGIVWWRLCSLAVLDVSGIEEWTAQTPLPRLVDDEMAERIGGVPSGTGRT
AVIRHVLDEGLSYLEPGALHGLAETVGLIESAAIPGCIIEAGCALGGSTMVLATAKAKER
PLHVFDVFGCIPPPGSNDGEEARARFAVIAAGESTGLNGKRYYGYEPDLLKNVQDNFVAL
GLPPAEHGITFVPGLYENTLYPSGPVALAHIDCDWYQSVKTCLERIAPHISPGGRMIIDD
YDHYSGCRRAVDEFLEASNGQFIRERYARVHLVRTKADGQETDVHRPGD
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