SitesBLAST
Comparing BPHYT_RS12010 FitnessBrowser__BFirm:BPHYT_RS12010 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 17 hits to proteins with known functional sites (download)
5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
68% identity, 100% coverage: 2:527/527 of query aligns to 3:490/490 of 5tw7F
1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
65% identity, 99% coverage: 4:527/527 of query aligns to 7:501/501 of 1gpmA
- active site: G57 (= G54), C84 (= C81), Y85 (= Y82), H179 (= H176), E181 (= E178), D237 (= D234), K357 (= K376)
- binding adenosine monophosphate: G231 (= G228), L232 (= L229), S233 (= S230), V258 (= V255), F313 (= F310)
- binding pyrophosphate 2-: S233 (= S230), G235 (= G232), V236 (= V233), D237 (= D234), S238 (= S235), K357 (= K376)
Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
42% identity, 100% coverage: 2:527/527 of query aligns to 6:555/555 of Q8IJR9
- Y18 (≠ V14) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- H20 (≠ Q16) mutation to A: Slight decrease in affinity for glutamine. 1.8-fold increase in affinity for ATP. Slight increase in affinity for XMP. Moderate reduction in glutaminase activity.
- K24 (≠ R20) mutation to L: 50 percent decrease in glutaminase activity. 5.3-fold decrease in affinity for glutamine. 1.7-fold increase in affinity for ATP. 2.8-fold decrease in affinity for XMP.
- R25 (= R21) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
- C89 (= C81) mutation to A: Loss of glutaminase activity, however, glutamine binding is not affected. In presence of exogenous ammonia, the amination of XMP to produce GMP is normal. 2.3-fold decrease in affinity for ATP and 1.8-fold decrease in affinity for XMP. 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-113.
- Q93 (= Q85) binding
- C113 (vs. gap) mutation to A: 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-89.
- K160 (= K121) mutation to L: No effect on glutaminase activity. 1.2-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.
- W167 (= W135) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
- N169 (≠ S137) binding ; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- D172 (= D140) binding ; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
- H208 (= H176) binding
- Y212 (≠ T180) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
- E213 (≠ H181) mutation to A: 40 percent decrease in glutaminase activity. 1.4-fold decrease in affinity for glutamine. 1.3-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.
- R336 (= R303) binding
- D371 (= D335) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
- E374 (= E338) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
- K376 (≠ A340) mutation to L: 20 percent decrease in glutaminase activity. 4.4-fold decrease in affinity for glutamine. 1.8-fold decrease in affinity for XMP.
- K386 (= K351) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
- T387 (≠ S352) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
- H388 (= H353) Important for ATPPase activity; mutation to A: Moderate decrease in ATP pyrophosphatase (ATPPase) activity. Reduces 49 percent decrease in glutaminase activity. Impaired GMP formation.
- H389 (= H354) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
- N390 (= N355) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
- K411 (= K376) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
- D412 (= D377) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
- D413 (≠ E378) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
- K415 (≠ R380) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
- Q476 (= Q448) binding
- R539 (= R511) mutation to L: 85 percent decrease in glutaminase activity.
- K547 (= K519) binding ; mutation to L: 85 percent decrease in glutaminase activity.
- I552 (= I524) binding
- E553 (= E525) binding ; mutation to L: 85 percent decrease in glutaminase activity.
- E555 (= E527) mutation to L: 20 percent decrease in glutaminase activity. No effect on GMP formation.
2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
48% identity, 99% coverage: 5:527/527 of query aligns to 2:475/475 of 2ywcA
- active site: G51 (= G54), R53 (≠ S56), C78 (= C81), Y79 (= Y82), H164 (= H176), E166 (= E178), D221 (= D234), K343 (= K376)
- binding xanthosine-5'-monophosphate: R288 (= R303), P366 (= P399), G367 (= G400), P368 (= P401), Q408 (= Q448), K467 (= K519), T471 (= T523), I472 (= I524), E473 (= E525)
4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
40% identity, 100% coverage: 3:527/527 of query aligns to 1:525/525 of 4wioA
- active site: G52 (= G54), A83 (≠ C81), Y84 (= Y82), H197 (= H176), E199 (= E178), D255 (= D234), K393 (= K376)
- binding glutamine: Q87 (= Q85), N158 (≠ S137), H159 (= H138), N160 (≠ G139), D161 (= D140), H197 (= H176)
3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
39% identity, 100% coverage: 2:527/527 of query aligns to 1:517/517 of 3uowA
- active site: G53 (= G54), C84 (= C81), Y85 (= Y82), H198 (= H176), E200 (= E178), D255 (= D234), K381 (= K376)
- binding xanthosine-5'-monophosphate: R325 (= R303), P404 (= P399), G405 (= G400), P406 (= P401), Q446 (= Q448), K509 (= K519), T513 (= T523), I514 (= I524), E515 (= E525)
3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
39% identity, 99% coverage: 4:527/527 of query aligns to 1:477/477 of 3uowB
- active site: G47 (= G54), C67 (= C81), Y68 (= Y82), H162 (= H176), E164 (= E178), D218 (= D234), K340 (= K376)
- binding xanthosine-5'-monophosphate: R288 (= R303), P363 (= P399), G364 (= G400), P365 (= P401), Q405 (= Q448), K469 (= K519), T473 (= T523), I474 (= I524), E475 (= E525)
2vxoB Human gmp synthetase in complex with xmp (see paper)
36% identity, 98% coverage: 5:520/527 of query aligns to 6:532/658 of 2vxoB
- active site: G55 (= G54), C82 (= C81), Y83 (= Y82), H165 (= H176), E167 (= E178), D223 (= D234), K381 (= K376)
- binding xanthosine-5'-monophosphate: R302 (= R303), G348 (= G346), K349 (vs. gap), P404 (= P399), G405 (= G400), P406 (= P401), R489 (= R466)
Sites not aligning to the query:
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
35% identity, 98% coverage: 5:520/527 of query aligns to 28:567/693 of P49915
- C104 (= C81) active site, For GATase activity
- H190 (= H176) active site, For GATase activity
- E192 (= E178) active site, For GATase activity
- R337 (= R303) binding
- D522 (= D464) binding
Sites not aligning to the query:
- 610 binding
- 685 binding
- 691 binding
6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
50% identity, 62% coverage: 203:527/527 of query aligns to 2:298/298 of 6jp9A
7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
31% identity, 37% coverage: 5:200/527 of query aligns to 2:181/183 of 7yc6A
Q42565 Anthranilate synthase beta subunit 1, chloroplastic; Anthranilate synthase component 2-1; Anthranilate synthase, glutamine amidotransferase component 2-1; Protein TRYPTOPHAN BIOSYNTHESIS 4; Protein WEAK ETHYLENE INSENSITIVE 7; EC 4.1.3.27 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
26% identity, 36% coverage: 2:193/527 of query aligns to 72:264/276 of Q42565
- G150 (= G79) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
- G176 (≠ V108) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.
P00903 Aminodeoxychorismate synthase component 2; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 2; Aminodeoxychorismate synthase, glutamine amidotransferase component; EC 2.6.1.85 from Escherichia coli (strain K12) (see paper)
26% identity, 30% coverage: 35:193/527 of query aligns to 38:185/187 of P00903
- C79 (= C81) mutation to S: 10000-fold decrease in catalytic efficiency.
- H168 (= H176) mutation to Q: Loss of activity.
- E170 (= E178) mutation to A: 150-fold decrease in catalytic efficiency.; mutation to D: 4-fold decrease in catalytic efficiency.; mutation E->K,Q: Loss of activity.
Q9LVW7 Carbamoyl phosphate synthase small chain, chloroplastic; Carbamoyl phosphate synthetase glutamine chain; Protein VENOSA 6; EC 6.3.5.5 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 34% coverage: 4:180/527 of query aligns to 243:406/430 of Q9LVW7
Sites not aligning to the query:
- 410 H→Y: In ven6-1; reticulate leaf phenotype.
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
25% identity, 36% coverage: 2:192/527 of query aligns to 3:187/673 of 8hx8A
Sites not aligning to the query:
- binding magnesium ion: 521, 655, 658
- binding tryptophan: 231, 232, 233, 241, 243, 458, 459, 460, 614
P00900 Anthranilate synthase component 2; AS; ASII; Anthranilate synthase, GATase component; Anthranilate synthase, glutamine amidotransferase component; EC 4.1.3.27 from Serratia marcescens (see 3 papers)
25% identity, 35% coverage: 5:191/527 of query aligns to 4:185/193 of P00900
- C84 (= C81) active site, Nucleophile; for GATase activity
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1i7qB Anthranilate synthase from s. Marcescens (see paper)
25% identity, 35% coverage: 5:191/527 of query aligns to 3:184/192 of 1i7qB
- active site: G58 (≠ S56), C83 (= C81), L84 (≠ Y82), H169 (= H176), E171 (= E178)
- binding glutamic acid: P55 (≠ G53), G56 (= G54), G58 (≠ S56), C83 (= C81), L84 (≠ Y82), Q87 (= Q85), H132 (= H138), S133 (≠ G139), L134 (≠ D140)
Query Sequence
>BPHYT_RS12010 FitnessBrowser__BFirm:BPHYT_RS12010
MHDKILILDFGSQVTQLIARRVREANVYSEIHPYDVDASFIRDFAPKGVILSGGPSSVTE
TDTPRVPQAVFELGVPVLGICYGMQAMAEQLGGKVDIGHLREFGYAEVRARNHTSLLEGI
KDFTTPEGHGMLKVWMSHGDKVLEMPPGFALMASTESCPIAAMADEKRHFYGLQWHPEVT
HTVQGRAMLERFVLQICGARADWEMGNYIDEAVAKIREQVGNEHVILGLSGGVDSSVAAA
LLHRAIGDQLTCVFVDHGLLRLNEAEQVMATFADHLGVKVIHVDASEVFLRKLAGVTDPE
AKRKIIGAEFVEVFQAEAGRLTDAKWLAQGTIYPDVIESAGKGKKGAQTIKSHHNVGGLP
ETLNLKLLEPLRELFKDEVRELGVKLGLPPAMVYRHPFPGPGLGVRILGEVKRDFADLLR
RADAIFIETLRTFIDKETGKSWYDLTSQAFAVFLPVKSVGVMGDGRTYEYVVALRAVQTL
DFMTAHWAHLPHELLGHVSNRIINEVRGINRVVYDISGKPPATIEWE
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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