SitesBLAST
Comparing WP_013010467.1 NCBI__GCF_000025725.1:WP_013010467.1 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)
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)
43% identity, 97% coverage: 1:180/186 of query aligns to 1:186/187 of P00903
- C79 (= C75) mutation to S: 10000-fold decrease in catalytic efficiency.
- H168 (= H162) mutation to Q: Loss of activity.
- E170 (= E164) 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.
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)
37% identity, 97% coverage: 2:181/186 of query aligns to 75:266/276 of Q42565
- G150 (= G73) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
- G176 (= G98) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.
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)
36% identity, 96% coverage: 2:179/186 of query aligns to 4:187/193 of P00900
- C84 (= C75) 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)
36% identity, 96% coverage: 2:179/186 of query aligns to 3:186/192 of 1i7qB
- active site: G58 (≠ S50), C83 (= C75), L84 (= L76), H169 (= H162), E171 (= E164)
- binding glutamic acid: P55 (= P47), G56 (= G48), G58 (≠ S50), C83 (= C75), L84 (= L76), Q87 (= Q79), H132 (= H125), S133 (= S126), L134 (= L127)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
37% identity, 96% coverage: 3:181/186 of query aligns to 7:190/673 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
7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
29% identity, 98% coverage: 1:183/186 of query aligns to 1:179/183 of 7yc6A
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
32% identity, 96% coverage: 3:181/186 of query aligns to 6:147/632 of 8hx9A
Sites not aligning to the query:
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: 453, 454, 455, 456, 547, 570, 590, 603, 604, 605, 606, 619, 623
- binding tryptophan: 189, 190, 191, 199, 201, 419, 420, 421, 574, 575
1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
27% identity, 85% coverage: 29:186/186 of query aligns to 39:204/501 of 1gpmA
Sites not aligning to the query:
- active site: 237, 357
- binding adenosine monophosphate: 231, 232, 233, 258, 313
- binding pyrophosphate 2-: 233, 235, 236, 237, 238, 357
2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
29% identity, 78% coverage: 41:185/186 of query aligns to 44:187/475 of 2ywcA
Sites not aligning to the query:
3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
28% identity, 97% coverage: 3:182/186 of query aligns to 4:219/517 of 3uowA
Sites not aligning to the query:
Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
27% identity, 97% coverage: 3:182/186 of query aligns to 9:229/555 of Q8IJR9
- Y18 (≠ T12) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- H20 (≠ N14) 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 (≠ L18) 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 (= R20) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
- C89 (= C75) 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 (= Q79) binding L-glutamine
- C113 (≠ K99) 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 (= K116) 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 (vs. gap) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
- N169 (≠ R123) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- D172 (≠ S126) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
- H208 (= H162) binding L-glutamine
- Y212 (≠ I166) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
- E213 (≠ L167) 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.
Sites not aligning to the query:
- 336 binding XMP
- 371 Important for ATPPase activity; D→A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
- 374 E→L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
- 376 K→L: 20 percent decrease in glutaminase activity. 4.4-fold decrease in affinity for glutamine. 1.8-fold decrease in affinity for XMP.
- 386 K→L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
- 387 T→A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
- 388 Important for ATPPase activity; H→A: Moderate decrease in ATP pyrophosphatase (ATPPase) activity. Reduces 49 percent decrease in glutaminase activity. Impaired GMP formation.
- 389 Important for ATPPase activity; H→A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
- 390 N→A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
- 411 K→L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
- 412 D→A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
- 413 D→A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
- 415 K→L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
- 476 binding XMP
- 539 R→L: 85 percent decrease in glutaminase activity.
- 547 binding XMP; K→L: 85 percent decrease in glutaminase activity.
- 552 binding XMP
- 553 binding XMP; E→L: 85 percent decrease in glutaminase activity.
- 555 E→L: 20 percent decrease in glutaminase activity. No effect on GMP formation.
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
29% identity, 75% coverage: 40:179/186 of query aligns to 69:207/693 of P49915
- C104 (= C75) active site, For GATase activity
- H190 (= H162) active site, For GATase activity
- E192 (= E164) active site, For GATase activity
Sites not aligning to the query:
- 337 binding XMP
- 522 binding XMP
- 610 binding XMP
- 685 binding XMP
- 691 binding XMP
P27708 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
29% identity, 83% coverage: 11:164/186 of query aligns to 185:338/2225 of P27708
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 33 M → R: in DEE50; uncertain significance; dbSNP:rs751610198
- 177 R → Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292
- 456 modified: Phosphothreonine; by MAPK1
- 735 Y → C: in a colorectal cancer sample; somatic mutation
- 1406 modified: Phosphoserine; by PKA
- 1471 binding Zn(2+); binding Zn(2+); H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
- 1473 binding Zn(2+); H→A: No zinc-binding and no catalytic activity.
- 1475 binding (S)-dihydroorotate
- 1505 binding (S)-dihydroorotate
- 1512 D→N: No change in catalytic activity.
- 1556 binding via carbamate group; binding via carbamate group; modified: N6-carboxylysine
- 1562 T→A: Abolishes dihydroorotase activity.
- 1563 F→A: Abolishes dihydroorotase activity.
- 1590 binding Zn(2+); H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
- 1613 binding Zn(2+); C→S: Reduces dihydroorotase activity.
- 1614 binding Zn(2+); H→A: Abolishes dihydroorotase activity.
- 1637 binding Zn(2+); E→T: Abolishes dihydroorotase activity.
- 1642 H→N: 11.5% of wild-type catalytic activity.
- 1661 binding (S)-dihydroorotate
- 1686 binding Zn(2+); D→N: Abolishes dihydroorotase activity.
- 1690 binding (S)-dihydroorotate; H→N: 3% of wild-type catalytic activity.
- 1702 binding (S)-dihydroorotate
- 1789:2225 natural variant: Missing (in DEE50; uncertain significance)
- 1859 modified: Phosphoserine; by RPS6KB1 and PKA
- 1873 modified: Phosphoserine; by PKC; in vitro; S→A: Abolishes PMA-induced Thr-456 phosphorylation.
- 1900 modified: Phosphoserine
3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
29% identity, 97% coverage: 3:182/186 of query aligns to 2:183/477 of 3uowB
Sites not aligning to the query:
5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
29% identity, 78% coverage: 41:185/186 of query aligns to 48:195/490 of 5tw7F
Sites not aligning to the query:
4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
27% identity, 97% coverage: 3:182/186 of query aligns to 3:218/525 of 4wioA
Sites not aligning to the query:
2vxoB Human gmp synthetase in complex with xmp (see paper)
27% identity, 75% coverage: 40:179/186 of query aligns to 47:182/658 of 2vxoB
Sites not aligning to the query:
- active site: 223, 381
- binding xanthosine-5'-monophosphate: 302, 348, 349, 404, 405, 406, 489, 575, 610, 650, 654, 655, 656
P08955 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
28% identity, 83% coverage: 11:164/186 of query aligns to 185:338/2225 of P08955
Sites not aligning to the query:
- 1406 modified: Phosphoserine; by PKA; S→A: No effect on enzyme kinetics.; S→D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.
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)
24% identity, 75% coverage: 42:181/186 of query aligns to 285:422/430 of Q9LVW7
- H410 (= H170) mutation to Y: In ven6-1; reticulate leaf phenotype.
P20054 Multifunctional protein pyr1-3; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Dictyostelium discoideum (Social amoeba)
27% identity, 84% coverage: 27:183/186 of query aligns to 227:384/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
Query Sequence
>WP_013010467.1 NCBI__GCF_000025725.1:WP_013010467.1
MFLMVDNYDSFTYNLVALFRLNGAKVDVIRNTEYKDANEYQGIILSPGPSNPANSGSTLE
YLDKYAGRTPIFGVCLGMQSIGHYLGYEVRRAKSVMHGKVDNIKLTGDSKILSGVKDDFA
TVRYHSLAVAAPEEMIIAKASADGECMAIEDDSKLLYGVQFHPESILSEHGDSIVKNFMN
ICGVEA
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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