SitesBLAST
Comparing WP_012708791.1 NCBI__GCF_000018545.1:WP_012708791.1 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)
P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
51% identity, 95% coverage: 13:393/401 of query aligns to 4:378/382 of P0A6F1
- S47 (= S56) binding L-glutamine
- G241 (= G255) binding L-glutamine
- G243 (= G257) binding L-glutamine
- L270 (= L285) binding L-glutamine
- Q273 (= Q288) binding L-glutamine
- N311 (= N326) binding L-glutamine
- G313 (= G328) binding L-glutamine
- F314 (= F329) binding L-glutamine
1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
51% identity, 95% coverage: 13:393/401 of query aligns to 3:377/379 of 1ce8B
1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
50% identity, 95% coverage: 13:393/401 of query aligns to 3:377/379 of 1c3oB
- active site: K201 (= K216), S268 (≠ C284), H352 (= H368), E354 (= E370)
- binding glutamine: S46 (= S56), N239 (= N254), G240 (= G255), G242 (= G257), S268 (≠ C284), L269 (= L285), N310 (= N326), H311 (= H327), G312 (= G328), F313 (= F329)
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)
45% identity, 97% coverage: 7:393/401 of query aligns to 53:427/430 of Q9LVW7
- H410 (≠ Q376) mutation to Y: In ven6-1; reticulate leaf phenotype.
Q09794 Multifunctional protein ura1; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
36% identity, 96% coverage: 16:398/401 of query aligns to 61:452/2244 of Q09794
Sites not aligning to the query:
- 1119 modified: Phosphoserine
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
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)
39% identity, 93% coverage: 16:387/401 of query aligns to 11:380/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
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)
38% identity, 94% coverage: 14:391/401 of query aligns to 2:359/2225 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.
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)
36% identity, 94% coverage: 14:391/401 of query aligns to 2:359/2225 of P27708
- A2 (= A14) modified: N-acetylalanine
- M33 (≠ L45) to R: in DEE50; uncertain significance; dbSNP:rs751610198
- R177 (= R184) to Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 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
Q18990 Multifunctional protein pyr-1; 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 Caenorhabditis elegans (see 3 papers)
37% identity, 95% coverage: 14:394/401 of query aligns to 3:365/2198 of Q18990
Sites not aligning to the query:
- 1602 H→Q: In cu8; probable loss of dihydroorotase activity. Severe late stage embryonic lethality in 50% of animals. The few surviving mutants have a shorter and thicker pharyngeal isthmus, an abnormal knobbed tail, mild egg-laying defects, moderate fluid accumulation in the coelom and a slower growth. Actin and intermediate filaments are disorganized in the pharynx. Moderate reduction in heparan sulfate levels and increased levels of chondroitin sulfate. In an umps-1 zu456 mutant background, prevents the formation of abnormally enlarged gut granules in embryos. Complete embryonic lethality in a rnst-2 qx245 mutant background.
P07258 Carbamoyl phosphate synthase arginine-specific small chain; CPS; CPSase; CPSase-arg; Arginine-specific carbamoyl phosphate synthetase, glutamine chain; Carbamoyl phosphate synthase A; CPS-A; Glutamine-dependent carbamoyl phosphate synthetase; EC 6.3.5.5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
36% identity, 95% coverage: 14:393/401 of query aligns to 8:374/411 of P07258
- C264 (= C284) mutation to D: Abolishes glutamine-dependent CPSase activity.
- H307 (= H327) mutation to D: Abolishes glutamine-dependent CPSase activity.
- H349 (= H368) mutation to D: Abolishes glutamine-dependent CPSase activity.
P07259 Multifunctional protein URA2; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
34% identity, 97% coverage: 5:393/401 of query aligns to 13:411/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
P05990 Multifunctional protein r; Protein rudimentary; 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 Drosophila melanogaster (Fruit fly) (see 2 papers)
37% identity, 94% coverage: 16:392/401 of query aligns to 8:377/2224 of P05990
Sites not aligning to the query:
- 1167 E→K: Severely diminishes UTP inhibition of CPSase; in Su(b).
- 1883 modified: Phosphoserine
- 1885 modified: Phosphoserine
- 1892 modified: Phosphoserine
- 1894 modified: Phosphoserine
Q8C196 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Mus musculus (Mouse) (see 2 papers)
35% identity, 97% coverage: 8:394/401 of query aligns to 40:403/1500 of Q8C196
- K44 (≠ P12) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- K287 (vs. gap) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
Sites not aligning to the query:
- 1291 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
P07756 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Rattus norvegicus (Rat) (see 2 papers)
35% identity, 97% coverage: 8:394/401 of query aligns to 40:403/1500 of P07756
Sites not aligning to the query:
- 537 modified: carbohydrate, O-linked (GlcNAc) serine; alternate
- 1331 modified: carbohydrate, O-linked (GlcNAc) serine
- 1332 modified: carbohydrate, O-linked (GlcNAc) threonine
- 1391 T→V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- 1394 T→A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- 1410 W→K: 60-fold increase in the activation constant of NAG.
- 1437 N→D: 70-fold increase in the activation constant of NAG.
- 1440 N→D: 110-fold increase in the activation constant of NAG. Modifies the specificity for the activator: Binds Phe-NAG considerably better than NAG.
P31327 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Homo sapiens (Human) (see 22 papers)
34% identity, 98% coverage: 1:394/401 of query aligns to 23:403/1500 of P31327
- K55 (≠ V23) modified: N6-glutaryllysine; alternate
- S123 (vs. gap) to F: in CPS1D; modestly decreases enzyme activity; to Y: in CPS1D; uncertain significance
- K171 (≠ A133) modified: N6-glutaryllysine; alternate
- R174 (= R136) to W: in CPS1D; uncertain significance; dbSNP:rs1553509661
- K176 (≠ N138) modified: N6-glutaryllysine
- K207 (≠ S179) modified: N6-glutaryllysine; alternate
- K210 (≠ S182) modified: N6-glutaryllysine; alternate
- K214 (≠ E194) modified: N6-glutaryllysine; alternate
- K219 (≠ H207) modified: N6-glutaryllysine; alternate
- K228 (= K216) modified: N6-glutaryllysine; alternate
- K237 (≠ G225) modified: N6-glutaryllysine
- K280 (vs. gap) modified: N6-glutaryllysine; alternate
- A304 (≠ L294) to V: in CPS1D; associated with T-986; dbSNP:rs775920437
- K307 (= K297) modified: N6-glutaryllysine; alternate
- K310 (= K300) modified: N6-glutaryllysine; alternate
- H337 (= H327) to R: in CPS1D; modestly decreases enzyme activity; dbSNP:rs28940283
- T344 (≠ S335) to A: no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs1047883
- N355 (≠ S346) to D: in CPS1D; around 80% decrease in enzyme activity; significant reduction in thermal stability; approximately 4-fold decrease in the apparent Vmax for ATP, bicarbonate and ammonia; dbSNP:rs1472190012
- Y389 (= Y380) to C: in CPS1D; around 40% decrease in enzyme activity; significant loss of thermal stability
- L390 (= L381) to R: in CPS1D; significant loss of protein stability
- G401 (≠ K392) to R: in CPS1D; uncertain significance; associated with N-937 in a patient; dbSNP:rs760895692
- K402 (= K393) modified: N6-glutaryllysine; alternate
Sites not aligning to the query:
- 412 modified: N6-glutaryllysine; alternate
- 438 A → P: in CPS1D; almost complete loss of enzyme activity; dbSNP:rs772497399
- 453 modified: N6-glutaryllysine; alternate
- 458 modified: N6-glutaryllysine; alternate
- 527 modified: N6-glutaryllysine; alternate
- 530 G → V: found in a patient with VACTERL syndrome and postsurgical PHN; uncertain significance; dbSNP:rs1250316045
- 532 modified: N6-glutaryllysine; alternate
- 544 T → M: in CPS1D; almost complete loss of enzyme activity; approximately 60-fold increase in the apparent Km for bicarbonate and approximately 4-fold respective decrease and increase in the apparent Vmax and Km for ammonia; dbSNP:rs121912592
- 553 modified: N6-glutaryllysine; alternate
- 678 Q → P: in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding
- 728 modified: N6-glutaryllysine
- 757 modified: N6-glutaryllysine; alternate
- 772 modified: N6-glutaryllysine; alternate
- 774 P → L: in CPS1D; the enzyme is inactive
- 793 modified: N6-glutaryllysine; alternate
- 811 modified: N6-glutaryllysine; alternate
- 841 modified: N6-glutaryllysine; alternate
- 843 L → S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
- 850 R → C: in CPS1D; moderate decrease in protein yield and partial loss of enzyme activity; dbSNP:rs1015051007; R → H: in CPS1D; partial loss of enzyme activity; dbSNP:rs767694281
- 856 modified: N6-glutaryllysine; alternate
- 869 modified: N6-glutaryllysine
- 871 T → P: in CPS1D; significant decrease in protein yield and enzyme activity
- 875 modified: N6-glutaryllysine; alternate; K → E: associated in cis with S-843 in a patient with carbamoyl-phosphate synthase deficiency; does not affect enzyme activity; significant decrease in protein yield and thermal stability; dbSNP:rs147062907
- 889 modified: N6-glutaryllysine; alternate
- 892 modified: N6-glutaryllysine; alternate
- 905 modified: N6-glutaryllysine
- 908 modified: N6-glutaryllysine; alternate
- 911 G → E: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs1388955593; G → V: in CPS1D; significant decrease in protein yield and enzyme activity
- 913 S → L: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs754706559
- 914 D → G: in CPS1D; significant decrease in protein yield and enzyme activity; D → H: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs765484849
- 915 modified: N6-glutaryllysine; alternate
- 918 S → P: in CPS1D; significant decrease in protein yield and enzyme activity
- 919 modified: N6-glutaryllysine; alternate
- 932 R → T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
- 937 I → N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
- 949 A → T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
- 958 L → P: in CPS1D; significant decrease in protein yield and enzyme activity
- 959 Y → C: in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity; dbSNP:rs1191587211
- 962 Y → C: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs955666400
- 964 G → D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
- 986 I → T: in CPS1D; associated with V-304; dbSNP:rs1553516442
- 987 G → C: in CPS1D; may affect splicing; dbSNP:rs1553516443
- 1074 modified: N6-glutaryllysine; alternate
- 1150 modified: N6-glutaryllysine
- 1168 modified: N6-glutaryllysine; alternate
- 1183 modified: N6-glutaryllysine; alternate
- 1215 I → V: in CPS1D; uncertain significance; dbSNP:rs141373204
- 1224 modified: N6-glutaryllysine
- 1254 I → F: in CPS1D; uncertain significance
- 1266 F → S: in dbSNP:rs1047886
- 1283 M → L: in dbSNP:rs1047887
- 1356 modified: N6-glutaryllysine; alternate
- 1360 modified: N6-glutaryllysine; alternate
- 1363:1366 natural variant: Missing (in CPS1D; uncertain significance)
- 1376 G → S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- 1378 A → T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
- 1381 L → S: in CPS1D; significant loss of protein stability
- 1406 T → N: probable risk factor for PHN; dbSNP:rs1047891
- 1411 P → L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773
- 1443 T → A: in CPS1D; almost complete loss of enzyme activity; approximately 10-fold decrease in the apparent Vmax for bicarbonate, ammonia and ATP; decreased affinity for NAG
- 1453 R → Q: in CPS1D; the enzyme is inactive; R → W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
- 1479 modified: N6-glutaryllysine; alternate
- 1486 modified: N6-glutaryllysine; alternate
- 1491 Y → H: in CPS1D; triggers a large decrease in the apparent affinity for N-acetyl-L-glutamate (NAG); dbSNP:rs1553519513
6w2jB Cps1 bound to allosteric inhibitor h3b-374 (see paper)
35% identity, 95% coverage: 13:394/401 of query aligns to 3:361/1364 of 6w2jB
Sites not aligning to the query:
- active site: 593, 607, 609, 615, 811, 937, 1055, 1191
- binding (2-fluoranyl-4-methoxy-phenyl)-[(3~{R},5~{R})-4-(2-fluoranyl-4-methoxy-phenyl)carbonyl-3,5-dimethyl-piperazin-1-yl]methanone: 547, 549, 557, 668, 669, 672, 673, 698, 702, 705, 706, 737, 739, 740
6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
35% identity, 95% coverage: 13:394/401 of query aligns to 3:361/1422 of 6w2jA
Sites not aligning to the query:
- active site: 651, 665, 667, 673, 869, 995, 1113, 1249
- binding (2-fluoranyl-4-methoxy-phenyl)-[(3~{R},5~{R})-4-(2-fluoranyl-4-methoxy-phenyl)carbonyl-3,5-dimethyl-piperazin-1-yl]methanone: 605, 607, 615, 725, 726, 727, 730, 732, 756, 760, 763, 764, 795, 797, 798
6uelA Cps1 bound to allosteric inhibitor h3b-193 (see paper)
35% identity, 95% coverage: 13:394/401 of query aligns to 3:361/1333 of 6uelA
Sites not aligning to the query:
- active site: 587, 601, 603, 609, 803, 929, 1032, 1168
- binding N~1~-[(4-fluorophenyl)methyl]-N~1~-methyl-N~4~-(4-methyl-1,3-thiazol-2-yl)piperidine-1,4-dicarboxamide: 544, 551, 662, 663, 665, 690, 698, 701, 729, 731, 732
5douD Crystal structure of human carbamoyl phosphate synthetase i (cps1), ligand-bound form (see paper)
35% identity, 95% coverage: 13:394/401 of query aligns to 3:361/1430 of 5douD
Sites not aligning to the query:
- active site: 505, 545, 576, 589, 617, 656, 658, 672, 674, 676, 680, 880, 1006, 1087, 1116, 1124, 1184, 1196, 1198, 1203, 1260
- binding adenosine-5'-diphosphate: 505, 543, 545, 550, 551, 552, 581, 583, 584, 585, 589, 614, 615, 616, 617, 658, 671, 672, 1085, 1110, 1111, 1116, 1140, 1142, 1143, 1144, 1184, 1186, 1195, 1196
- binding magnesium ion: 658, 672, 672, 674
- binding n-acetyl-l-glutamate: 1307, 1308, 1332, 1334, 1335, 1351, 1379, 1384, 1385, 1386, 1390
- binding phosphate ion: 550, 551, 617, 672, 674, 676, 679
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)
31% identity, 42% coverage: 218:387/401 of query aligns to 14:186/187 of P00903
- C79 (= C284) mutation to S: 10000-fold decrease in catalytic efficiency.
- H168 (= H368) mutation to Q: Loss of activity.
- E170 (= E370) 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.
Query Sequence
>WP_012708791.1 NCBI__GCF_000018545.1:WP_012708791.1
MTATPAWTTQKPTALLVLADGTVIEGKGIGATGKVQAEVCFNTALTGYQEILTDPSYLGQ
IVTFTFPHIGNIGANDEDIEDLTPAARHGAVGVIFKADITDPSNYRAAKHLDAWLKARGV
IGLCGIDTRALTAWIRENGMPNAVIAHDPSGVFDIQTLKAEAKAWSGLVGLDLAKVATSG
QSYRWNEKPWAWNEGHATLGETEAAYHVVALDYGVKRNILRLFAGLDCRVTVVPAATSAD
EVLALKPDGIFLSNGPGDPAATGEYAVPVIKNLLKSDIPVFGICLGHQMLALALGAKTEK
MHQGHHGANHPVKDHTTGKVEIVSMNHGFAVDSKSLPEGVEETHISLFDGTNCGLRVNGK
PVFSVQHHPEASPGPQDSHYLFRRFLNLIREKKGEPALAER
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