SitesBLAST
Comparing PP_1379 FitnessBrowser__Putida:PP_1379 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)
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
42% identity, 96% coverage: 3:434/450 of query aligns to 15:460/476 of A0A0K2JL82
- N93 (= N76) mutation to A: Slight decrease in activity.
- D125 (= D108) mutation D->N,V: Almost loss of activity.
- R137 (≠ D120) binding
- R140 (≠ D123) binding
- R201 (= R184) binding
- H253 (= H227) mutation to A: Loss of activity.
- S302 (= S276) mutation to A: Loss of activity.
- K308 (= K282) binding ; mutation to A: Loss of activity.
- N310 (= N284) binding ; mutation to A: Loss of activity.
- R341 (= R315) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
41% identity, 96% coverage: 3:434/450 of query aligns to 1:429/439 of 5xnzA
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
30% identity, 96% coverage: 10:441/450 of query aligns to 4:424/427 of 2x75A
Sites not aligning to the query:
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
30% identity, 94% coverage: 10:433/450 of query aligns to 5:420/431 of P12047
- H89 (= H101) mutation to Q: Abolishes enzyme activity.
- H141 (≠ W153) mutation to Q: Abolishes enzyme activity.
- Q212 (= Q229) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N284) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R315) mutation R->K,Q: Abolishes enzyme activity.
Q9X0I0 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
27% identity, 94% coverage: 10:434/450 of query aligns to 5:421/431 of Q9X0I0
- H141 (≠ W153) active site, Proton donor/acceptor
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
23% identity, 90% coverage: 10:412/450 of query aligns to 5:387/423 of 4eeiB
- active site: H67 (≠ Y62), S140 (≠ T152), H141 (≠ W153), K256 (= K282), E263 (≠ A289)
- binding adenosine monophosphate: K66 (≠ R61), H67 (≠ Y62), D68 (= D63), Q212 (= Q229), R289 (= R315), I291 (≠ L317), S294 (≠ W320), R298 (≠ W324)
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
25% identity, 76% coverage: 10:350/450 of query aligns to 5:324/419 of 5hw2A
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
27% identity, 97% coverage: 10:444/450 of query aligns to 21:463/484 of P30566
- M26 (= M15) to L: in ADSLD; severe; dbSNP:rs1311171245
- I72 (≠ Y62) to V: in ADSLD; severe
- P100 (= P94) to A: in ADSLD; moderate; dbSNP:rs119450942
- Y114 (≠ D108) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ T135) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (≠ W153) active site, Proton donor/acceptor
- R190 (= R184) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ L188) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ D231) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D253) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S276) active site, Proton donor/acceptor
- R303 (≠ V290) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ V298) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (≠ T304) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (= V350) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (≠ D360) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (vs. gap) to R: in ADSLD; severe
- R396 (= R381) to C: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs755492501; to H: in ADSLD; severe; abolishes cooperativity and reduces enzyme activity; dbSNP:rs763542069
- D422 (≠ V405) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (= L406) to V: in ADSLD; moderate
- R426 (≠ E409) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (≠ S413) to N: in ADSLD; mild; dbSNP:rs554254383
- S438 (≠ E419) to P: in ADSLD; severe; dbSNP:rs119450940
- S447 (≠ A428) to P: in ADSLD; severe; dbSNP:rs777821034
- T450 (≠ L431) to S: in ADSLD; moderate; dbSNP:rs372895468
- R452 (≠ Q433) to P: in ADSLD; severe
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine; A → V: in ADSLD; severe; dbSNP:rs143083947
- 3 A → V: in ADSLD; severe
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
26% identity, 97% coverage: 10:444/450 of query aligns to 14:456/477 of 5nx9D
- active site: H79 (≠ N76), T151 (= T152), H152 (≠ W153), S283 (= S277), K288 (= K282), E295 (≠ A289)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T152), H152 (≠ W153)
- binding adenosine monophosphate: Y14 (≠ F10), R78 (≠ G75), H79 (≠ N76), D80 (≠ S77), S105 (= S106), Q234 (= Q224), R296 (≠ V290), L324 (= L317), S327 (≠ W320), A328 (≠ H321), R331 (≠ W324)
- binding fumaric acid: H79 (≠ N76), S105 (= S106), Q234 (= Q224), S282 (= S276), S283 (= S277), K288 (= K282)
Sites not aligning to the query:
P24058 Argininosuccinate lyase; ASAL; Arginosuccinase; Delta crystallin II; Delta-2 crystallin; EC 4.3.2.1 from Anas platyrhynchos (Mallard) (Anas boschas) (see 4 papers)
29% identity, 58% coverage: 100:359/450 of query aligns to 109:366/468 of P24058
- N116 (≠ Q107) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D108) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T152) binding in chain C; mutation to A: Loss of activity.; mutation to D: Loss of activity.; mutation to S: 30% decrease in catalytic efficiency.; mutation to V: Loss of activity.
- H162 (≠ W153) mutation to E: Loss of activity.
- R238 (= R230) mutation to Q: Loss of activity.
- T281 (≠ G274) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S276) mutation to A: Loss of activity.; mutation to C: Loss of activity.; mutation to D: Loss of activity.; mutation to H: Loss of activity.; mutation to T: Loss of activity.
- N291 (= N284) binding in chain B; mutation to L: Loss of activity.
- D293 (≠ V286) mutation to N: 99% decrease in catalytic efficiency.
- E296 (≠ A289) mutation to D: Loss of activity.
- Y323 (≠ H313) binding in chain A
- K325 (≠ R315) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (≠ H321) binding in chain A
- D330 (≠ E323) mutation to N: Loss of activity.
- K331 (≠ W324) binding in chain A; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 11 W→A: 98% decrease in catalytic efficiency.; W→F: 90% decrease in catalytic efficiency.; W→M: 99% decrease in catalytic efficiency.; W→R: 97% decrease in catalytic efficiency.; W→Y: 50% decrease in catalytic efficiency.
- 29 binding in chain A; S→A: 10% decrease in catalytic efficiency.
- 33 D→N: 99% decrease in catalytic efficiency.
- 89 D→N: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
28% identity, 58% coverage: 100:359/450 of query aligns to 92:349/450 of 1k7wD
- active site: T144 (= T152), H145 (≠ W153), A266 (≠ S276), S267 (= S277), K272 (= K282), E279 (≠ A289)
- binding argininosuccinate: R98 (≠ S106), N99 (≠ Q107), V102 (≠ M110), T144 (= T152), H145 (≠ W153), Y306 (≠ H313), Q311 (≠ H321), K314 (≠ W324)
Sites not aligning to the query:
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
28% identity, 58% coverage: 100:359/450 of query aligns to 90:347/447 of 1hy0A
Sites not aligning to the query:
2ptqA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171n with bound amp and fumarate (see paper)
26% identity, 94% coverage: 14:434/450 of query aligns to 22:448/459 of 2ptqA
- active site: H91 (≠ S77), T170 (= T152), N171 (≠ W153), S296 (= S277), K301 (= K282), E308 (≠ A289)
- binding adenosine monophosphate: N90 (= N76), H91 (≠ S77), Q247 (= Q229), N309 (≠ V290), R335 (= R315), L337 (= L317), S340 (≠ W324), T341 (≠ E325), R344 (≠ P328)
- binding fumaric acid: H91 (≠ S77), T122 (= T105), S123 (= S106), Q247 (= Q229), S295 (= S276), S296 (= S277), M298 (= M279), K301 (= K282), N303 (= N284)
Sites not aligning to the query:
P0AB89 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Escherichia coli (strain K12) (see 2 papers)
25% identity, 94% coverage: 14:434/450 of query aligns to 22:448/456 of P0AB89
- NHD 90:92 (≠ NSA 76:78) binding ; binding
- H91 (≠ S77) binding
- K94 (≠ P80) modified: N6-acetyllysine
- TS 122:123 (= TS 105:106) binding ; binding
- H171 (≠ W153) mutation H->A,N: Reduces catalytic activity about 500-fold.
- Q247 (= Q229) binding ; binding ; binding
- S295 (= S276) mutation to A: Reduces catalytic activity about 1000-fold.
- S296 (= S277) binding ; binding
- KVN 301:303 (≠ KRN 282:284) binding ; binding
- N309 (≠ V290) binding ; binding
- R335 (= R315) binding ; binding
- STVLR 340:344 (≠ WETLP 324:328) binding ; binding
- K366 (vs. gap) modified: N6-acetyllysine
Sites not aligning to the query:
3gzhA Crystal structure of phosphate-bound adenylosuccinate lyase from e. Coli (see paper)
25% identity, 94% coverage: 14:434/450 of query aligns to 35:461/469 of 3gzhA
- active site: H104 (≠ S77), T183 (= T152), H184 (≠ W153), S309 (= S277), K314 (= K282), E321 (≠ A289)
- binding phosphate ion: H104 (≠ S77), T135 (= T105), S136 (= S106), S353 (≠ W324), T354 (≠ E325), R357 (≠ P328)
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
29% identity, 57% coverage: 103:359/450 of query aligns to 110:364/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
2ptrA Crystal structure of escherichia coli adenylosuccinate lyase mutant h171a with bound adenylosuccinate substrate (see paper)
28% identity, 61% coverage: 14:286/450 of query aligns to 22:305/454 of 2ptrA
- active site: H91 (≠ S77), T170 (= T152), A171 (≠ W153), K301 (= K282)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: H91 (≠ S77), D92 (≠ A78), T122 (= T105), S123 (= S106), Q247 (= Q229), S295 (= S276), S296 (= S277), M298 (= M279), K301 (= K282), N303 (= N284)
Sites not aligning to the query:
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
27% identity, 77% coverage: 99:445/450 of query aligns to 36:395/415 of 5nxaB
- active site: T89 (= T152), H90 (≠ W153), S221 (= S277), K226 (= K282), E233 (≠ A289)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ V286), R234 (≠ V290)
- binding fumaric acid: S220 (= S276), S221 (= S277), M223 (= M279), K226 (= K282), N228 (= N284)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: S43 (= S106), T89 (= T152), H90 (≠ W153), Q172 (= Q224), L262 (= L317), S265 (≠ W320), A266 (≠ H321), R269 (≠ W324)
Sites not aligning to the query:
Q05911 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 94% coverage: 10:434/450 of query aligns to 15:450/482 of Q05911
- K196 (≠ G193) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5nxaA Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
25% identity, 97% coverage: 10:444/450 of query aligns to 14:443/464 of 5nxaA
- active site: H79 (≠ N76), T151 (= T152), H152 (≠ W153), K275 (= K282), E282 (≠ A289)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: Y14 (≠ F10), R78 (≠ G75), H79 (≠ N76), D80 (≠ S77), T104 (= T105), S105 (= S106), Q234 (= Q224), K275 (= K282), R283 (≠ V290), L311 (= L317), S314 (≠ W320), A315 (≠ H321), R318 (≠ W324)
Sites not aligning to the query:
Query Sequence
>PP_1379 FitnessBrowser__Putida:PP_1379
MSNQLFDAYFTAPAMREIFSDRGRLQGMLDFEAALARAEASAGLVPHSAVAAIEAACQAE
RYDVGALANAIATAGNSAIPLVKALGKVIATGVPEAERYVHLGATSQDAMDTGLVLQLRD
ALDLIEADLGKLADTLSQQALKHADTPLVGRTWLQHATPVTLGMKLAGVLGALTRHRQRL
QELRPRLLVLQFGGASGSLAALGSKAMPVAEALAEQLKLTLPEQPWHTQRDRLVEFASVL
GLVAGSLGKFGRDISLLMQTEAGEVFEPSAPGKGGSSTMPHKRNPVGAAVLIGAATRVPG
LLSTLFAAMPQEHERSLGLWHAEWETLPDICCLVSGALRQAQVIAEGMEVDAARMRRNLD
LTQGLVLAEAVSIVLAQRLGRDRAHHLLEQCCQRAVAEQRHLRAVLGDEPQVSAELSGEE
LDRLLDPAHYLGQARVWVARAVSEHQRFTA
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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