SitesBLAST
Comparing WP_086508615.1 NCBI__GCF_002151265.1:WP_086508615.1 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)
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
39% identity, 93% coverage: 23:447/457 of query aligns to 40:464/476 of A0A0K2JL82
- N93 (= N76) mutation to A: Slight decrease in activity.
- D125 (= D105) mutation D->N,V: Almost loss of activity.
- R137 (≠ P117) binding
- R140 (≠ A120) binding
- R201 (≠ E181) binding
- H253 (= H236) mutation to A: Loss of activity.
- S302 (= S285) mutation to A: Loss of activity.
- K308 (= K291) binding ; mutation to A: Loss of activity.
- N310 (= N293) binding ; mutation to A: Loss of activity.
- R341 (= R324) mutation to A: Loss of activity.
5xnzA Crystal structure of cred complex with fumarate (see paper)
37% identity, 93% coverage: 23:447/457 of query aligns to 26:433/439 of 5xnzA
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
28% identity, 88% coverage: 43:442/457 of query aligns to 38:420/431 of P12047
- H89 (= H98) mutation to Q: Abolishes enzyme activity.
- H141 (≠ L150) mutation to Q: Abolishes enzyme activity.
- Q212 (= Q224) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N293) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R324) 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)
26% identity, 92% coverage: 20:440/457 of query aligns to 15:418/431 of Q9X0I0
- H141 (≠ L150) active site, Proton donor/acceptor
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
28% identity, 66% coverage: 78:380/457 of query aligns to 69:356/427 of 2x75A
Sites not aligning to the query:
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
28% identity, 86% coverage: 22:413/457 of query aligns to 17:380/419 of 5hw2A
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
28% identity, 83% coverage: 22:401/457 of query aligns to 17:367/423 of 4eeiB
- active site: H67 (≠ N76), S140 (≠ T149), H141 (≠ L150), K256 (= K291), E263 (≠ A298)
- binding adenosine monophosphate: K66 (≠ G75), H67 (≠ N76), D68 (≠ A77), Q212 (≠ P231), R289 (= R324), I291 (≠ L326), S294 (≠ W329), R298 (≠ W333)
5eytA Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex with amp (see paper)
27% identity, 69% coverage: 97:412/457 of query aligns to 98:410/472 of 5eytA
Sites not aligning to the query:
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
27% identity, 71% coverage: 36:359/457 of query aligns to 50:345/451 of 1tj7B
Q05911 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
24% identity, 81% coverage: 9:377/457 of query aligns to 10:385/482 of Q05911
- K196 (≠ P183) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
5nx9D Crystal structure of neanderthal adenylosuccinate lyase (adsl) in complex with its products amp and fumarate (see paper)
24% identity, 77% coverage: 98:449/457 of query aligns to 100:452/477 of 5nx9D
- active site: T151 (= T149), H152 (≠ L150), S283 (= S286), K288 (= K291), E295 (≠ A298)
- binding 2-[9-(3,4-dihydroxy-5-phosphonooxymethyl-tetrahydro-furan-2-yl)-9h-purin-6-ylamino]-succinic acid: T151 (= T149), H152 (≠ L150)
- binding adenosine monophosphate: S105 (= S103), Q234 (≠ W235), R296 (≠ L299), L324 (= L326), S327 (≠ W329), A328 (≠ H330), R331 (≠ W333)
- binding fumaric acid: S105 (= S103), Q234 (≠ W235), S282 (= S285), S283 (= S286), K288 (= K291)
Sites not aligning to the query:
P30566 Adenylosuccinate lyase; ADSL; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Homo sapiens (Human) (see 13 papers)
24% identity, 77% coverage: 98:449/457 of query aligns to 107:459/484 of P30566
- Y114 (≠ D105) to H: in ADSLD; severe; total loss of activity; dbSNP:rs374259530
- R141 (≠ A132) to W: in ADSLD; severe; dbSNP:rs756210458
- H159 (≠ L150) active site, Proton donor/acceptor
- R190 (≠ E181) to Q: in ADSLD; moderate; dbSNP:rs28941471
- R194 (≠ Q185) to C: in ADSLD; severe; reduces protein stability; dbSNP:rs1465152683
- K246 (≠ Q240) to E: in ADSLD; moderate; strongly reduced catalytic activity; dbSNP:rs119450944
- D268 (= D262) to N: in ADSLD; severe; total loss of activity; dbSNP:rs746501563
- S289 (= S285) active site, Proton donor/acceptor
- R303 (≠ L299) to C: in ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity; dbSNP:rs373458753
- L311 (≠ V307) to V: in ADSLD; severe; slightly reduced enzyme activity
- P318 (≠ V313) to L: in ADSLD; severe; dbSNP:rs202064195
- V364 (= V359) to M: in ADSLD; severe; dbSNP:rs370851726
- R374 (vs. gap) to W: in ADSLD; severe; dbSNP:rs376533026
- S395 (vs. gap) to R: in ADSLD; severe
- R396 (vs. gap) 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 (vs. gap) to Y: in ADSLD; moderate; dbSNP:rs119450943
- L423 (vs. gap) to V: in ADSLD; moderate
- R426 (= R405) to H: in ADSLD; severe; most frequent mutation; dbSNP:rs119450941
- D430 (≠ V409) to N: in ADSLD; mild; dbSNP:rs554254383
- S438 (≠ A417) to P: in ADSLD; severe; dbSNP:rs119450940
- S447 (≠ A437) to P: in ADSLD; severe; dbSNP:rs777821034
- T450 (≠ L440) to S: in ADSLD; moderate; dbSNP:rs372895468
- R452 (≠ S442) 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
- 26 M → L: in ADSLD; severe; dbSNP:rs1311171245
- 72 I → V: in ADSLD; severe
- 100 P → A: in ADSLD; moderate; dbSNP:rs119450942
5nxaB Crystal structure of neanderthal adenylosuccinate lyase (adsl)in complex with its products aicar and fumarate (see paper)
25% identity, 47% coverage: 236:449/457 of query aligns to 174:390/415 of 5nxaB
- active site: S221 (= S286), K226 (= K291), E233 (≠ A298)
- binding aminoimidazole 4-carboxamide ribonucleotide: M230 (≠ V295), R234 (≠ L299)
- binding fumaric acid: S220 (= S285), S221 (= S286), M223 (= M288), K226 (= K291), N228 (= N293)
- binding n-{[5-amino-1-(5-o-phosphono-beta-d-arabinofuranosyl)-1h-imidazol-4-yl]carbonyl}-l-aspartic acid: L262 (= L326), S265 (≠ W329), A266 (≠ H330), R269 (≠ W333)
Sites not aligning to the query:
1fupA Fumarase with bound pyromellitic acid (see paper)
28% identity, 61% coverage: 34:310/457 of query aligns to 50:339/455 of 1fupA
1fuqA Fumarase with bound 3-trimethylsilylsuccinic acid (see paper)
28% identity, 61% coverage: 34:310/457 of query aligns to 51:340/456 of 1fuqA
- active site: N104 (≠ A78), T184 (= T149), H185 (≠ L150), S315 (= S285), K321 (= K291), E328 (≠ A298)
- binding citric acid: T97 (≠ V71), S136 (≠ T102), S137 (= S103), N138 (≠ Q104)
- binding 3-trimethylsilylsuccinic acid: R123 (= R95), H126 (= H98), P127 (vs. gap), N128 (vs. gap), D129 (vs. gap)
1fuoA FumarasE C with bound citrate (see paper)
28% identity, 61% coverage: 34:310/457 of query aligns to 51:340/456 of 1fuoA
P05042 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Escherichia coli (strain K12) (see 4 papers)
28% identity, 61% coverage: 34:310/457 of query aligns to 54:343/467 of P05042
- R126 (= R95) binding ; mutation to A: 10-fold decrease of fumarase activity.
- K127 (≠ H96) mutation to D: No effect.
- H129 (= H98) mutation to N: No effect on fumarase activity and essentially same conformation compared to the wild-type, but appears to dramatically reduce binding of ligands at the B-site.
- HPND 129:132 (≠ H--- 98) binding in site B
- SSN 139:141 (≠ TSQ 102:104) binding
- H188 (≠ L150) active site, Proton donor/acceptor; mutation to N: 200-fold decrease of fumarase activity.
- E315 (= E280) mutation to Q: There is essentially no effect on the affinity values for both S-malate and fumarate. In contrast, the catalytic efficiency values have been lowered by 10-fold in both directions.
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
24% identity, 60% coverage: 96:369/457 of query aligns to 106:365/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
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)
24% identity, 67% coverage: 12:315/457 of query aligns to 28:313/468 of P24058
- S29 (≠ Q13) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (≠ S17) mutation to N: 99% decrease in catalytic efficiency.
- D89 (≠ A78) mutation to N: Loss of activity.
- N116 (≠ Q104) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D105) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T149) 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 (≠ L150) mutation to E: Loss of activity.
- R238 (= R225) mutation to Q: Loss of activity.
- T281 (≠ M282) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S285) 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 (= N293) binding in chain B; mutation to L: Loss of activity.
- D293 (≠ V295) mutation to N: 99% decrease in catalytic efficiency.
- E296 (≠ A298) mutation to D: 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.
- 323 binding in chain A
- 325 K→N: 99% decrease in catalytic efficiency.
- 328 binding in chain A
- 330 D→N: Loss of activity.
- 331 binding in chain A; K→Q: Loss of activity.
Query Sequence
>WP_086508615.1 NCBI__GCF_002151265.1:WP_086508615.1
MSDALLQHPFMSQTALSECSAEAMVAGMLAFELALAEVQEARGLLPEGVAAQMRKALEGH
AFDISSIGAGVASGGNAAIPFVKQARAALPAELRRHFHLGATSQDVIDSALMLLLKPRLA
ALDTLLRRCRSAALALMQAHETTVMVGRTLMQQALPITFGVKVAHWGIGLEQARCRLATL
ELPVQFGGAVAVHSGLDGPGLDGQGSDEADPGGLGLELMDALAQRLELSVPVLPWHTDRQ
PIHALATALDAVAGAAEKLALDVALLTQTEVGEVSEPGGEGMGESSSMPHKRNPVRCALI
RGAARQVHGHVSVILNAHAQPLERGLGEWHAEWTPLLDSALLVEGALEQAAVLLEGLEVH
PEAMRRNLAATGGGIMAEPVSRLLAPTLGQEAAKRISAEAAEAARLQGVAYSDALQAHPE
LQGQVEAQALRQATDPALYLGSSQAQVRRAAAWLQRE
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