SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing AZOBR_RS01360 FitnessBrowser__azobra:AZOBR_RS01360 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 3 hits to proteins with known functional sites (download)

Q9XBQ8 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Clostridium subterminale (see paper)
41% identity, 95% coverage: 16:342/344 of query aligns to 40:365/416 of Q9XBQ8

query
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Q9XBQ8

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E86 (= E62) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
D96 (= D72) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
R130 (= R106) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
R134 (= R110) mutation to K: Complete loss of activity. Significant decrease in iron and sulfide and PLP content.; mutation to Q: Complete loss of activity. Slight decrease in iron and sulfide and PLP content.
R135 (= R111) mutation to K: Reduction in activity. Decrease in iron and sulfide and PLP content.; mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
R136 (≠ E112) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
D165 (≠ E141) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
D172 (= D148) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
E236 (= E213) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
D293 (= D270) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
D330 (= D307) mutation D->A,N: Complete loss of activity. Decrease in iron and sulfide and PLP content.

2a5hB 2.1 angstrom x-ray crystal structure of lysine-2,3-aminomutase from clostridium subterminale sb4, with michaelis analog (l-alpha-lysine external aldimine form of pyridoxal-5'-phosphate). (see paper)
41% identity, 95% coverage: 16:342/344 of query aligns to 38:363/410 of 2a5hB

query
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2a5hB

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active site: R110 (= R88), Y111 (= Y89), R114 (= R92), C123 (= C101), C127 (= C105), C130 (= C108), R132 (= R110), D291 (= D270), D328 (= D307), K335 (= K314)
binding lysine: L96 (≠ I74), L116 (= L94), R132 (= R110), L165 (≠ V143), S167 (≠ T145), Y288 (≠ H267), D291 (= D270), D328 (= D307)
binding pyridoxal-5'-phosphate: T108 (≠ V86), Y111 (= Y89), R114 (= R92), L116 (= L94), R196 (= R174), Y285 (= Y264), Y286 (= Y265), K335 (= K314)
binding s-adenosylmethionine: H129 (≠ F107), T131 (≠ F109), R132 (= R110), S167 (≠ T145), G169 (= G147), G198 (≠ H176), H228 (= H207), Q256 (= Q235), V258 (= V237), Y288 (≠ H267), C290 (≠ P269), D291 (= D270)
binding iron/sulfur cluster: C123 (= C101), C127 (= C105), C130 (= C108), G169 (= G147), R200 (= R178), H228 (= H207)

Sites not aligning to the query:

binding zinc ion: 373, 375, 378

O34676 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Bacillus subtilis (strain 168) (see paper)
36% identity, 99% coverage: 3:342/344 of query aligns to 36:374/471 of O34676

query
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O34676

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K290 (≠ R258) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
K346 (= K314) mutation to Q: No activity and no bound PLP.
K361 (≠ G329) mutation to Q: 95% loss of activity, normal PLP binding capacity.

Query Sequence

>AZOBR_RS01360 FitnessBrowser__azobra:AZOBR_RS01360
MKAAHSVTDLVAAGLMTPAAGEAVAAVADRYAIALTPYLLEALADAAPGDPLYAQYVPSP
EEAYTAPEEREDPIGDVVRSPVKGIVHRYPDRVLLKPLHACAVYCRFCFRREMVGPGGEA
LAPEELDAALAYVRARPEVWEVVVTGGDPLLLSPRRLSHIVRSLSDIPHVGVVRLHTRIP
VADPARVTPELVEALKAPDLATWMAIHVNHADELTEPARGAIARLADAGIPLLGQTVLLK
GINDDAAALEALFRGLVRNRIKPYYLHHPDLAAGTSHFRPTLAEGQALVKGLRGRVSGLC
QPTYVLDIPGGHGKAPAAPGWVRPDGEGGYLAEDFTGATHRYRG

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