SitesBLAST
Comparing WP_012502633.1 NCBI__GCF_000020505.1:WP_012502633.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
57% identity, 95% coverage: 17:436/440 of query aligns to 11:416/416 of Q9XBQ8
- E86 (= E95) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
- D96 (= D105) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
- R130 (= R139) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
- R134 (= R143) 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 (≠ K144) 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 (= R145) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- D165 (= D174) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D172 (= D181) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
- E236 (= E245) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D293 (= D302) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
- D330 (= D339) 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)
57% identity, 95% coverage: 17:432/440 of query aligns to 9:410/410 of 2a5hB
- active site: R110 (= R121), Y111 (= Y122), R114 (= R125), C123 (= C134), C127 (= C138), C130 (= C141), R132 (= R143), D291 (= D302), D328 (= D339), K335 (= K346)
- binding lysine: L96 (= L107), L116 (= L127), R132 (= R143), L165 (= L176), S167 (= S178), Y288 (= Y299), D291 (= D302), D328 (= D339)
- binding pyridoxal-5'-phosphate: T108 (= T119), Y111 (= Y122), R114 (= R125), L116 (= L127), R196 (= R207), Y285 (= Y296), Y286 (= Y297), K335 (= K346)
- binding s-adenosylmethionine: H129 (= H140), T131 (= T142), R132 (= R143), S167 (= S178), G169 (= G180), G198 (= G209), H228 (= H239), Q256 (= Q267), V258 (= V269), Y288 (= Y299), C290 (= C301), D291 (= D302)
- binding iron/sulfur cluster: C123 (= C134), C127 (= C138), C130 (= C141), G169 (= G180), R200 (= R211), H228 (= H239)
- binding zinc ion: C373 (≠ F384), C375 (= C389), C378 (= C392)
O34676 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Bacillus subtilis (strain 168) (see paper)
51% identity, 94% coverage: 23:435/440 of query aligns to 26:429/471 of O34676
- K290 (≠ A290) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
- K346 (= K346) mutation to Q: No activity and no bound PLP.
- K361 (= K361) mutation to Q: 95% loss of activity, normal PLP binding capacity.
Query Sequence
>WP_012502633.1 NCBI__GCF_000020505.1:WP_012502633.1
MTLSLAQKQIIKRIDPETTPSDWSDWRWQMRHSIRDLDTFERLLDITLSDEQRKAFGETV
QKFPMSTTPYYLSLINTDDMENDPVFLQSVPSPLELKIMKGDMADPLHEDEDSPAPCVTH
RYPDRVLLLVSNTCPMYCRHCTRKRKVGDEDTIPNRAAIQAGIDYIRNTPQVRDVLLSGG
DPFLLSDEMLDWILTELRAIEHVEIIRVGTRTPVVLPQRITPELVAILGKHQPVWVNTHF
NHPREMTQSARNALARLADVGVPLGNQTVLLSGINDCPRIMKALVHKLVANRVRPYYLYQ
CDLSEGLSHFRTPVGKGIEILESLIGHTSGFCVPTYVIDAPGGGGKIPVMPNYLISWSTN
KVVLRNYEGVITTYKEPDSYEPTFCDRNCTECDLQLNFEDAEQSKAIGVQQLLADHDQTI
SLIPSSNARHKRRKGEAEEA
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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