SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_109941996.1 NCBI__GCF_003173335.1:WP_109941996.1 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)
58% identity, 87% coverage: 18:396/437 of query aligns to 13:389/416 of Q9XBQ8

query
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Q9XBQ8

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E86 (= E94) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
D96 (= D104) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
R130 (= R138) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
R134 (= R142) 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 (≠ K143) 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 (= R144) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
D165 (= D173) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
D172 (= D180) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
E236 (= E244) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
D293 (= D301) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
D330 (= D338) 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)
58% identity, 87% coverage: 18:396/437 of query aligns to 11:387/410 of 2a5hB

query
sites
2a5hB

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active site: R110 (= R120), Y111 (= Y121), R114 (= R124), C123 (= C133), C127 (= C137), C130 (= C140), R132 (= R142), D291 (= D301), D328 (= D338), K335 (= K345)
binding lysine: L96 (= L106), L116 (= L126), R132 (= R142), L165 (= L175), S167 (= S177), Y288 (≠ F298), D291 (= D301), D328 (= D338)
binding pyridoxal-5'-phosphate: T108 (= T118), Y111 (= Y121), R114 (= R124), L116 (= L126), R196 (= R206), Y285 (= Y295), Y286 (= Y296), K335 (= K345)
binding s-adenosylmethionine: H129 (= H139), T131 (= T141), R132 (= R142), S167 (= S177), G169 (= G179), G198 (= G208), H228 (= H238), Q256 (= Q266), V258 (= V268), Y288 (≠ F298), C290 (= C300), D291 (= D301)
binding iron/sulfur cluster: C123 (= C133), C127 (= C137), C130 (= C140), G169 (= G179), R200 (= R210), H228 (= H238)
binding zinc ion: C373 (≠ I382), C375 (= C384), C378 (≠ N387)

O34676 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Bacillus subtilis (strain 168) (see paper)
53% identity, 95% coverage: 21:434/437 of query aligns to 25:428/471 of O34676

query
sites
O34676

K

K

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D

Y

K

E

E

N

V

S

S

I

F

T

T

I

-

L

-

P

P

A

E

V

N

L

V

N

D

R

R

I

I

A

K

R

R

R

R

Q

E

K290 (= K289) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
K346 (= K345) mutation to Q: No activity and no bound PLP.
K361 (= K360) mutation to Q: 95% loss of activity, normal PLP binding capacity.

Query Sequence

>WP_109941996.1 NCBI__GCF_003173335.1:WP_109941996.1
MTNVETIPASGPEPVQQNNAKWKDWKWQVGHSITDITTLEQTLGMNLSKSEREDMIKTCD
IFPMSITPYYLSLINTDDPLHDPIFRQAVPSPGELIIENYDLHDPLSEDADSPCPLITHR
YPDRVLFLISNTCAMYCRHCTRKRKVGQVLSAPLKEELDEAFSYIETHSEIRDVLLSGGD
PLMLSDKELDTILRRLRKIPHVEIIRIGSRVPVVLPFRITDNLVSILKKYHPLWLNTHFN
HPHEFTTESCEALAKLADAGIPLGNQSVLLAGVNDCPEIMRKLVHELVKNRVRPYYLFQC
DLAEGLAHFRTPVGKGIEIIESLIGHTSGLAVPTYVIDAPGGGGKIPVMPYYLVSWSSNK
VVLRNYEGMFTTYQEPDNYQGITCDLNCEKCRLQHIEDQETMVKRAQGIEALLSDYENSI
TILPAVLNRIARRQDGE

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