SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011778117.1 NCBI__GCF_000015305.1:WP_011778117.1 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 4 hits to proteins with known functional sites (download)

P0A6X1 Glutamyl-tRNA reductase; GluTR; EC 1.2.1.70 from Escherichia coli (strain K12) (see 2 papers)
33% identity, 90% coverage: 1:412/456 of query aligns to 1:405/418 of P0A6X1

query
sites
P0A6X1

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G7 (= G7) mutation to D: Loss of activity.
T49 (= T49) mutation to V: 10% and 5% of wild-type reductase and esterase activity, respectively.
C50 (= C50) mutation to S: Loss of activity.
R52 (= R52) mutation to K: 5% and 4% of wild-type reductase and esterase activity, respectively.; mutation to Q: Loss of activity.
E54 (= E54) mutation to K: 6% and 2% of wild-type reductase and esterase activity, respectively.
C74 (≠ S74) mutation to S: No effect.
H99 (= H99) mutation to N: 5% and 4% of wild-type reductase and esterase activity, respectively.
G106 (= G106) mutation to N: Loss of activity.
S109 (= S109) mutation to A: 28% and 25% of wild-type reductase and esterase activity, respectively.
E114 (= E114) mutation to K: Loss of activity.
Q116 (= Q116) mutation to L: Loss of reductase activity. 30% of wild-type esterase activity.
S145 (≠ A145) mutation to F: Loss of activity.
C170 (≠ L170) mutation to S: No effect.
G191 (= G191) mutation to D: Loss of reductase activity. Retains esterase activity.
R314 (vs. gap) mutation to C: Loss of activity.

5yjlB Crystal structure of arabidopsis glutamyl-tRNA reductase in complex with NADPH and gbp (see paper)
30% identity, 93% coverage: 2:425/456 of query aligns to 2:413/415 of 5yjlB

query
sites
5yjlB

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active site: C50 (= C50), H99 (= H99)
binding nadp nicotinamide-adenine-dinucleotide phosphate: C50 (= C50), A162 (≠ G162), G187 (= G191), K188 (≠ S192), M189 (= M193), N209 (= N213), R210 (= R214), S211 (≠ T215), R214 (= R218), T249 (= T255), A250 (≠ G256), S251 (≠ A257), I280 (≠ L285), V282 (≠ M287)

Q9UXR8 Glutamyl-tRNA reductase; GluTR; EC 1.2.1.70 from Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) (see paper)
35% identity, 69% coverage: 3:316/456 of query aligns to 4:299/404 of Q9UXR8

query
sites
Q9UXR8

V

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C48 (= C50) mutation to S: Complete loss of activity.
H84 (= H99) mutation to A: Complete loss of activity.; mutation to N: 30% of wild-type reductase activity. 15% of wild-type esterase activity.

1gpjA Glutamyl-tRNA reductase from methanopyrus kandleri (see paper)
35% identity, 68% coverage: 7:316/456 of query aligns to 8:299/399 of 1gpjA

query
sites
1gpjA

G

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K

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E

V

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active site: S48 (≠ C50), H84 (= H99)
binding glutamic acid: T47 (= T49), N49 (= N51), R50 (= R52), S94 (= S109), E99 (= E114), E101 (≠ Q116), I102 (≠ V117), Q105 (= Q120)
binding (2r,3r,4s,5s)-4-amino-2-[6-(dimethylamino)-9h-purin-9-yl]-5-(hydroxymethyl)tetrahydro-3-furanol: S48 (≠ C50), E101 (≠ Q116)

Query Sequence

>WP_011778117.1 NCBI__GCF_000015305.1:WP_011778117.1
MSVLLFGVSHRSAPVSVLEQLSVDDSDQAKLIDQVLQSSLVTEAMVLSTCNRVEIYAVVE
AFHGGLSVIGQVLSEHSGMSLQDLTKHAYVRYAEAAVEHLFSVAGGLDSAVIGEQQVLGQ
VRRAYASAEANHTVGRTLHELSQRALAVGKRVHSETGIDAAGASVVSVALDTAEKKVGSL
AGRSAVLVGAGSMGALAAKQLMRAGVERIHVVNRTLPRAAKLAENVRSYGITAEAFPFDH
LPPLLTDADIVVTCTGAVRPVVSLADVHRGLAHVREPKELVICDLGMPRDVDPAVAGLPG
VFVVDMERILREPTARAAATDADAARTIVAAEVAKYLAGQRMAEVTPTVTALRQRAADVV
EAELLRLDNRLPGLDAAHRDEVANTVRRVVDKLLHAPTVRVKQLAGAPGGDSYAEALREL
FELDQHAVDAVAGTELGPLAGGDELGSLAIDLDMTE

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