SitesBLAST
Comparing H281DRAFT_04143 FitnessBrowser__Burk376:H281DRAFT_04143 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 15 hits to proteins with known functional sites (download)
P83788 Kynureninase; L-kynurenine hydrolase; EC 3.7.1.3 from Pseudomonas fluorescens (see paper)
68% identity, 100% coverage: 1:416/416 of query aligns to 1:416/416 of P83788
- T97 (≠ I97) binding pyridoxal 5'-phosphate
- S98 (= S98) binding pyridoxal 5'-phosphate
- D132 (= D132) mutation to A: Reduces binding to pyridoxal phosphate and strongly reduces catalytic activity.; mutation to E: Enhances binding to pyridoxal phosphate.
- T172 (= T172) binding pyridoxal 5'-phosphate
- D201 (= D201) binding pyridoxal 5'-phosphate; mutation to E: Enhances binding to pyridoxal phosphate.
- H204 (= H204) binding pyridoxal 5'-phosphate
1qz9A The three dimensional structure of kynureninase from pseudomonas fluorescens (see paper)
70% identity, 96% coverage: 4:404/416 of query aligns to 3:403/404 of 1qz9A
- active site: F128 (= F129), D200 (= D201), Y225 (= Y226), K226 (= K227), R374 (= R375)
- binding pyridoxal-5'-phosphate: T95 (= T96), T96 (≠ I97), S97 (= S98), F128 (= F129), D131 (= D132), T171 (= T172), D200 (= D201), A202 (= A203), H203 (= H204), C223 (= C224), Y225 (= Y226), K226 (= K227)
P70712 Kynureninase; L-kynurenine hydrolase; EC 3.7.1.3 from Rattus norvegicus (Rat) (see paper)
27% identity, 94% coverage: 7:399/416 of query aligns to 30:458/464 of P70712
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
2hzpA Crystal structure of homo sapiens kynureninase (see paper)
28% identity, 94% coverage: 7:399/416 of query aligns to 25:445/447 of 2hzpA
- active site: F160 (= F129), D245 (= D201), Y270 (= Y226), K271 (= K227), R421 (= R375)
- binding pyridoxal-5'-phosphate: L132 (≠ I97), T133 (≠ S98), F160 (= F129), D163 (= D132), D245 (= D201), A247 (= A203), H248 (= H204), Y270 (= Y226), K271 (= K227)
3e9kA Crystal structure of homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex (see paper)
28% identity, 94% coverage: 7:399/416 of query aligns to 25:444/446 of 3e9kA
- active site: F160 (= F129), D245 (= D201), Y270 (= Y226), K271 (= K227), R420 (= R375)
- binding 3-Hydroxyhippuric acid: S70 (= S36), F160 (= F129), H248 (= H204), K271 (= K227), R420 (= R375)
- binding pyridoxal-5'-phosphate: L132 (≠ I97), T133 (≠ S98), F160 (= F129), D163 (= D132), D245 (= D201), A247 (= A203), H248 (= H204), Y270 (= Y226), K271 (= K227)
Q16719 Kynureninase; L-kynurenine hydrolase; EC 3.7.1.3 from Homo sapiens (Human) (see 4 papers)
28% identity, 94% coverage: 7:399/416 of query aligns to 30:458/465 of Q16719
- T138 (≠ S98) binding pyridoxal 5'-phosphate
- T198 (≠ L149) to A: in HYXKY; reduced 3-hydroxykynureninase activity; dbSNP:rs606231307
- D250 (= D201) binding pyridoxal 5'-phosphate
- H253 (= H204) binding pyridoxal 5'-phosphate
- Y275 (= Y226) binding pyridoxal 5'-phosphate
- W305 (= W256) binding pyridoxal 5'-phosphate
- N333 (≠ T282) binding pyridoxal 5'-phosphate
- K412 (≠ G352) to E: in dbSNP:rs9013
Sites not aligning to the query:
- 156:465 natural variant: Missing (in VCRL2; strongly reduced 3-hydroxykynureninase activity)
P0A6B7 Cysteine desulfurase IscS; NifS protein homolog; ThiI transpersulfidase; TusA transpersulfidase; EC 2.8.1.7 from Escherichia coli (strain K12) (see 4 papers)
27% identity, 52% coverage: 30:244/416 of query aligns to 5:221/404 of P0A6B7
- Q183 (≠ H204) binding pyridoxal 5'-phosphate
- SGH 203:205 (≠ CTY 224:226) binding pyridoxal 5'-phosphate
- K206 (= K227) modified: N6-(pyridoxal phosphate)lysine
Sites not aligning to the query:
- 243 binding pyridoxal 5'-phosphate
- 328 active site, Cysteine persulfide intermediate; C→A: Loss of cysteine desulfurization.
- 376:404 mutation Missing: Normal cysteine desulfurase activity, decreased binding to IscU, decreased sulfur transfer to IscU, decreased Fe-S cluster assembly.
P0A6B9 Cysteine desulfurase IscS; EC 2.8.1.7 from Escherichia coli O157:H7 (see paper)
27% identity, 52% coverage: 30:244/416 of query aligns to 5:221/404 of P0A6B9
- R39 (= R62) mutation to E: Decreased binding to CyaY.
- W45 (= W64) mutation to R: No binding to TusA, decreased binding to ThiI. 3% 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U), 7% 4-thiouridine produced.
- E49 (≠ G68) mutation to A: No binding to TusA. 24% mnm(5)s(2)U tRNA produced.
- D52 (≠ A71) mutation D->A,M,R,Y: No binding to TusA. 0-20% mnm(5)s(2)U tRNA produced.
- D65 (≠ A87) mutation to F: Decreased binding to TusA. 22% mnm(5)s(2)U tRNA produced.
- AT 75:76 (≠ -T 96) binding pyridoxal 5'-phosphate
- F89 (≠ A114) mutation to E: Decreased binding to ThiI.
- R112 (≠ Q137) mutation to E: Decreased binding to IscX.
- R116 (= R145) mutation to E: Decreased binding to CyaY, IscX, ThiI.
- Q183 (≠ H204) binding pyridoxal 5'-phosphate
- SGH 203:205 (≠ CTY 224:226) binding pyridoxal 5'-phosphate
- K206 (= K227) modified: N6-(pyridoxal phosphate)lysine
- R220 (≠ Q243) mutation to E: No binding to CyaY, IscX, ThiI.
Sites not aligning to the query:
- 223 R→E: No binding CyaY, IscX, decreased binding to ThiI.
- 223:225 RVR→EVE: No binding to IscX.
- 225:227 RIE→EIR: No binding to CyaY, IscX.
- 234 G→L: Decreased binding to CyaY, IscX.
- 237:239 RGM→EGE: No binding to CyaY, IscX, ThiI.
- 243 binding pyridoxal 5'-phosphate
- 311 E→R: Decreased binding to ThiI.
- 327 A→V: No binding to IscX, decreased binding to CyaY, IscU, ThiI.
- 328 C→S: Retains binding to IscU, ThiI.
- 340 R→E: No binding to CyaY, ThiI, decreased binding to IscX, TusA.
3lvmB Crystal structure of e.Coli iscs (see paper)
27% identity, 52% coverage: 30:244/416 of query aligns to 11:227/394 of 3lvmB
- active site: H110 (≠ F129), D186 (= D201), T188 (≠ A203), Q189 (≠ H204), K212 (= K227)
- binding pyridoxal-5'-phosphate: G80 (vs. gap), A81 (vs. gap), T82 (= T96), H110 (≠ F129), D186 (= D201), T188 (≠ A203), Q189 (≠ H204), H211 (≠ Y226), K212 (= K227)
Sites not aligning to the query:
5b87A Crystal structure of a cysteine desulfurase from thermococcus onnurineus na1 in complex with alanine at 2.3 angstrom resolution (see paper)
23% identity, 80% coverage: 19:351/416 of query aligns to 6:336/397 of 5b87A
- active site: H113 (≠ F129), D189 (= D201), A191 (= A203), Q192 (≠ H204), K215 (= K227)
- binding alanine: A23 (≠ S36), N164 (≠ Y176), K215 (= K227)
- binding pyridoxal-5'-phosphate: N84 (≠ T96), T85 (≠ I97), S86 (= S98), H113 (≠ F129), N164 (≠ Y176), D189 (= D201), A191 (= A203), Q192 (≠ H204), S212 (≠ C224), H214 (≠ Y226), K215 (= K227)
Sites not aligning to the query:
5b7uA Apo structure of cysteine desulfurase from thermococcus onnurineus na1 at 1.89a (see paper)
23% identity, 80% coverage: 19:351/416 of query aligns to 12:342/402 of 5b7uA
Sites not aligning to the query:
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
28% identity, 31% coverage: 111:238/416 of query aligns to 86:216/377 of 1vjoA
Sites not aligning to the query:
1m32A Crystal structure of 2-aminoethylphosphonate transaminase (see paper)
24% identity, 38% coverage: 111:266/416 of query aligns to 69:220/361 of 1m32A
Sites not aligning to the query:
1m32B Crystal structure of 2-aminoethylphosphonate transaminase (see paper)
24% identity, 38% coverage: 111:266/416 of query aligns to 70:221/362 of 1m32B
Sites not aligning to the query:
P96060 2-aminoethylphosphonate--pyruvate transaminase; 2-aminoethylphosphonate aminotransferase; AEP transaminase; AEPT; EC 2.6.1.37 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
24% identity, 38% coverage: 111:266/416 of query aligns to 74:225/367 of P96060
- D168 (= D201) mutation to A: Loss of enzymatic activity.
- K194 (= K227) mutation K->L,R: Loss of enzymatic activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 340 mutation R->A,K: Decreased affinity for all of the substrates.
Query Sequence
>H281DRAFT_04143 FitnessBrowser__Burk376:H281DRAFT_04143
MKHREEALALDSADPLATLRDQFALSATTIYLDGNSLGVPPAAAAQRAQTVIAAEWGEGL
IRSWNAAGWFALPRRLGNKLAPLIGAAENEVVVTDTISINLFKLLSAALRLANARDPKRR
VIVSERSNFPTDLYIAQGLIEQLDRGYDLRLVDDPSELPEAIGEDTAIAMITHVNYRTGY
MHDMAALTRLIHDKGALALWDLAHSAGAVPVDLNGVGADYAVGCTYKYLNGGPGSPAFVW
VPQRHQNDFAQPLSGWWGHRAPFKMDPAYQPDDGIGRFLCGTQPMVSMALVECGLDVFLQ
TDMQAIRRKSLALTDLFIELVETRCSEFPLKLVTPRAHSQRGSHASFEHPHGYEVMQALI
ARGVIGDYREPHVLRFGFTPLYTRFVDVWDAVETLREVLVRETWRAPEFAARGAVT
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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