SitesBLAST
Comparing WP_085640330.1 NCBI__GCF_002115805.1:WP_085640330.1 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 20 (the maximum) hits to proteins with known functional sites (download)
P83788 Kynureninase; L-kynurenine hydrolase; EC 3.7.1.3 from Pseudomonas fluorescens (see paper)
51% identity, 98% coverage: 8:397/397 of query aligns to 20:416/416 of P83788
- T97 (≠ L85) binding pyridoxal 5'-phosphate
- S98 (= S86) binding pyridoxal 5'-phosphate
- D132 (= D116) mutation to A: Reduces binding to pyridoxal phosphate and strongly reduces catalytic activity.; mutation to E: Enhances binding to pyridoxal phosphate.
- T172 (= T155) binding pyridoxal 5'-phosphate
- D201 (= D184) binding pyridoxal 5'-phosphate; mutation to E: Enhances binding to pyridoxal phosphate.
- H204 (= H187) binding pyridoxal 5'-phosphate
1qz9A The three dimensional structure of kynureninase from pseudomonas fluorescens (see paper)
52% identity, 95% coverage: 8:385/397 of query aligns to 19:403/404 of 1qz9A
- active site: F128 (= F113), D200 (= D184), Y225 (= Y209), K226 (= K210), R374 (= R356)
- binding pyridoxal-5'-phosphate: T95 (= T84), T96 (≠ L85), S97 (= S86), F128 (= F113), D131 (= D116), T171 (= T155), D200 (= D184), A202 (= A186), H203 (= H187), C223 (= C207), Y225 (= Y209), K226 (= K210)
P70712 Kynureninase; L-kynurenine hydrolase; EC 3.7.1.3 from Rattus norvegicus (Rat) (see paper)
29% identity, 91% coverage: 18:380/397 of query aligns to 69:458/464 of P70712
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
3e9kA Crystal structure of homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex (see paper)
28% identity, 92% coverage: 15:380/397 of query aligns to 61:444/446 of 3e9kA
- active site: F160 (= F113), D245 (= D184), Y270 (= Y209), K271 (= K210), R420 (= R356)
- binding 3-Hydroxyhippuric acid: S70 (= S24), F160 (= F113), H248 (= H187), K271 (= K210), R420 (= R356)
- binding pyridoxal-5'-phosphate: L132 (= L85), T133 (≠ S86), F160 (= F113), D163 (= D116), D245 (= D184), A247 (= A186), H248 (= H187), Y270 (= Y209), K271 (= K210)
Q16719 Kynureninase; L-kynurenine hydrolase; EC 3.7.1.3 from Homo sapiens (Human) (see 4 papers)
28% identity, 92% coverage: 15:380/397 of query aligns to 66:458/465 of Q16719
- T138 (≠ S86) binding pyridoxal 5'-phosphate
- T198 (≠ A144) to A: in HYXKY; reduced 3-hydroxykynureninase activity; dbSNP:rs606231307
- D250 (= D184) binding pyridoxal 5'-phosphate
- H253 (= H187) binding pyridoxal 5'-phosphate
- Y275 (= Y209) binding pyridoxal 5'-phosphate
- W305 (= W239) binding pyridoxal 5'-phosphate
- N333 (≠ T265) binding pyridoxal 5'-phosphate
- K412 (≠ Y334) to E: in dbSNP:rs9013
Sites not aligning to the query:
- 156:465 natural variant: Missing (in VCRL2; strongly reduced 3-hydroxykynureninase activity)
2hzpA Crystal structure of homo sapiens kynureninase (see paper)
28% identity, 92% coverage: 15:380/397 of query aligns to 61:445/447 of 2hzpA
- active site: F160 (= F113), D245 (= D184), Y270 (= Y209), K271 (= K210), R421 (= R356)
- binding pyridoxal-5'-phosphate: L132 (= L85), T133 (≠ S86), F160 (= F113), D163 (= D116), D245 (= D184), A247 (= A186), H248 (= H187), Y270 (= Y209), K271 (= K210)
3lvmB Crystal structure of e.Coli iscs (see paper)
25% identity, 83% coverage: 10:340/397 of query aligns to 6:323/394 of 3lvmB
- active site: H110 (≠ N112), D186 (= D184), T188 (≠ A186), Q189 (≠ H187), K212 (= K210)
- binding pyridoxal-5'-phosphate: G80 (vs. gap), A81 (vs. gap), T82 (vs. gap), H110 (≠ N112), D186 (= D184), T188 (≠ A186), Q189 (≠ H187), H211 (≠ Y209), K212 (= K210)
Sites not aligning to the query:
P0A6B7 Cysteine desulfurase IscS; NifS protein homolog; ThiI transpersulfidase; TusA transpersulfidase; EC 2.8.1.7 from Escherichia coli (strain K12) (see 4 papers)
25% identity, 81% coverage: 18:340/397 of query aligns to 5:317/404 of P0A6B7
- Q183 (≠ H187) binding pyridoxal 5'-phosphate
- SGH 203:205 (≠ CTY 207:209) binding pyridoxal 5'-phosphate
- K206 (= K210) modified: N6-(pyridoxal phosphate)lysine
- T243 (= T265) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 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)
25% identity, 81% coverage: 18:340/397 of query aligns to 5:317/404 of P0A6B9
- R39 (vs. gap) mutation to E: Decreased binding to CyaY.
- W45 (= W52) 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 (≠ G56) mutation to A: No binding to TusA. 24% mnm(5)s(2)U tRNA produced.
- D52 (= D59) mutation D->A,M,R,Y: No binding to TusA. 0-20% mnm(5)s(2)U tRNA produced.
- D65 (≠ E75) mutation to F: Decreased binding to TusA. 22% mnm(5)s(2)U tRNA produced.
- AT 75:76 (vs. gap) binding pyridoxal 5'-phosphate
- F89 (≠ L97) mutation to E: Decreased binding to ThiI.
- R112 (≠ I124) mutation to E: Decreased binding to IscX.
- R116 (≠ G128) mutation to E: Decreased binding to CyaY, IscX, ThiI.
- Q183 (≠ H187) binding pyridoxal 5'-phosphate
- SGH 203:205 (≠ CTY 207:209) binding pyridoxal 5'-phosphate
- K206 (= K210) modified: N6-(pyridoxal phosphate)lysine
- R220 (= R227) mutation to E: No binding to CyaY, IscX, ThiI.
- R223 (≠ D230) mutation to E: No binding CyaY, IscX, decreased binding to ThiI.
- RVR 223:225 (≠ DMA 230:232) mutation to EVE: No binding to IscX.
- RIE 225:227 (≠ ALP 232:234) mutation to EIR: No binding to CyaY, IscX.
- G234 (= G241) mutation to L: Decreased binding to CyaY, IscX.
- RG---------------M 237:239 (≠ SPFAFDLGYKAGVGISRM 244:261) mutation to EGE: No binding to CyaY, IscX, ThiI.
- T243 (= T265) binding pyridoxal 5'-phosphate
- E311 (≠ Y334) mutation to R: Decreased binding to ThiI.
Sites not aligning to the query:
- 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.
6o11A E. Coli cysteine desulfurase sufs c364a with a cys-aldimine intermediate (see paper)
25% identity, 64% coverage: 127:381/397 of query aligns to 146:403/406 of 6o11A
Sites not aligning to the query:
5db5A Crystal structure of plp-bound e. Coli sufs (cysteine persulfide intermediate) in space group p21
25% identity, 64% coverage: 127:381/397 of query aligns to 144:401/404 of 5db5A
- active site: D198 (= D184), A200 (= A186), Q201 (≠ H187), K224 (= K210), R357 (≠ A339), C362 (vs. gap)
- binding cysteine: R377 (= R356)
- binding pyridoxal-5'-phosphate: D198 (= D184), A200 (= A186), Q201 (≠ H187), S221 (≠ C207), H223 (≠ Y209), K224 (= K210), G275 (= G264), T276 (= T265)
Sites not aligning to the query:
6ndnA Crystal structure of selenocysteine lyase from escherichia coli
25% identity, 64% coverage: 127:381/397 of query aligns to 146:403/406 of 6ndnA
Sites not aligning to the query:
P77444 Cysteine desulfurase; Cysteine sulfinate desulfinase; CSD; Selenocysteine beta-lyase; SCL; Selenocysteine lyase; Selenocysteine reductase; EC 2.8.1.7; EC 3.13.1.-; EC 4.4.1.16 from Escherichia coli (strain K12) (see 2 papers)
25% identity, 64% coverage: 127:381/397 of query aligns to 146:403/406 of P77444
- C364 (vs. gap) mutation to A: Abolishes activity towards L-cysteine but not towards selenocysteine.
- R379 (= R356) mutation to A: Loss of function.
Sites not aligning to the query:
- 55 H→A: No effect.
- 123 H→A: Loss of function; possibly due to destabilization of PLP in the active site.
Q9Y697 Cysteine desulfurase; EC 2.8.1.7 from Homo sapiens (Human) (see 5 papers)
23% identity, 81% coverage: 18:340/397 of query aligns to 59:370/457 of Q9Y697
- R72 (≠ K30) to Q: in COXPD52; decreased protein expression in homozygous patient cells; dbSNP:rs200592030
- A127 (≠ D83) binding pyridoxal 5'-phosphate
- T128 (= T84) binding pyridoxal 5'-phosphate
- Q235 (≠ H187) binding pyridoxal 5'-phosphate
- S255 (≠ C207) binding pyridoxal 5'-phosphate
- H257 (≠ Y209) binding pyridoxal 5'-phosphate
- K258 (= K210) modified: N6-(pyridoxal phosphate)lysine
- T295 (= T265) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
6o13A E. Coli cysteine desulfurase sufs h123a with a cys-ketimine intermediate (see paper)
25% identity, 64% coverage: 127:381/397 of query aligns to 145:402/405 of 6o13A
Sites not aligning to the query:
1kmkA E. Coli nifs/csdb protein at 2.20a with the cysteine perselenide intermediate (residue csz). (see paper)
25% identity, 64% coverage: 127:381/397 of query aligns to 145:402/405 of 1kmkA
- active site: D199 (= D184), A201 (= A186), Q202 (≠ H187), K225 (= K210), R358 (≠ A339), C363 (vs. gap)
- binding pyridoxal-5'-phosphate: D199 (= D184), A201 (= A186), Q202 (≠ H187), S222 (≠ C207), H224 (≠ Y209), K225 (= K210)
- binding selenocysteine: N174 (≠ Y159), K225 (= K210), R358 (≠ A339), C363 (vs. gap), R378 (= R356)
Sites not aligning to the query:
1i29A Crystal structure of csdb complexed with l-propargylglycine (see paper)
25% identity, 64% coverage: 127:381/397 of query aligns to 145:402/405 of 1i29A
Sites not aligning to the query:
8tvtA Structure of human cysteine desulfurase nfs1 with l-propargylglycine bound to active site plp in complex with isd11, acp1 and iscu2
23% identity, 81% coverage: 18:340/397 of query aligns to 5:316/400 of 8tvtA
- binding L-Propargylglycine: Q10 (≠ N23), A11 (≠ S24), H102 (≠ N112), N153 (≠ Y159), H203 (≠ Y209), K204 (= K210)
- binding pyridoxal-5'-phosphate: G72 (= G82), A73 (≠ D83), T74 (= T84), H102 (≠ N112), D178 (= D184), Q181 (≠ H187), S201 (≠ C207), H203 (≠ Y209), K204 (= K210)
Sites not aligning to the query:
6nzuA Structure of the human frataxin-bound iron-sulfur cluster assembly complex (see paper)
23% identity, 81% coverage: 18:340/397 of query aligns to 4:315/402 of 6nzuA
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)
25% identity, 50% coverage: 52:250/397 of query aligns to 26:226/367 of P96060
- D168 (= D184) mutation to A: Loss of enzymatic activity.
- K194 (= K210) 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
>WP_085640330.1 NCBI__GCF_002115805.1:WP_085640330.1
MTDFTATRAAFHLPEGMIYLDGNSLGPLPKSAAARVAQTVASEWGDHLITGWNACGWMDM
PARLGDQIGRLIGAEAGHVVVGDTLSIKVFQALAAALKLNPHRRVILSDTGNFPSDLYMA
EGLISLLGPDYELRLVAPEEVGAAITDEIAVTLITEVDYRTGRKHDMAALTAKAHANGVV
TVWDLAHSAGAIPVDLAGAKADFAIGCTYKYLNGGPGAPAFIYVAPRHADMALPALSGWL
GHDSPFAFDLGYKAGVGISRMRVGTPPVLQMAALDAALDVWDDVDLNDLRTRSIDLSERF
IAGVEATCPDLTLASPRNAAERGSQVSFKFEEGYAAMQALIAHKVIGDFRAPDIMRFGFT
PLYLILEDVDQAVERLARIMRDRLWDTPEFKQRKAVT
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