SitesBLAST
Comparing Pf1N1B4_3821 2-methylcitrate dehydratase FeS dependent (EC 4.2.1.79) to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P09339 Aconitate hydratase A; ACN; Aconitase; Aconitate/2-methylaconitate hydratase; Iron-responsive protein-like; IRP-like; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.- from Bacillus subtilis (strain 168) (see 2 papers)
42% identity, 98% coverage: 11:860/864 of query aligns to 23:909/909 of P09339
- C450 (= C406) mutation to S: Loss of aconitase activity. It is glutamate auxotroph and accumulates citrate. Exhibits overexpression of the citB promoter and accumulates high levels of inactive aconitase.
- R741 (≠ K690) mutation to E: Same aconitase activity compared to the wild-type. It is glutamate prototroph and accumulates citrate. Exhibits overexpression of the citB promoter and accumulates high levels of active aconitase.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P21399 Cytoplasmic aconitate hydratase; Aconitase; Citrate hydro-lyase; Ferritin repressor protein; Iron regulatory protein 1; IRP1; Iron-responsive element-binding protein 1; IRE-BP 1; EC 4.2.1.3 from Homo sapiens (Human) (see 2 papers)
42% identity, 95% coverage: 31:850/864 of query aligns to 32:881/889 of P21399
- C300 (≠ A295) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ D313) to M: in dbSNP:rs150373174
- C437 (= C406) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C472) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C475) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R505) mutation to Q: Strongly reduced RNA binding.
- R541 (= R510) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ M661) mutation to K: No effect on RNA binding.
- S778 (= S745) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R747) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
42% identity, 95% coverage: 31:850/864 of query aligns to 31:880/888 of 2b3xA
- active site: D124 (= D119), H125 (= H120), D204 (= D200), R535 (= R505), S777 (= S745), R779 (= R747)
- binding iron/sulfur cluster: H125 (= H120), I175 (= I171), H177 (= H173), D204 (= D200), H206 (= H202), S435 (= S405), C436 (= C406), C502 (= C472), C505 (= C475), I506 (≠ N476), N534 (= N504)
Q9SIB9 Aconitate hydratase 3, mitochondrial; Aconitase 3; mACO1; Citrate hydro-lyase 3; EC 4.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
43% identity, 95% coverage: 32:849/864 of query aligns to 129:980/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
41% identity, 95% coverage: 31:850/864 of query aligns to 31:842/850 of 3snpA
- active site: D124 (= D119), H125 (= H120), D186 (= D200), R505 (= R505), S739 (= S745), R741 (= R747)
- binding : H125 (= H120), S126 (= S121), H188 (= H202), L243 (= L257), R250 (= R264), N279 (= N293), M280 (= M294), E283 (= E297), C351 (≠ M362), S352 (≠ A363), P357 (= P368), K360 (≠ R371), T419 (= T407), N420 (= N408), T421 (= T409), N504 (= N504), R505 (= R505), L520 (= L520), A521 (= A521), S642 (= S643), P643 (= P644), A644 (≠ S645), G645 (≠ N646), N646 (≠ A647), I647 (= I648), A648 (≠ M649), R649 (≠ L650), P664 (≠ E665), R665 (≠ E666), S669 (= S670), Y670 (= Y671), G671 (≠ A672), R674 (= R675), M680 (≠ A681), R689 (≠ K690), S739 (= S745), R741 (= R747), D742 (= D748)
A0QX20 Aconitate hydratase A; ACN; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; Iron-responsive protein-like; IRP-like; Probable 2-methyl-cis-aconitate hydratase; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
44% identity, 54% coverage: 396:860/864 of query aligns to 468:942/943 of A0QX20