SitesBLAST
Comparing Echvi_2531 FitnessBrowser__Cola:Echvi_2531 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)
P19414 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
60% identity, 98% coverage: 12:755/757 of query aligns to 41:778/778 of P19414
- R604 (= R581) mutation to K: Strongly diminishes the catalytic activity towards both known substrates, aconitate and homoaconitate.
Sites not aligning to the query:
- 1:16 modified: transit peptide, Mitochondrion
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
60% identity, 98% coverage: 12:755/757 of query aligns to 18:754/754 of 5acnA
- active site: D100 (= D95), H101 (= H96), D165 (= D160), R447 (= R448), S642 (= S643), R644 (= R645)
- binding fe3-s4 cluster: I145 (= I140), H147 (= H142), H167 (= H162), C358 (= C359), C421 (= C422), C424 (= C425), N446 (= N447)
- binding tricarballylic acid: K198 (= K193), G235 (= G230), R666 (= R667)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
60% identity, 98% coverage: 12:755/757 of query aligns to 45:781/781 of P16276
- Q99 (= Q67) binding substrate
- DSH 192:194 (= DSH 160:162) binding substrate
- C385 (= C359) binding [4Fe-4S] cluster
- C448 (= C422) binding [4Fe-4S] cluster
- C451 (= C425) binding [4Fe-4S] cluster
- R474 (= R448) binding substrate
- R479 (= R453) binding substrate
- R607 (= R581) binding substrate
- SR 670:671 (= SR 644:645) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
60% identity, 98% coverage: 12:754/757 of query aligns to 45:780/780 of P20004
- Q99 (= Q67) binding substrate
- DSH 192:194 (= DSH 160:162) binding substrate
- C385 (= C359) binding [4Fe-4S] cluster
- C448 (= C422) binding [4Fe-4S] cluster
- C451 (= C425) binding [4Fe-4S] cluster
- R474 (= R448) binding substrate
- R479 (= R453) binding substrate
- R607 (= R581) binding substrate
- SR 670:671 (= SR 644:645) binding substrate
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
60% identity, 98% coverage: 12:755/757 of query aligns to 17:753/753 of 1b0kA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), A641 (≠ S643), R643 (= R645)
- binding citrate anion: Q71 (= Q67), H100 (= H96), D164 (= D160), S165 (= S161), R446 (= R448), R451 (= R453), R579 (= R581), A641 (≠ S643), S642 (= S644), R643 (= R645)
- binding oxygen atom: D164 (= D160), H166 (= H162)
- binding iron/sulfur cluster: H100 (= H96), D164 (= D160), H166 (= H162), S356 (= S358), C357 (= C359), C420 (= C422), C423 (= C425)
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
60% identity, 98% coverage: 12:755/757 of query aligns to 17:753/753 of 8acnA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S643), R643 (= R645)
- binding nitroisocitric acid: Q71 (= Q67), T74 (= T70), H100 (= H96), D164 (= D160), S165 (= S161), R446 (= R448), R451 (= R453), R579 (= R581), S641 (= S643), S642 (= S644), R643 (= R645)
- binding iron/sulfur cluster: H100 (= H96), D164 (= D160), H166 (= H162), S356 (= S358), C357 (= C359), C420 (= C422), C423 (= C425), I424 (= I426)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
60% identity, 98% coverage: 12:755/757 of query aligns to 17:753/753 of 1fghA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S643), R643 (= R645)
- binding 4-hydroxy-aconitate ion: Q71 (= Q67), T74 (= T70), H100 (= H96), D164 (= D160), S165 (= S161), R446 (= R448), R451 (= R453), R579 (= R581), S641 (= S643), S642 (= S644), R643 (= R645)
- binding iron/sulfur cluster: H100 (= H96), D164 (= D160), H166 (= H162), S356 (= S358), C357 (= C359), C420 (= C422), C423 (= C425), I424 (= I426), R451 (= R453)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
60% identity, 98% coverage: 12:755/757 of query aligns to 17:753/753 of 1amjA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S643), R643 (= R645)
- binding iron/sulfur cluster: I144 (= I140), H166 (= H162), C357 (= C359), C420 (= C422), C423 (= C425)
- binding sulfate ion: Q71 (= Q67), R579 (= R581), R643 (= R645)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
60% identity, 98% coverage: 12:755/757 of query aligns to 17:753/753 of 1amiA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S643), R643 (= R645)
- binding alpha-methylisocitric acid: Q71 (= Q67), T74 (= T70), H100 (= H96), D164 (= D160), S165 (= S161), R446 (= R448), R451 (= R453), R579 (= R581), S641 (= S643), S642 (= S644), R643 (= R645)
- binding iron/sulfur cluster: H100 (= H96), I144 (= I140), D164 (= D160), H166 (= H162), S356 (= S358), C357 (= C359), C420 (= C422), C423 (= C425), N445 (= N447)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
60% identity, 98% coverage: 12:755/757 of query aligns to 17:753/753 of 1acoA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S643), R643 (= R645)
- binding iron/sulfur cluster: H100 (= H96), I144 (= I140), D164 (= D160), H166 (= H162), S356 (= S358), C357 (= C359), C420 (= C422), C423 (= C425), N445 (= N447)
- binding aconitate ion: Q71 (= Q67), D164 (= D160), S165 (= S161), R446 (= R448), R451 (= R453), R579 (= R581), S641 (= S643), S642 (= S644), R643 (= R645)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
60% identity, 98% coverage: 12:755/757 of query aligns to 17:753/753 of 1nisA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S643), R643 (= R645)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q67), H100 (= H96), D164 (= D160), S165 (= S161), R446 (= R448), R451 (= R453), R579 (= R581), S641 (= S643), S642 (= S644)
- binding iron/sulfur cluster: H100 (= H96), I144 (= I140), H166 (= H162), S356 (= S358), C357 (= C359), C420 (= C422), C423 (= C425)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
54% identity, 97% coverage: 12:749/757 of query aligns to 35:782/789 of P39533
- K610 (≠ R581) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
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)
28% identity, 92% coverage: 57:755/757 of query aligns to 76:889/889 of P21399
- C300 (≠ G255) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ R273) to M: in dbSNP:rs150373174
- C437 (= C359) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C422) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C425) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R448) mutation to Q: Strongly reduced RNA binding.
- R541 (= R453) mutation to Q: Strongly reduced RNA binding.
- R699 (vs. gap) mutation to K: No effect on RNA binding.
- S778 (= S643) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R645) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
28% identity, 92% coverage: 57:755/757 of query aligns to 75:888/888 of 2b3xA
- active site: D124 (= D95), H125 (= H96), D204 (= D160), R535 (= R448), S777 (= S643), R779 (= R645)
- binding iron/sulfur cluster: I175 (= I140), H206 (= H162), C436 (= C359), C502 (= C422), C505 (= C425), I506 (= I426), N534 (= N447)
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)
28% identity, 92% coverage: 57:755/757 of query aligns to 172:989/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
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)
28% identity, 93% coverage: 57:757/757 of query aligns to 86:909/909 of P09339
- C450 (= C359) 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 (vs. gap) 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
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
29% identity, 83% coverage: 57:683/757 of query aligns to 75:779/850 of 3snpA
- active site: D124 (= D95), H125 (= H96), D186 (= D160), R505 (= R448), S739 (= S643), R741 (= R645)
- binding : H125 (= H96), S126 (= S110), H188 (= H162), L243 (= L217), R250 (≠ T224), N279 (= N253), E283 (= E257), S352 (≠ N324), P357 (= P329), K360 (≠ A332), T419 (= T360), N420 (= N361), T421 (≠ S362), N504 (= N447), R505 (= R448), L520 (≠ V464), S642 (= S572), P643 (≠ M573), A644 (= A574), G645 (= G575), N646 (vs. gap), R649 (vs. gap), R665 (vs. gap), S669 (vs. gap), G671 (vs. gap), R674 (= R581), R741 (= R645)
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)
26% identity, 85% coverage: 42:683/757 of query aligns to 72:862/943 of A0QX20
- K394 (≠ E292) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
O14289 3-isopropylmalate dehydratase; Alpha-IPM isomerase; IPMI; Isopropylmalate isomerase; EC 4.2.1.33 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
25% identity, 86% coverage: 29:681/757 of query aligns to 3:655/758 of O14289
- S486 (vs. gap) modified: Phosphoserine
- S488 (vs. gap) modified: Phosphoserine
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
28% identity, 59% coverage: 30:479/757 of query aligns to 2:417/423 of 4kp1A
- active site: D64 (= D95), H65 (= H96), D121 (= D160), R387 (= R448)
- binding 2,4-dimethylpentane-2,4-diol: F299 (≠ L355), S302 (= S358), S383 (≠ H444), F389 (= F450)
- binding magnesium ion: C303 (= C359), T304 (= T360), R387 (= R448)
Query Sequence
>Echvi_2531 FitnessBrowser__Cola:Echvi_2531
MAFDIEMIKAVYAKYPERIAAARKTVGKPLTLAEKILYAHLWGGDATQAFERGKSYVDFA
PDRVAMQDATAQMALLQFMQAGKEKVAVPSTAHCDHLILAQKGAEEDLRSSLTASGEVFN
FLESVSNKYGIGFWKPGAGIIHQVVLENYAFPGGMMIGTDSHTVNAGGLGMVAIGVGGAD
AVDVMAGMPWELKFPKLIGVKLTGKMNGWTSAKDVILKVAGILTVKGGTGCIVEYFGEGA
KSLSATGKGTICNMGAEIGATTSTFGYDESMERYLRSTDRADVADLANEVKEHLTGDDEV
YANPEQYFDQVIEIDLSTLEPHINGPFTPDRATPVSQIRAEAEKNGWPTKVEWGLIGSCT
NSSYEDLSRASSIAQQAVDKQLKTKADFGINPGSEQVRFTAERDGMLKIFEDLDATIFTN
ACGPCIGQWARTGADKQEKNTIVHSFNRNFSKRADGNPNTHAFVTSPEMVAAIAISGDLG
FNPLTDTLTNANGEEVKLDPPKGEELPAKGFAVEDNGYQAPAEDGSGIEVKVNPDSKRLQ
LLTPFEPWDGKNITGAKLLIKAFGKCTTDHISMAGPWLRFRGHLDNISDNCLIGAVNAFN
EETNAVKSQLTGEYGPVPATQRAYKAAGIPTIVVGDHNYGEGSSREHAAMEPRHLGVKAV
LVKSFARIHETNLKKQGMLALTFDNEADYDKVQEDDTINFLDLDQFAPDKPLTLEFVHAD
GSKDVIVANHSYNDAQIKWFKAGSALNLIKEEQKKNA
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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