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Comparing BWI76_RS11940 BWI76_RS11940 aconitate hydratase 1 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)
56% identity, 100% coverage: 1:890/890 of query aligns to 1:906/909 of P09339
- M1 (= M1) modified: Initiator methionine, Removed
- C450 (= C435) 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 (= R725) 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.
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)
57% identity, 100% coverage: 2:890/890 of query aligns to 9:939/943 of A0QX20
- K394 (≠ A395) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
55% identity, 98% coverage: 22:889/890 of query aligns to 117:987/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
53% identity, 96% coverage: 37:889/890 of query aligns to 33:886/888 of 2b3xA
- active site: D124 (= D128), H125 (= H129), D204 (= D212), R535 (= R534), S777 (= S776), R779 (= R778)
- binding iron/sulfur cluster: I175 (= I179), H206 (= H214), C436 (= C435), C502 (= C501), C505 (= C504), I506 (= I505), N534 (= N533)
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)
53% identity, 96% coverage: 37:889/890 of query aligns to 34:887/889 of P21399
- C300 (≠ S307) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ D325) to M: in dbSNP:rs150373174
- C437 (= C435) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C501) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C504) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R534) mutation to Q: Strongly reduced RNA binding.
- R541 (= R539) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ H696) mutation to K: No effect on RNA binding.
- S778 (= S776) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R778) mutation to Q: Nearly abolishes RNA binding.
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
52% identity, 96% coverage: 37:889/890 of query aligns to 33:848/850 of 3snpA
- active site: D124 (= D128), H125 (= H129), D186 (= D212), R505 (= R534), S739 (= S776), R741 (= R778)
- binding : H125 (= H129), S126 (= S130), H188 (= H214), L243 (= L269), R250 (= R276), N279 (= N305), E283 (= E309), S352 (≠ A375), P357 (= P380), K360 (≠ R383), T419 (= T436), N420 (= N437), T421 (= T438), N504 (= N533), R505 (= R534), L520 (= L549), S642 (= S678), P643 (= P679), A644 (= A680), G645 (= G681), N646 (≠ S682), R649 (≠ A685), R665 (≠ I701), S669 (= S705), G671 (= G707), R674 (= R710), R741 (= R778)
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)
28% identity, 89% coverage: 66:857/890 of query aligns to 66:745/778 of P19414
- R604 (≠ H696) 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)
28% identity, 88% coverage: 82:861/890 of query aligns to 65:725/754 of 5acnA
- active site: D100 (= D128), H101 (= H129), D165 (= D212), R447 (= R534), S642 (= S776), R644 (= R778)
- binding fe3-s4 cluster: I145 (= I179), H147 (= H181), H167 (= H214), C358 (= C435), C421 (= C501), C424 (= C504), N446 (= N533)
- binding tricarballylic acid: K198 (≠ L245), G235 (= G282), R666 (= R800)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 88% coverage: 82:861/890 of query aligns to 92:752/781 of P16276
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 88% coverage: 30:816/890 of query aligns to 46:711/789 of P39533
- K610 (≠ H696) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
28% identity, 88% coverage: 82:861/890 of query aligns to 64:724/753 of 1b0kA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R534), A641 (≠ S776), R643 (= R778)
- binding citrate anion: Q71 (= Q89), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R534), R451 (= R539), R579 (≠ H696), A641 (≠ S776), S642 (= S777), R643 (= R778)
- binding oxygen atom: D164 (= D212), H166 (= H214)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D212), H166 (= H214), S356 (= S434), C357 (= C435), C420 (= C501), C423 (= C504)
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
28% identity, 88% coverage: 82:861/890 of query aligns to 64:724/753 of 8acnA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R534), S641 (= S776), R643 (= R778)
- binding nitroisocitric acid: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R534), R451 (= R539), R579 (≠ H696), S641 (= S776), S642 (= S777), R643 (= R778)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D212), H166 (= H214), S356 (= S434), C357 (= C435), C420 (= C501), C423 (= C504), I424 (= I505)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 88% coverage: 82:861/890 of query aligns to 64:724/753 of 1fghA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R534), S641 (= S776), R643 (= R778)
- binding 4-hydroxy-aconitate ion: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R534), R451 (= R539), R579 (≠ H696), S641 (= S776), S642 (= S777), R643 (= R778)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D212), H166 (= H214), S356 (= S434), C357 (= C435), C420 (= C501), C423 (= C504), I424 (= I505), R451 (= R539)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 88% coverage: 82:861/890 of query aligns to 64:724/753 of 1amjA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R534), S641 (= S776), R643 (= R778)
- binding iron/sulfur cluster: I144 (= I179), H166 (= H214), C357 (= C435), C420 (= C501), C423 (= C504)
- binding sulfate ion: Q71 (= Q89), R579 (≠ H696), R643 (= R778)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 88% coverage: 82:861/890 of query aligns to 64:724/753 of 1amiA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R534), S641 (= S776), R643 (= R778)
- binding alpha-methylisocitric acid: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R534), R451 (= R539), R579 (≠ H696), S641 (= S776), S642 (= S777), R643 (= R778)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), D164 (= D212), H166 (= H214), S356 (= S434), C357 (= C435), C420 (= C501), C423 (= C504), N445 (= N533)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 88% coverage: 82:861/890 of query aligns to 64:724/753 of 1acoA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R534), S641 (= S776), R643 (= R778)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), D164 (= D212), H166 (= H214), S356 (= S434), C357 (= C435), C420 (= C501), C423 (= C504), N445 (= N533)
- binding aconitate ion: Q71 (= Q89), D164 (= D212), S165 (= S213), R446 (= R534), R451 (= R539), R579 (≠ H696), S641 (= S776), S642 (= S777), R643 (= R778)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 88% coverage: 82:861/890 of query aligns to 64:724/753 of 1nisA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R534), S641 (= S776), R643 (= R778)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q89), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R534), R451 (= R539), R579 (≠ H696), S641 (= S776), S642 (= S777)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), H166 (= H214), S356 (= S434), C357 (= C435), C420 (= C501), C423 (= C504)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 88% coverage: 82:861/890 of query aligns to 92:752/780 of P20004
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)
26% identity, 43% coverage: 207:586/890 of query aligns to 135:492/758 of O14289
- S486 (≠ Q580) modified: Phosphoserine
- S488 (≠ V582) modified: Phosphoserine
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
23% identity, 48% coverage: 142:564/890 of query aligns to 63:417/423 of 4kp1A
- active site: D64 (≠ E143), H65 (≠ E144), D121 (= D212), R387 (= R534)
- binding 2,4-dimethylpentane-2,4-diol: F299 (≠ L415), S302 (= S434), S383 (≠ G527), F389 (= F536)
- binding magnesium ion: C303 (= C435), T304 (= T436), R387 (= R534)
Query Sequence
>BWI76_RS11940 BWI76_RS11940 aconitate hydratase 1
MSSTLRAASKDTLQVKDKTWHYYSLPLAAKQLGDLSRLPKSLKVLLENLLRWQDGDSVTA
EDIHALAGWLKHAHADREIAYRPARVLMQDFTGVPAVVDLAAMREAVKRLGGDTAKVNPL
SPVDLVIDHSVTVDRFGDDDAFEENVRLEMERNHERYVFLRWGQQAFSRFSVVPPGTGIC
HQVNLEYLGRAVWSEQQNGEWVAFPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQ
PVSMLIPDVVGFKLSGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADR
ATIANMSPEYGATCGFFPIDAVTLDYMRLTGRSEEQVALVEAYAKAQGMWRQPGDEPVFT
STLALDMGTVEASLAGPKRPQDRVALGDVPQAFAASSELEVNHAQKDKRPIDYTLNGQQY
SLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVERGLKPQPWVKASLAPGSKVVSDYL
AHAKLTPWLDELGFNLVGYGCTTCIGNSGPLPDPIERAIKQGDLTVGAVLSGNRNFEGRI
HPLVKTNWLASPPLVVAYALAGNMNLDLTREPLGTGKDGQPVYLKDIWPSGIEVAQAVEQ
VSTEMFRKEYAEVFEGTAEWKAIKVDRSDTYDWQNDSTYIRLSPFFDEMGVEPKPVEDIH
GARILAMLGDSVTTDHISPAGSIKADSPAGRYLQNHGVERIDFNSYGSRRGNHEVMMRGT
FANIRIRNEMVPGVEGGMTRHLPDTQPIAIYDAAMLYKEEGTPLAVIAGKEYGSGSSRDW
AAKGPRLLGVRVVIAESFERIHRSNLIGMGILPLEFPQGMTRKTLGLNGEERIDISNLQA
LQPGMTVPVTLTRADGRQEVIDCRCRIDTATELTYYQNDGILHYVIRNML
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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