SitesBLAST
Comparing 351600 FitnessBrowser__Btheta:351600 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)
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)
57% identity, 98% coverage: 15:745/747 of query aligns to 41:770/778 of P19414
- R604 (= R579) 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
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
58% identity, 98% coverage: 12:745/747 of query aligns to 45:773/780 of P20004
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
57% identity, 98% coverage: 12:745/747 of query aligns to 17:745/753 of 8acnA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S641), R643 (= R643)
- binding nitroisocitric acid: Q71 (= Q67), T74 (= T70), H100 (= H96), D164 (= D160), S165 (= S161), R446 (= R448), R451 (= R453), R579 (= R579), S641 (= S641), S642 (= S642), R643 (= R643)
- 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)
57% identity, 98% coverage: 12:745/747 of query aligns to 17:745/753 of 1fghA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S641), R643 (= R643)
- binding 4-hydroxy-aconitate ion: Q71 (= Q67), T74 (= T70), H100 (= H96), D164 (= D160), S165 (= S161), R446 (= R448), R451 (= R453), R579 (= R579), S641 (= S641), S642 (= S642), R643 (= R643)
- 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)
57% identity, 98% coverage: 12:745/747 of query aligns to 17:745/753 of 1amjA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S641), R643 (= R643)
- binding iron/sulfur cluster: I144 (= I140), H166 (= H162), C357 (= C359), C420 (= C422), C423 (= C425)
- binding sulfate ion: Q71 (= Q67), R579 (= R579), R643 (= R643)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
57% identity, 98% coverage: 12:745/747 of query aligns to 17:745/753 of 1amiA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S641), R643 (= R643)
- binding alpha-methylisocitric acid: Q71 (= Q67), T74 (= T70), H100 (= H96), D164 (= D160), S165 (= S161), R446 (= R448), R451 (= R453), R579 (= R579), S641 (= S641), S642 (= S642), R643 (= R643)
- 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)
57% identity, 98% coverage: 12:745/747 of query aligns to 17:745/753 of 1acoA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S641), R643 (= R643)
- 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 (= R579), S641 (= S641), S642 (= S642), R643 (= R643)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
57% identity, 98% coverage: 12:745/747 of query aligns to 17:745/753 of 1nisA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), S641 (= S641), R643 (= R643)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q67), H100 (= H96), D164 (= D160), S165 (= S161), R446 (= R448), R451 (= R453), R579 (= R579), S641 (= S641), S642 (= S642)
- binding iron/sulfur cluster: H100 (= H96), I144 (= I140), H166 (= H162), S356 (= S358), C357 (= C359), C420 (= C422), C423 (= C425)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
57% identity, 98% coverage: 12:745/747 of query aligns to 45:773/781 of P16276
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
57% identity, 98% coverage: 12:745/747 of query aligns to 18:746/754 of 5acnA
- active site: D100 (= D95), H101 (= H96), D165 (= D160), R447 (= R448), S642 (= S641), R644 (= R643)
- binding fe3-s4 cluster: I145 (= I140), H147 (= H142), H167 (= H162), C358 (= C359), C421 (= C422), C424 (= C425), N446 (= N447)
- binding tricarballylic acid: K198 (= K193), G235 (≠ N230), R666 (= R665)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
57% identity, 98% coverage: 12:745/747 of query aligns to 17:745/753 of 1b0kA
- active site: D99 (= D95), H100 (= H96), D164 (= D160), R446 (= R448), A641 (≠ S641), R643 (= R643)
- binding citrate anion: Q71 (= Q67), H100 (= H96), D164 (= D160), S165 (= S161), R446 (= R448), R451 (= R453), R579 (= R579), A641 (≠ S641), S642 (= S642), R643 (= R643)
- 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)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
54% identity, 96% coverage: 29:745/747 of query aligns to 53:780/789 of P39533
- K610 (≠ R579) 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: 57:745/747 of query aligns to 76:881/889 of P21399
- C300 (≠ G255) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (= T273) 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 (= S641) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R643) 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: 57:745/747 of query aligns to 75:880/888 of 2b3xA
- active site: D124 (= D95), H125 (= H96), D204 (= D160), R535 (= R448), S777 (= S641), R779 (= R643)
- binding iron/sulfur cluster: I175 (= I140), H206 (= H162), C436 (= C359), C502 (= C422), C505 (= C425), I506 (= I426), N534 (= N447)
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)
27% identity, 92% coverage: 57:744/747 of query aligns to 86:898/909 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 (≠ W605) 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
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: 57:744/747 of query aligns to 172:980/990 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)
27% identity, 92% coverage: 57:745/747 of query aligns to 75:842/850 of 3snpA
- active site: D124 (= D95), H125 (= H96), D186 (= D160), R505 (= R448), S739 (= S641), R741 (= R643)
- binding : H125 (= H96), S126 (≠ T110), 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 (= S570), P643 (≠ M571), A644 (= A572), G645 (= G573), N646 (vs. gap), R649 (vs. gap), R665 (vs. gap), S669 (vs. gap), G671 (vs. gap), R674 (vs. gap), R741 (= R643)
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)
25% identity, 90% coverage: 57:726/747 of query aligns to 82:912/943 of A0QX20
- K394 (≠ A296) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
26% identity, 60% coverage: 30:479/747 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 (≠ T444), F389 (= F450)
- binding magnesium ion: C303 (= C359), T304 (= T360), R387 (= R448)
4nqyA The reduced form of mj0499 (see paper)
27% identity, 48% coverage: 121:479/747 of query aligns to 71:404/409 of 4nqyA
Sites not aligning to the query:
Query Sequence
>351600 FitnessBrowser__Btheta:351600
MVYDLTMLEAFYSAYKGKVEHVRAVLKRPLTLAEKILYAHLFNEGDLKNYKRGEDYVNFR
PDRVAMQDATAQMALLQFMNAGKEKVAVPSTVHCDHLIQAYKGAKEDIATATKTNEEVYD
FLRDVSSRYGIGFWKPGAGIIHQVVLENYAFPGGMMVGTDSHTPNAGGLGMVAIGVGGAD
AVDVMTGMEWELKMPRIIGVRLTGKLSGWTSPKDVILKLAGILTVKGGTNSIIEYFGPGT
ASLSATGKATICNMGAEVGATTSLFPFDGRMATYLRATGRDRIVELAEAVDCELRADQQV
TDEPEKYYDRVIDIDLSTLEPYINGPFTPDAATPISEFAEKVLLNGYPRKMEVGLIGSCT
NSSYQDLSRAASLARQVKEKNLSVASPLIINPGSEQIRATAERDGMMDDFMQIGAVIMAN
ACGPCIGQWKRHTDDPTRKNSIVTSFNRNFAKRADGNPNTYAFVASPELTMALTIAGDLC
FNPLKDRLMNHDGEKVKLAEPVGDELPLRGFTSGNEGYITPGGTKTAINVNPASQRLQLL
TPFPAWDGQDILNMPLLIKAQGKCTTDHISMAGPWLRFRGHLENISDNMLMGAVNAFNGE
TNNVWNRSTNTYGTVSGTAKMYKSEGIPSIVVAEENYGEGSSREHAAMEPRFLNVRVILA
KSFARIHETNLKKQGMLALTFADKADYDKIQEHDLLSVIGLPDFAPGRNLTVVLHHEDGT
KESFEAQHTYNEQQIAWFRAGSALNAR
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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