SitesBLAST
Comparing WP_010530341.1 NCBI__GCF_000224785.1:WP_010530341.1 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)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
32% identity, 99% coverage: 3:643/650 of query aligns to 54:782/789 of P39533
- K610 (≠ R496) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
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)
29% identity, 96% coverage: 27:649/650 of query aligns to 87:778/778 of P19414
- R604 (= R496) 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
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
31% identity, 100% coverage: 3:649/650 of query aligns to 35:753/753 of 8acnA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S539), R643 (= R541)
- binding nitroisocitric acid: Q71 (= Q35), T74 (= T38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R496), S641 (= S539), S642 (= S540), R643 (= R541)
- binding iron/sulfur cluster: H100 (= H65), D164 (= D119), H166 (= H121), S356 (= S296), C357 (≠ S297), C420 (= C357), C423 (= C360), I424 (= I361)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
31% identity, 100% coverage: 3:649/650 of query aligns to 35:753/753 of 1fghA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S539), R643 (= R541)
- binding 4-hydroxy-aconitate ion: Q71 (= Q35), T74 (= T38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R496), S641 (= S539), S642 (= S540), R643 (= R541)
- binding iron/sulfur cluster: H100 (= H65), D164 (= D119), H166 (= H121), S356 (= S296), C357 (≠ S297), C420 (= C357), C423 (= C360), I424 (= I361), R451 (= R384)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
31% identity, 100% coverage: 3:649/650 of query aligns to 35:753/753 of 1amjA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S539), R643 (= R541)
- binding iron/sulfur cluster: I144 (≠ V99), H166 (= H121), C357 (≠ S297), C420 (= C357), C423 (= C360)
- binding sulfate ion: Q71 (= Q35), R579 (= R496), R643 (= R541)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
31% identity, 100% coverage: 3:649/650 of query aligns to 35:753/753 of 1amiA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S539), R643 (= R541)
- binding alpha-methylisocitric acid: Q71 (= Q35), T74 (= T38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R496), S641 (= S539), S642 (= S540), R643 (= R541)
- binding iron/sulfur cluster: H100 (= H65), I144 (≠ V99), D164 (= D119), H166 (= H121), S356 (= S296), C357 (≠ S297), C420 (= C357), C423 (= C360), N445 (≠ P378)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
31% identity, 100% coverage: 3:649/650 of query aligns to 35:753/753 of 1acoA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S539), R643 (= R541)
- binding iron/sulfur cluster: H100 (= H65), I144 (≠ V99), D164 (= D119), H166 (= H121), S356 (= S296), C357 (≠ S297), C420 (= C357), C423 (= C360), N445 (≠ P378)
- binding aconitate ion: Q71 (= Q35), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R496), S641 (= S539), S642 (= S540), R643 (= R541)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
31% identity, 100% coverage: 3:649/650 of query aligns to 35:753/753 of 1nisA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S539), R643 (= R541)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q35), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R496), S641 (= S539), S642 (= S540)
- binding iron/sulfur cluster: H100 (= H65), I144 (≠ V99), H166 (= H121), S356 (= S296), C357 (≠ S297), C420 (= C357), C423 (= C360)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
31% identity, 99% coverage: 3:648/650 of query aligns to 63:780/780 of P20004
- Q99 (= Q35) binding substrate
- DSH 192:194 (= DSH 119:121) binding substrate
- C385 (≠ S297) binding [4Fe-4S] cluster
- C448 (= C357) binding [4Fe-4S] cluster
- C451 (= C360) binding [4Fe-4S] cluster
- R474 (= R379) binding substrate
- R479 (= R384) binding substrate
- R607 (= R496) binding substrate
- SR 670:671 (= SR 540:541) binding substrate
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
31% identity, 100% coverage: 3:649/650 of query aligns to 36:754/754 of 5acnA
- active site: D100 (= D64), H101 (= H65), D165 (= D119), R447 (= R379), S642 (= S539), R644 (= R541)
- binding fe3-s4 cluster: I145 (≠ V99), H147 (= H101), H167 (= H121), C358 (≠ S297), C421 (= C357), C424 (= C360), N446 (≠ P378)
- binding tricarballylic acid: K198 (= K152), G235 (= G189), R666 (= R563)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
31% identity, 100% coverage: 3:649/650 of query aligns to 63:781/781 of P16276
- Q99 (= Q35) binding substrate
- DSH 192:194 (= DSH 119:121) binding substrate
- C385 (≠ S297) binding [4Fe-4S] cluster
- C448 (= C357) binding [4Fe-4S] cluster
- C451 (= C360) binding [4Fe-4S] cluster
- R474 (= R379) binding substrate
- R479 (= R384) binding substrate
- R607 (= R496) binding substrate
- SR 670:671 (= SR 540:541) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
31% identity, 100% coverage: 3:649/650 of query aligns to 35:753/753 of 1b0kA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), A641 (≠ S539), R643 (= R541)
- binding citrate anion: Q71 (= Q35), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R496), A641 (≠ S539), S642 (= S540), R643 (= R541)
- binding oxygen atom: D164 (= D119), H166 (= H121)
- binding iron/sulfur cluster: H100 (= H65), D164 (= D119), H166 (= H121), S356 (= S296), C357 (≠ S297), C420 (= C357), C423 (= C360)
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
29% identity, 64% coverage: 3:415/650 of query aligns to 2:423/423 of 4kp1A
- active site: D64 (= D64), H65 (= H65), D121 (= D119), R387 (= R379)
- binding 2,4-dimethylpentane-2,4-diol: F299 (≠ Y293), S302 (= S296), S383 (≠ R375), F389 (= F381)
- binding magnesium ion: C303 (≠ S297), T304 (≠ A298), R387 (= R379)
4nqyA The reduced form of mj0499 (see paper)
29% identity, 63% coverage: 3:413/650 of query aligns to 1:408/409 of 4nqyA
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)
27% identity, 88% coverage: 8:577/650 of query aligns to 14:655/758 of O14289
- S486 (vs. gap) modified: Phosphoserine
- S488 (≠ N416) modified: Phosphoserine
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)
25% identity, 91% coverage: 51:643/650 of query aligns to 226:983/990 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)
27% identity, 53% coverage: 66:412/650 of query aligns to 152:587/909 of P09339
- C450 (≠ S297) 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.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 741 R→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.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
29% identity, 37% coverage: 70:310/650 of query aligns to 145:406/888 of 2b3xA
Sites not aligning to the query:
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)
29% identity, 37% coverage: 70:310/650 of query aligns to 146:407/889 of P21399
- C300 (≠ G214) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ R232) to M: in dbSNP:rs150373174
Sites not aligning to the query:
- 437 C→S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- 503 C→S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- 506 C→S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- 536 R→Q: Strongly reduced RNA binding.
- 541 R→Q: Strongly reduced RNA binding.
- 699 R→K: No effect on RNA binding.
- 778 S→A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- 780 R→Q: Nearly abolishes RNA binding.
D9X0I3 Aconitate hydratase A; ACN; Aconitase; EC 4.2.1.3 from Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494) (see paper)
32% identity, 41% coverage: 18:285/650 of query aligns to 67:381/931 of D9X0I3
- SVIAD 125:129 (≠ NLIQ- 66:69) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
Sites not aligning to the query:
- 538 C→A: Loss of aconitase activity. Cannot rescue the growth defect of a disruption mutant and results in only a slight increase in PTT production in the mutant. Shows weak IRE-binding activity.
- 763 R→E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- 767 Q→E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
Query Sequence
>WP_010530341.1 NCBI__GCF_000224785.1:WP_010530341.1
MALNVTQKLIKDHLVSGEMKPGAEIGLQIDQTLTQDATGTMVMLELEAMGLDYAKTEASA
QYVDHNLIQEDNKNPDDHLFLESAAQRFGLHFSRPGNGVSHPVHMQRLAIPGKTLLGSDS
HTCANGCMGMLAMGAGGIDVAMAITGEPIYIKMPEVMGVKLTGKLPDWVSAKDVILEMLR
RHDVKGGVGKIIEYYGPGLDDLTAMDRHVIANMGAELGATATVFPSDNEVKRFLSMQDRE
NDWVELTADNNAAYDIHEEINLSELEPLVAKPSSPGNVVPARELAGTPIYQSYIGSSANP
GYRDFAIAAEIVKDRNIATGVSFDINPTSRQMLTNLVKEMHIASLLQSGARLHQAGCNGC
IGMGQAPASGRNSLRTTPRNFPGRSGTKEDSVFLSSPETAAVSALTGEITDPRTMNFPYP
KVTDPSEPNVDDRLLEKPLPPEEAQKKELAKGPNIASIPAMDSLPDTLDVPVLLKVGDNI
STDEILAGGARVLPYRSNLPEISKFTYEDVDPTYVDRANVTKEKSGHTIVGGLNYGQGSS
REHAALAPRYLGLRVVLVKDFARIHWQNLVNFGVLPLKFTNEDDYEKIEKEAVLHFEDLR
SQVKNNDNIKLTRTDSGDEIIAEHNLSERQREVILSGGLINWIKDRQQKV
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