SitesBLAST
Comparing WP_086508286.1 NCBI__GCF_002151265.1:WP_086508286.1 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)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 98% coverage: 2:642/656 of query aligns to 53:782/789 of P39533
- K610 (≠ P504) 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)
31% identity, 98% coverage: 2:643/656 of query aligns to 58:773/778 of P19414
- R604 (≠ Y495) 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)
32% identity, 98% coverage: 2:643/656 of query aligns to 35:749/754 of 5acnA
- active site: D100 (= D64), H101 (= H65), D165 (= D119), R447 (= R379), S642 (= S539), R644 (= R541)
- binding fe3-s4 cluster: I145 (= I99), H147 (= H101), H167 (= H121), C358 (≠ S297), C421 (= C357), C424 (= C360), N446 (≠ P378)
- binding tricarballylic acid: K198 (≠ S152), G235 (≠ N189), R666 (= R563)
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
31% identity, 98% coverage: 2:643/656 of query aligns to 34:748/753 of 8acnA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S539), R643 (= R541)
- binding nitroisocitric acid: Q71 (= Q35), T74 (≠ L38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (vs. gap), 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, 98% coverage: 2:643/656 of query aligns to 34:748/753 of 1fghA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S539), R643 (= R541)
- binding 4-hydroxy-aconitate ion: Q71 (= Q35), T74 (≠ L38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (vs. gap), 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, 98% coverage: 2:643/656 of query aligns to 34:748/753 of 1amjA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S539), R643 (= R541)
- binding iron/sulfur cluster: I144 (= I99), H166 (= H121), C357 (≠ S297), C420 (= C357), C423 (= C360)
- binding sulfate ion: Q71 (= Q35), R579 (vs. gap), R643 (= R541)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
31% identity, 98% coverage: 2:643/656 of query aligns to 34:748/753 of 1amiA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S539), R643 (= R541)
- binding alpha-methylisocitric acid: Q71 (= Q35), T74 (≠ L38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (vs. gap), S641 (= S539), S642 (= S540), R643 (= R541)
- binding iron/sulfur cluster: H100 (= H65), I144 (= I99), 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, 98% coverage: 2:643/656 of query aligns to 34:748/753 of 1acoA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S539), R643 (= R541)
- binding iron/sulfur cluster: H100 (= H65), I144 (= I99), 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 (vs. gap), S641 (= S539), S642 (= S540), R643 (= R541)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
32% identity, 98% coverage: 2:643/656 of query aligns to 62:776/781 of P16276
- Q99 (= Q35) binding
- DSH 192:194 (= DSH 119:121) binding
- C385 (≠ S297) binding
- C448 (= C357) binding
- C451 (= C360) binding
- R474 (= R379) binding
- R479 (= R384) binding
- R607 (vs. gap) binding
- SR 670:671 (= SR 540:541) binding
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
31% identity, 98% coverage: 2:643/656 of query aligns to 34:748/753 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 (vs. gap), S641 (= S539), S642 (= S540)
- binding iron/sulfur cluster: H100 (= H65), I144 (= I99), H166 (= H121), S356 (= S296), C357 (≠ S297), C420 (= C357), C423 (= C360)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
31% identity, 98% coverage: 2:643/656 of query aligns to 34:748/753 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 (vs. gap), 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)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
32% identity, 98% coverage: 2:643/656 of query aligns to 62:776/780 of P20004
- Q99 (= Q35) binding
- DSH 192:194 (= DSH 119:121) binding
- C385 (≠ S297) binding
- C448 (= C357) binding
- C451 (= C360) binding
- R474 (= R379) binding
- R479 (= R384) binding
- R607 (vs. gap) binding
- SR 670:671 (= SR 540:541) binding
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
27% identity, 63% coverage: 3:415/656 of query aligns to 2:423/423 of 4kp1A
- active site: D64 (≠ H65), H65 (≠ G66), 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 (≠ G298), R387 (= R379)
4nqyA The reduced form of mj0499 (see paper)
26% identity, 63% coverage: 3:413/656 of query aligns to 1:408/409 of 4nqyA
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
25% identity, 95% coverage: 24:644/656 of query aligns to 74:884/888 of 2b3xA
- active site: D124 (= D64), H125 (= H65), D204 (= D119), R535 (= R379), S777 (= S539), R779 (= R541)
- binding iron/sulfur cluster: I175 (= I99), H206 (= H121), C436 (≠ S297), C502 (= C357), C505 (= C360), I506 (= I361), N534 (≠ P378)
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)
25% identity, 95% coverage: 24:644/656 of query aligns to 75:885/889 of P21399
- C300 (≠ G214) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ R232) to M: in dbSNP:rs150373174
- C437 (≠ S297) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C357) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C360) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R379) mutation to Q: Strongly reduced RNA binding.
- R541 (= R384) mutation to Q: Strongly reduced RNA binding.
- R699 (vs. gap) mutation to K: No effect on RNA binding.
- S778 (= S539) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R541) mutation to Q: Nearly abolishes RNA binding.
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)
26% identity, 71% coverage: 24:489/656 of query aligns to 85:697/909 of P09339
- C450 (vs. gap) 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.
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)
24% identity, 97% coverage: 2:636/656 of query aligns to 8:706/758 of O14289
- S486 (≠ A426) modified: Phosphoserine
- S488 (≠ M428) modified: Phosphoserine
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
26% identity, 95% coverage: 24:644/656 of query aligns to 74:846/850 of 3snpA
- active site: D124 (= D64), H125 (= H65), D186 (= D119), R505 (= R379), S739 (= S539), R741 (= R541)
- binding : H125 (= H65), S126 (≠ G66), H188 (= H121), L243 (= L176), R250 (≠ G183), N279 (= N212), E283 (= E216), S352 (≠ A270), P357 (= P275), K360 (≠ V278), T419 (≠ I325), N420 (= N326), T421 (≠ P327), N504 (≠ P378), R505 (= R379), L520 (= L394), S642 (≠ M486), P643 (= P487), A644 (= A488), G645 (= G489), N646 (≠ Q490), R649 (≠ M493), R665 (≠ F505), S669 (≠ A509), G671 (vs. gap), R674 (vs. gap), R741 (= R541)
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)
26% identity, 73% coverage: 12:490/656 of query aligns to 157:781/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
Query Sequence
>WP_086508286.1 NCBI__GCF_002151265.1:WP_086508286.1
MPLNLAQQLIRDHLVDGEMTPGSEIALRIDQALLQDVLGTLVMLELEAMGLDRVKTQPSV
QYIDHGLVQADNLNAETYLFLKSACERFGVWYSGPGNGISHPVHMEHFGIPGQSIVGCDS
HTTAAGSLGMLAIGAGGIEVAMAMAGEPLYLSMPEIWGIRLAGSLPDWVSAKDAVLELLR
RHGVAGAKNTIIEYHGPGLANLSAMDRHVLANMGTEMGATATVFPSDEEARRFLAARGRE
ADWKPLAAEPGCTYDREEVLDLSSLEPLIALPSSPDKVVPVREVVGEPLHQAYIGSSGNP
GYRDFAVVAEMVRGRTVADGVSLDINPSSRQVLATLIRDGYLADLVASGARLHQTGCNGC
IGMGQAPAVGRNSLRTVPRNFPGRSGTREDSVFLCSPETAAASALAGSIADPRSLDMAYP
RIAEPAQMVVNRDVFVAPLPLAEARLKPLQKTDNTPALPELAALPDTLEVPVLLVTGDNV
STDDIMPAGQRVMPYWSSVYASAPFTFEAVDADYARRAENTRTLGGHAIVGGHNYGQGSS
RENAALVPRYLGLQAVLAKSFARIHWQNLICFGALPLSFIDAQDYDRLEQGDSLVIHDLH
AQLAAGAELTAEVVGKGAFRLHHGLTPRQRELLACGGVINHIRRGKGASAGAAGIS
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