SitesBLAST
Comparing WP_012383914.1 NCBI__GCF_000019845.1:WP_012383914.1 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)
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)
32% identity, 95% coverage: 6:640/668 of query aligns to 62:770/778 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
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
31% identity, 96% coverage: 5:644/668 of query aligns to 56:788/789 of P39533
- K610 (≠ R496) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
32% identity, 95% coverage: 5:640/668 of query aligns to 38:746/754 of 5acnA
- active site: D100 (= D64), H101 (= H65), D165 (= D119), R447 (= R379), S642 (= S536), R644 (= R538)
- binding fe3-s4 cluster: I145 (= I99), H147 (= H101), H167 (= H121), C358 (≠ S297), C421 (= C357), C424 (= C360), N446 (≠ P378)
- binding tricarballylic acid: K198 (≠ A152), G235 (= G189), R666 (= R560)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
32% identity, 95% coverage: 5:640/668 of query aligns to 65:773/781 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 537:538) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
32% identity, 95% coverage: 5:640/668 of query aligns to 37:745/753 of 1b0kA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), A641 (≠ S536), R643 (= R538)
- binding citrate anion: Q71 (= Q35), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R496), A641 (≠ S536), S642 (= S537), R643 (= R538)
- 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, 96% coverage: 5:647/668 of query aligns to 65:780/780 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 537:538) binding substrate
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
32% identity, 95% coverage: 5:640/668 of query aligns to 37:745/753 of 8acnA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S536), R643 (= R538)
- binding nitroisocitric acid: Q71 (= Q35), T74 (= T38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R496), S641 (= S536), S642 (= S537), R643 (= R538)
- 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)
32% identity, 95% coverage: 5:640/668 of query aligns to 37:745/753 of 1fghA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S536), R643 (= R538)
- binding 4-hydroxy-aconitate ion: Q71 (= Q35), T74 (= T38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R496), S641 (= S536), S642 (= S537), R643 (= R538)
- 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)
32% identity, 95% coverage: 5:640/668 of query aligns to 37:745/753 of 1amjA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S536), R643 (= R538)
- binding iron/sulfur cluster: I144 (= I99), H166 (= H121), C357 (≠ S297), C420 (= C357), C423 (= C360)
- binding sulfate ion: Q71 (= Q35), R579 (= R496), R643 (= R538)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
32% identity, 95% coverage: 5:640/668 of query aligns to 37:745/753 of 1amiA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S536), R643 (= R538)
- binding alpha-methylisocitric acid: Q71 (= Q35), T74 (= T38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R496), S641 (= S536), S642 (= S537), R643 (= R538)
- 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)
32% identity, 95% coverage: 5:640/668 of query aligns to 37:745/753 of 1acoA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S536), R643 (= R538)
- 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 (= R496), S641 (= S536), S642 (= S537), R643 (= R538)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
32% identity, 95% coverage: 5:640/668 of query aligns to 37:745/753 of 1nisA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S536), R643 (= R538)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q35), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R496), S641 (= S536), S642 (= S537)
- binding iron/sulfur cluster: H100 (= H65), I144 (= I99), H166 (= H121), S356 (= S296), C357 (≠ S297), C420 (= C357), C423 (= C360)
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, 88% coverage: 19:604/668 of query aligns to 124:873/909 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.
- R741 (= R509) 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
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
30% identity, 59% coverage: 19:415/668 of query aligns to 18:423/423 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)
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
26% identity, 79% coverage: 59:585/668 of query aligns to 126:826/888 of 2b3xA
Sites not aligning to the query:
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)
27% identity, 85% coverage: 19:585/668 of query aligns to 210:924/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
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)
26% identity, 79% coverage: 59:585/668 of query aligns to 127:827/889 of P21399
- C300 (≠ G214) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (vs. gap) to M: in dbSNP:rs150373174
- C437 (vs. gap) 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 (= S536) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R538) mutation to Q: Nearly abolishes RNA binding.
4nqyA The reduced form of mj0499 (see paper)
29% identity, 59% coverage: 19:413/668 of query aligns to 17:408/409 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)
25% identity, 86% coverage: 3:574/668 of query aligns to 9:655/758 of O14289
- S486 (≠ A401) modified: Phosphoserine
- S488 (= S403) modified: Phosphoserine
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, 40% coverage: 19:283/668 of query aligns to 112:379/931 of D9X0I3
- SVIAD 125:129 (≠ TLTQD 32:36) 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_012383914.1 NCBI__GCF_000019845.1:WP_012383914.1
MAQNVSQKLIGSHLVDGVMNPGAPITLRIDQTLTQDATGTLVMLTLEAMELDHVKTEVSV
QYVDHNLLQIDNLNADDHLFLESACRRFGIWYSRPGNGISHVVHMERFGRPGKSLLGSDS
HTPAAGSLSMLAIGAGGLDVALAMAGEPYPTAMPRIFGVELKGALPDWVSAKDVILEMLR
RHGVSGGVGKIIEYYGPGLDCLSAMDRHVIANMGAELGATTTVFPSDEETKKFLEARGRG
RDWCAIAADPGCEYDDHDEIDLSKLEPLIAQPSSPGNVVAVKDIEGEDIYQAYIGSSANP
GWRDFAVAAEIVRGKSIPAHVSFDVNPTSRQGLEILVADGHLNDLLVAGARIHQTGCNGC
IGMGQAPAIGKNSLRTTPRNFPGRSGTEEDAVFLCSPETAAASALTGKITDPRSLSMSYP
RLREAESIAMTSSLIASPLSFEEARRVTLVKGPNIRSLPTLDPLPDSLDLPILLKMGDNV
STDEIMPAGAKVLPYRSNIEKIATFSFERIDETYVERTRTVPGHAVIAGRNYGQGSSREH
AAVGPRSLGLRLVLAKSFARIHRQNLINYGVLPLVFVEPKDYDSLEKDDVLAVRDLRRIL
EKGDEVVALESKGATKGVILARHGLTPKQIEIILAGGVTNLRRNASKLPPTEGAGTQRII
EHDALIVH
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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