SitesBLAST
Comparing WP_015798815.1 NCBI__GCF_000023265.1:WP_015798815.1 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)
57% identity, 96% coverage: 22:749/755 of query aligns to 46:773/778 of P19414
- R604 (= R580) 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)
56% identity, 97% coverage: 21:750/755 of query aligns to 22:750/754 of 5acnA
- active site: D100 (= D99), H101 (= H100), D165 (= D164), R447 (= R452), S642 (= S642), R644 (= R644)
- binding fe3-s4 cluster: I145 (= I144), H147 (= H146), H167 (= H166), C358 (= C363), C421 (= C426), C424 (= C429), N446 (= N451)
- binding tricarballylic acid: K198 (≠ R197), G235 (= G234), R666 (= R666)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
56% identity, 97% coverage: 21:750/755 of query aligns to 49:777/781 of P16276
- Q99 (= Q71) binding substrate
- DSH 192:194 (= DSH 164:166) binding substrate
- C385 (= C363) binding [4Fe-4S] cluster
- C448 (= C426) binding [4Fe-4S] cluster
- C451 (= C429) binding [4Fe-4S] cluster
- R474 (= R452) binding substrate
- R479 (= R457) binding substrate
- R607 (= R580) binding substrate
- SR 670:671 (= SR 643:644) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
56% identity, 97% coverage: 21:750/755 of query aligns to 21:749/753 of 1b0kA
- active site: D99 (= D99), H100 (= H100), D164 (= D164), R446 (= R452), A641 (≠ S642), R643 (= R644)
- binding citrate anion: Q71 (= Q71), H100 (= H100), D164 (= D164), S165 (= S165), R446 (= R452), R451 (= R457), R579 (= R580), A641 (≠ S642), S642 (= S643), R643 (= R644)
- binding oxygen atom: D164 (= D164), H166 (= H166)
- binding iron/sulfur cluster: H100 (= H100), D164 (= D164), H166 (= H166), S356 (= S362), C357 (= C363), C420 (= C426), C423 (= C429)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
56% identity, 97% coverage: 21:750/755 of query aligns to 49:777/780 of P20004
- Q99 (= Q71) binding substrate
- DSH 192:194 (= DSH 164:166) binding substrate
- C385 (= C363) binding [4Fe-4S] cluster
- C448 (= C426) binding [4Fe-4S] cluster
- C451 (= C429) binding [4Fe-4S] cluster
- R474 (= R452) binding substrate
- R479 (= R457) binding substrate
- R607 (= R580) binding substrate
- SR 670:671 (= SR 643:644) binding substrate
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
56% identity, 97% coverage: 21:750/755 of query aligns to 21:749/753 of 8acnA
- active site: D99 (= D99), H100 (= H100), D164 (= D164), R446 (= R452), S641 (= S642), R643 (= R644)
- binding nitroisocitric acid: Q71 (= Q71), T74 (= T74), H100 (= H100), D164 (= D164), S165 (= S165), R446 (= R452), R451 (= R457), R579 (= R580), S641 (= S642), S642 (= S643), R643 (= R644)
- binding iron/sulfur cluster: H100 (= H100), D164 (= D164), H166 (= H166), S356 (= S362), C357 (= C363), C420 (= C426), C423 (= C429), I424 (= I430)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
56% identity, 97% coverage: 21:750/755 of query aligns to 21:749/753 of 1fghA
- active site: D99 (= D99), H100 (= H100), D164 (= D164), R446 (= R452), S641 (= S642), R643 (= R644)
- binding 4-hydroxy-aconitate ion: Q71 (= Q71), T74 (= T74), H100 (= H100), D164 (= D164), S165 (= S165), R446 (= R452), R451 (= R457), R579 (= R580), S641 (= S642), S642 (= S643), R643 (= R644)
- binding iron/sulfur cluster: H100 (= H100), D164 (= D164), H166 (= H166), S356 (= S362), C357 (= C363), C420 (= C426), C423 (= C429), I424 (= I430), R451 (= R457)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
56% identity, 97% coverage: 21:750/755 of query aligns to 21:749/753 of 1amjA
- active site: D99 (= D99), H100 (= H100), D164 (= D164), R446 (= R452), S641 (= S642), R643 (= R644)
- binding iron/sulfur cluster: I144 (= I144), H166 (= H166), C357 (= C363), C420 (= C426), C423 (= C429)
- binding sulfate ion: Q71 (= Q71), R579 (= R580), R643 (= R644)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
56% identity, 97% coverage: 21:750/755 of query aligns to 21:749/753 of 1amiA
- active site: D99 (= D99), H100 (= H100), D164 (= D164), R446 (= R452), S641 (= S642), R643 (= R644)
- binding alpha-methylisocitric acid: Q71 (= Q71), T74 (= T74), H100 (= H100), D164 (= D164), S165 (= S165), R446 (= R452), R451 (= R457), R579 (= R580), S641 (= S642), S642 (= S643), R643 (= R644)
- binding iron/sulfur cluster: H100 (= H100), I144 (= I144), D164 (= D164), H166 (= H166), S356 (= S362), C357 (= C363), C420 (= C426), C423 (= C429), N445 (= N451)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
56% identity, 97% coverage: 21:750/755 of query aligns to 21:749/753 of 1acoA
- active site: D99 (= D99), H100 (= H100), D164 (= D164), R446 (= R452), S641 (= S642), R643 (= R644)
- binding iron/sulfur cluster: H100 (= H100), I144 (= I144), D164 (= D164), H166 (= H166), S356 (= S362), C357 (= C363), C420 (= C426), C423 (= C429), N445 (= N451)
- binding aconitate ion: Q71 (= Q71), D164 (= D164), S165 (= S165), R446 (= R452), R451 (= R457), R579 (= R580), S641 (= S642), S642 (= S643), R643 (= R644)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
56% identity, 97% coverage: 21:750/755 of query aligns to 21:749/753 of 1nisA
- active site: D99 (= D99), H100 (= H100), D164 (= D164), R446 (= R452), S641 (= S642), R643 (= R644)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q71), H100 (= H100), D164 (= D164), S165 (= S165), R446 (= R452), R451 (= R457), R579 (= R580), S641 (= S642), S642 (= S643)
- binding iron/sulfur cluster: H100 (= H100), I144 (= I144), H166 (= H166), S356 (= S362), C357 (= C363), C420 (= C426), C423 (= C429)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
49% identity, 97% coverage: 14:748/755 of query aligns to 36:782/789 of P39533
- K610 (≠ R580) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
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)
30% identity, 91% coverage: 61:748/755 of query aligns to 86:901/909 of P09339
- C450 (= C363) 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 (≠ G593) 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
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, 95% coverage: 30:750/755 of query aligns to 31:886/889 of P21399
- C300 (≠ G259) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ A277) to M: in dbSNP:rs150373174
- C437 (= C363) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C426) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C429) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R452) mutation to Q: Strongly reduced RNA binding.
- R541 (= R457) mutation to Q: Strongly reduced RNA binding.
- R699 (vs. gap) mutation to K: No effect on RNA binding.
- S778 (= S642) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R644) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
29% identity, 95% coverage: 30:750/755 of query aligns to 30:885/888 of 2b3xA
- active site: D124 (= D99), H125 (= H100), D204 (= D164), R535 (= R452), S777 (= S642), R779 (= R644)
- binding iron/sulfur cluster: I175 (= I144), H206 (= H166), C436 (= C363), C502 (= C426), C505 (= C429), I506 (= I430), N534 (= N451)
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: 51:745/755 of query aligns to 153:980/990 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)
29% identity, 84% coverage: 119:750/755 of query aligns to 131:847/850 of 3snpA
- active site: D186 (= D164), R505 (= R452), S739 (= S642), R741 (= R644)
- binding : H188 (= H166), L243 (= L221), R250 (≠ T228), N279 (= N257), E283 (= E261), S352 (≠ V328), P357 (= P333), K360 (vs. gap), T419 (= T364), N420 (= N365), T421 (≠ S366), N504 (= N451), R505 (= R452), L520 (≠ I468), S642 (= S571), P643 (≠ A572), A644 (= A573), G645 (= G574), N646 (vs. gap), R649 (vs. gap), R665 (vs. gap), S669 (vs. gap), G671 (vs. gap), R674 (= R580), R741 (= R644)
Sites not aligning to the query:
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)
36% identity, 36% coverage: 61:333/755 of query aligns to 74:371/931 of D9X0I3
- SVIAD 125:129 (≠ LIQAE 101:105) 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.
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
26% identity, 48% coverage: 125:483/755 of query aligns to 84:417/423 of 4kp1A
Sites not aligning to the query:
4nqyA The reduced form of mj0499 (see paper)
26% identity, 48% coverage: 125:483/755 of query aligns to 71:404/409 of 4nqyA
Sites not aligning to the query:
Query Sequence
>WP_015798815.1 NCBI__GCF_000023265.1:WP_015798815.1
MAEVRDTTPAALVAKALARYEEVASVLRERLGRPLTFAEKVLYAHLRHPERAELERGVSW
IELDPDRVAMQDATAQMALLQFMVADLPEVRVPTTVHCDHLIQAERGADDDLAAARVTNR
EVYDFLSSVSARYGIGFWEPGAGIIHQVVLEQYAFPGGMIIGTDSHTPNAGGLGMVAIGV
GGADAVDVMVGDPFTVRMPRLIGVRLTGRPNGWTSAKDVILRVAEILTVKGGTGAVVEYF
GPGARALSTTGKATICNMGAEIGATCSLFPADDHAVAYLRATGRDEIAALVEARLGSLEA
DPEVEEDPARYFDQVIEIDLDTLEPQIVGPATPDLGRGVGSIGREAREHGWPLELSSALV
GSCTNSSYEDIARAASVARWASARGLRVRTPLLVTPGSERIRATIERDGLLRDLEAIGAT
VLANACGPCIGQWHRTDIEPGTTNSIITSYNRNFPRRNDGNAATLAFIASPEVVVAYALA
GTLDFNPLTDELAGERLPEPEGLELPSAGLAREVRGFVAPPADGSAIEVRIDPASERLQV
LTPFEPFEGGDLVGLVVLAKAVGKCTTDHISAAGPWLRYRGHLDNISRNLFLGVQNAFAA
EPGHGWCQIHQADEPLPEIARHYRDAGQGWVMIGDENYGEGSSREHAAMEPRYLGARAII
ARSFARIHETNLKKQGMLPLTFTDPADYERIERDDRVDLVGLDELAPDQPIRAVVHRPDG
TSFDLELRHTFSEDQIAWFRAGSALNMIRQRHHHG
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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