SitesBLAST
Comparing WP_013706496.1 NCBI__GCF_000195295.1:WP_013706496.1 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)
35% identity, 92% coverage: 3:592/641 of query aligns to 55:731/789 of P39533
- K610 (≠ R492) 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)
35% identity, 91% coverage: 3:587/641 of query aligns to 60:721/778 of P19414
- R604 (= R492) 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)
35% identity, 92% coverage: 3:593/641 of query aligns to 64:730/780 of P20004
- Q99 (= Q34) binding substrate
- DSH 192:194 (= DSH 118:120) binding substrate
- C385 (= C296) binding [4Fe-4S] cluster
- C448 (= C356) binding [4Fe-4S] cluster
- C451 (= C359) binding [4Fe-4S] cluster
- R474 (= R378) binding substrate
- R479 (= R383) binding substrate
- R607 (= R492) binding substrate
- SR 670:671 (= SR 533:534) binding substrate
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 36:702/753 of 8acnA
- active site: D99 (= D63), H100 (= H64), D164 (= D118), R446 (= R378), S641 (= S532), R643 (= R534)
- binding nitroisocitric acid: Q71 (= Q34), T74 (= T37), H100 (= H64), D164 (= D118), S165 (= S119), R446 (= R378), R451 (= R383), R579 (= R492), S641 (= S532), S642 (= S533), R643 (= R534)
- binding iron/sulfur cluster: H100 (= H64), D164 (= D118), H166 (= H120), S356 (= S295), C357 (= C296), C420 (= C356), C423 (= C359), I424 (= I360)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 36:702/753 of 1fghA
- active site: D99 (= D63), H100 (= H64), D164 (= D118), R446 (= R378), S641 (= S532), R643 (= R534)
- binding 4-hydroxy-aconitate ion: Q71 (= Q34), T74 (= T37), H100 (= H64), D164 (= D118), S165 (= S119), R446 (= R378), R451 (= R383), R579 (= R492), S641 (= S532), S642 (= S533), R643 (= R534)
- binding iron/sulfur cluster: H100 (= H64), D164 (= D118), H166 (= H120), S356 (= S295), C357 (= C296), C420 (= C356), C423 (= C359), I424 (= I360), R451 (= R383)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 36:702/753 of 1amjA
- active site: D99 (= D63), H100 (= H64), D164 (= D118), R446 (= R378), S641 (= S532), R643 (= R534)
- binding iron/sulfur cluster: I144 (= I98), H166 (= H120), C357 (= C296), C420 (= C356), C423 (= C359)
- binding sulfate ion: Q71 (= Q34), R579 (= R492), R643 (= R534)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 36:702/753 of 1amiA
- active site: D99 (= D63), H100 (= H64), D164 (= D118), R446 (= R378), S641 (= S532), R643 (= R534)
- binding alpha-methylisocitric acid: Q71 (= Q34), T74 (= T37), H100 (= H64), D164 (= D118), S165 (= S119), R446 (= R378), R451 (= R383), R579 (= R492), S641 (= S532), S642 (= S533), R643 (= R534)
- binding iron/sulfur cluster: H100 (= H64), I144 (= I98), D164 (= D118), H166 (= H120), S356 (= S295), C357 (= C296), C420 (= C356), C423 (= C359), N445 (≠ P377)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 36:702/753 of 1acoA
- active site: D99 (= D63), H100 (= H64), D164 (= D118), R446 (= R378), S641 (= S532), R643 (= R534)
- binding iron/sulfur cluster: H100 (= H64), I144 (= I98), D164 (= D118), H166 (= H120), S356 (= S295), C357 (= C296), C420 (= C356), C423 (= C359), N445 (≠ P377)
- binding aconitate ion: Q71 (= Q34), D164 (= D118), S165 (= S119), R446 (= R378), R451 (= R383), R579 (= R492), S641 (= S532), S642 (= S533), R643 (= R534)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 37:703/754 of 5acnA
- active site: D100 (= D63), H101 (= H64), D165 (= D118), R447 (= R378), S642 (= S532), R644 (= R534)
- binding fe3-s4 cluster: I145 (= I98), H147 (= H100), H167 (= H120), C358 (= C296), C421 (= C356), C424 (= C359), N446 (≠ P377)
- binding tricarballylic acid: K198 (≠ V151), G235 (= G188), R666 (= R556)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 36:702/753 of 1nisA
- active site: D99 (= D63), H100 (= H64), D164 (= D118), R446 (= R378), S641 (= S532), R643 (= R534)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q34), H100 (= H64), D164 (= D118), S165 (= S119), R446 (= R378), R451 (= R383), R579 (= R492), S641 (= S532), S642 (= S533)
- binding iron/sulfur cluster: H100 (= H64), I144 (= I98), H166 (= H120), S356 (= S295), C357 (= C296), C420 (= C356), C423 (= C359)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
35% identity, 92% coverage: 3:593/641 of query aligns to 64:730/781 of P16276
- Q99 (= Q34) binding substrate
- DSH 192:194 (= DSH 118:120) binding substrate
- C385 (= C296) binding [4Fe-4S] cluster
- C448 (= C356) binding [4Fe-4S] cluster
- C451 (= C359) binding [4Fe-4S] cluster
- R474 (= R378) binding substrate
- R479 (= R383) binding substrate
- R607 (= R492) binding substrate
- SR 670:671 (= SR 533:534) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 36:702/753 of 1b0kA
- active site: D99 (= D63), H100 (= H64), D164 (= D118), R446 (= R378), A641 (≠ S532), R643 (= R534)
- binding citrate anion: Q71 (= Q34), H100 (= H64), D164 (= D118), S165 (= S119), R446 (= R378), R451 (= R383), R579 (= R492), A641 (≠ S532), S642 (= S533), R643 (= R534)
- binding oxygen atom: D164 (= D118), H166 (= H120)
- binding iron/sulfur cluster: H100 (= H64), D164 (= D118), H166 (= H120), S356 (= S295), C357 (= C296), C420 (= C356), C423 (= C359)
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
31% identity, 64% coverage: 3:414/641 of query aligns to 3:423/423 of 4kp1A
- active site: D64 (= D63), H65 (= H64), D121 (= D118), R387 (= R378)
- binding 2,4-dimethylpentane-2,4-diol: F299 (≠ A292), S302 (= S295), S383 (≠ R374), F389 (= F380)
- binding magnesium ion: C303 (= C296), T304 (≠ S297), R387 (= R378)
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)
27% identity, 86% coverage: 23:572/641 of query aligns to 75:818/889 of P21399
- C300 (≠ G213) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ S231) to M: in dbSNP:rs150373174
- C437 (= C296) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C356) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C359) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R378) mutation to Q: Strongly reduced RNA binding.
- R541 (= R383) mutation to Q: Strongly reduced RNA binding.
- R699 (= R492) mutation to K: No effect on RNA binding.
- S778 (= S532) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R534) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
27% identity, 86% coverage: 23:572/641 of query aligns to 74:817/888 of 2b3xA
- active site: D124 (= D63), H125 (= H64), D204 (= D118), R535 (= R378), S777 (= S532), R779 (= R534)
- binding iron/sulfur cluster: I175 (= I98), H206 (= H120), C436 (= C296), C502 (= C356), C505 (= C359), I506 (= I360), N534 (≠ P377)
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, 87% coverage: 25:581/641 of query aligns to 137:841/909 of P09339
- C450 (= C296) 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 (vs. gap) 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
4nqyA The reduced form of mj0499 (see paper)
29% identity, 64% coverage: 3:412/641 of query aligns to 2:408/409 of 4nqyA
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, 90% coverage: 6:581/641 of query aligns to 157:924/990 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)
28% identity, 86% coverage: 23:572/641 of query aligns to 74:779/850 of 3snpA
- active site: D124 (= D63), H125 (= H64), D186 (= D118), R505 (= R378), S739 (= S532), R741 (= R534)
- binding : H125 (= H64), S126 (≠ N65), H188 (= H120), L243 (= L175), R250 (≠ T182), N279 (= N211), E283 (= E215), S352 (≠ A269), P357 (= P274), K360 (≠ V277), T419 (≠ S297), N420 (= N298), T421 (≠ S299), N504 (≠ R374), R505 (= R378), L520 (= L393), S642 (≠ M482), P643 (= P483), A644 (= A484), G645 (= G485), N646 (vs. gap), R649 (vs. gap), R665 (vs. gap), S669 (vs. gap), G671 (vs. gap), R674 (vs. gap), R741 (= R534)
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, 94% coverage: 3:607/641 of query aligns to 10:695/758 of O14289
- S486 (≠ R424) modified: Phosphoserine
- S488 (≠ F426) modified: Phosphoserine
Query Sequence
>WP_013706496.1 NCBI__GCF_000195295.1:WP_013706496.1
MSTVTERIIKAHLVSGKMALGEEIAIRIDQTLTQDATGTMACLEFEAMGAPSVHTELSVS
YVDHNLLQTDYKNADDHRFLQSFAAGHGIYFSPPGNGICHQVHLEAFGVPGKTLLGSDSH
TPTGGGLGMLAIGAGGLDVALAMAGQPFYLVMPEVVGVHLIGRLPDWVSAKDVILELLRR
LTVKGGVGKILEYFGPGVQTLSVPDRATIANMGAELGATTSVFPSDAVTKSFLASQGRTA
VYRSLRASNAEDFKEIIEVDLGSLTPKIACPSSPDKVRDVSDVEGTPVQQVAIGSCSNSS
YRDLMIVAKILEGRKIHPQVSLEINPGSRQVLENVTIAGGLLSLIRAGARMHQSGCLGCI
GMGQAPATNTVSLRTFPRNFPGRSGTKNDQVYLVSPETAAAAAIYGKITDPRRLGDYPKI
RQPRHFVIENRQLQAPLDPGQSCEIIRGPNIQPFPKFTAIPETWEGQVFLKVGDNITTDH
IMPAGSQILPLRSNIPAISRFVYQAVDPGFIARAEQSGEGAVVGGDNYGQGSSREHAALA
PRYLGVRIKLAKSFARIHKANLINFGILPLVFENPQDYDRIQSGDRLLLPNLRQRLMAGD
ERLPLLVNGEECWVRLELSPRHRQIIAAGGLLNMPDGNSPK
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