SitesBLAST
Comparing WP_025274291.1 NCBI__GCF_000527155.1:WP_025274291.1 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)
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)
72% identity, 100% coverage: 1:906/906 of query aligns to 1:931/931 of D9X0I3
- SVIAD 125:129 (≠ SVVVD 125:129) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C510) mutation to 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.
- R763 (= R735) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (= Q739) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
A0QX20 Aconitate hydratase A; ACN; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; Iron-responsive protein-like; IRP-like; Probable 2-methyl-cis-aconitate hydratase; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
69% identity, 100% coverage: 2:905/906 of query aligns to 10:940/943 of A0QX20
- K394 (≠ R386) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
53% identity, 99% coverage: 2:901/906 of query aligns to 9:903/909 of P09339
- C450 (= C444) 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 (= R735) 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)
49% identity, 99% coverage: 10:903/906 of query aligns to 13:887/889 of P21399
- C300 (≠ S298) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ D316) to M: in dbSNP:rs150373174
- C437 (= C444) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C510) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C513) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R543) mutation to Q: Strongly reduced RNA binding.
- R541 (= R548) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ Q706) mutation to K: No effect on RNA binding.
- S778 (= S788) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R790) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
49% identity, 99% coverage: 10:903/906 of query aligns to 12:886/888 of 2b3xA
- active site: D124 (= D123), H125 (= H124), D204 (= D203), R535 (= R543), S777 (= S788), R779 (= R790)
- binding iron/sulfur cluster: I175 (= I174), H206 (= H205), C436 (= C444), C502 (= C510), C505 (= C513), I506 (= I514), N534 (= N542)
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)
50% identity, 98% coverage: 15:903/906 of query aligns to 111:987/990 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)
48% identity, 98% coverage: 15:903/906 of query aligns to 17:848/850 of 3snpA
- active site: D124 (= D123), H125 (= H124), D186 (= D203), R505 (= R543), S739 (= S788), R741 (= R790)
- binding : H125 (= H124), S126 (= S125), H188 (= H205), L243 (= L260), R250 (= R267), N279 (= N296), E283 (= E300), S352 (≠ A366), P357 (= P371), K360 (≠ R374), T419 (= T445), N420 (= N446), T421 (= T447), N504 (= N542), R505 (= R543), L520 (= L558), S642 (= S688), P643 (= P689), A644 (= A690), G645 (≠ S691), N646 (≠ A692), R649 (≠ V695), R665 (≠ K711), S669 (= S715), G671 (= G717), R674 (= R720), R741 (= R790)
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)
27% identity, 87% coverage: 74:863/906 of query aligns to 85:739/778 of P19414
- R604 (≠ Q706) 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)
28% identity, 86% coverage: 71:846/906 of query aligns to 58:699/753 of 8acnA
- active site: D99 (= D123), H100 (= H124), D164 (= D203), R446 (= R543), S641 (= S788), R643 (= R790)
- binding nitroisocitric acid: Q71 (= Q84), T74 (= T87), H100 (= H124), D164 (= D203), S165 (= S204), R446 (= R543), R451 (= R548), R579 (≠ N714), S641 (= S788), S642 (= S789), R643 (= R790)
- binding iron/sulfur cluster: H100 (= H124), D164 (= D203), H166 (= H205), S356 (= S443), C357 (= C444), C420 (= C510), C423 (= C513), I424 (= I514)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 86% coverage: 71:846/906 of query aligns to 58:699/753 of 1fghA
- active site: D99 (= D123), H100 (= H124), D164 (= D203), R446 (= R543), S641 (= S788), R643 (= R790)
- binding 4-hydroxy-aconitate ion: Q71 (= Q84), T74 (= T87), H100 (= H124), D164 (= D203), S165 (= S204), R446 (= R543), R451 (= R548), R579 (≠ N714), S641 (= S788), S642 (= S789), R643 (= R790)
- binding iron/sulfur cluster: H100 (= H124), D164 (= D203), H166 (= H205), S356 (= S443), C357 (= C444), C420 (= C510), C423 (= C513), I424 (= I514), R451 (= R548)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 86% coverage: 71:846/906 of query aligns to 58:699/753 of 1amjA
- active site: D99 (= D123), H100 (= H124), D164 (= D203), R446 (= R543), S641 (= S788), R643 (= R790)
- binding iron/sulfur cluster: I144 (= I174), H166 (= H205), C357 (= C444), C420 (= C510), C423 (= C513)
- binding sulfate ion: Q71 (= Q84), R579 (≠ N714), R643 (= R790)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 86% coverage: 71:846/906 of query aligns to 58:699/753 of 1amiA
- active site: D99 (= D123), H100 (= H124), D164 (= D203), R446 (= R543), S641 (= S788), R643 (= R790)
- binding alpha-methylisocitric acid: Q71 (= Q84), T74 (= T87), H100 (= H124), D164 (= D203), S165 (= S204), R446 (= R543), R451 (= R548), R579 (≠ N714), S641 (= S788), S642 (= S789), R643 (= R790)
- binding iron/sulfur cluster: H100 (= H124), I144 (= I174), D164 (= D203), H166 (= H205), S356 (= S443), C357 (= C444), C420 (= C510), C423 (= C513), N445 (= N542)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 86% coverage: 71:846/906 of query aligns to 58:699/753 of 1acoA
- active site: D99 (= D123), H100 (= H124), D164 (= D203), R446 (= R543), S641 (= S788), R643 (= R790)
- binding iron/sulfur cluster: H100 (= H124), I144 (= I174), D164 (= D203), H166 (= H205), S356 (= S443), C357 (= C444), C420 (= C510), C423 (= C513), N445 (= N542)
- binding aconitate ion: Q71 (= Q84), D164 (= D203), S165 (= S204), R446 (= R543), R451 (= R548), R579 (≠ N714), S641 (= S788), S642 (= S789), R643 (= R790)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
28% identity, 86% coverage: 71:846/906 of query aligns to 59:700/754 of 5acnA
- active site: D100 (= D123), H101 (= H124), D165 (= D203), R447 (= R543), S642 (= S788), R644 (= R790)
- binding fe3-s4 cluster: I145 (= I174), H147 (= H176), H167 (= H205), C358 (= C444), C421 (= C510), C424 (= C513), N446 (= N542)
- binding tricarballylic acid: K198 (≠ L236), G235 (= G273), R666 (= R812)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 88% coverage: 71:864/906 of query aligns to 86:743/780 of P20004
- Q99 (= Q84) binding substrate
- DSH 192:194 (= DSH 203:205) binding substrate
- C385 (= C444) binding [4Fe-4S] cluster
- C448 (= C510) binding [4Fe-4S] cluster
- C451 (= C513) binding [4Fe-4S] cluster
- R474 (= R543) binding substrate
- R479 (= R548) binding substrate
- R607 (≠ N714) binding substrate
- SR 670:671 (= SR 789:790) binding substrate
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 86% coverage: 71:846/906 of query aligns to 58:699/753 of 1nisA
- active site: D99 (= D123), H100 (= H124), D164 (= D203), R446 (= R543), S641 (= S788), R643 (= R790)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q84), H100 (= H124), D164 (= D203), S165 (= S204), R446 (= R543), R451 (= R548), R579 (≠ N714), S641 (= S788), S642 (= S789)
- binding iron/sulfur cluster: H100 (= H124), I144 (= I174), H166 (= H205), S356 (= S443), C357 (= C444), C420 (= C510), C423 (= C513)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 89% coverage: 23:828/906 of query aligns to 44:711/789 of P39533
- K610 (≠ R720) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 86% coverage: 71:846/906 of query aligns to 86:727/781 of P16276
- Q99 (= Q84) binding substrate
- DSH 192:194 (= DSH 203:205) binding substrate
- C385 (= C444) binding [4Fe-4S] cluster
- C448 (= C510) binding [4Fe-4S] cluster
- C451 (= C513) binding [4Fe-4S] cluster
- R474 (= R543) binding substrate
- R479 (= R548) binding substrate
- R607 (≠ N714) binding substrate
- SR 670:671 (= SR 789:790) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
28% identity, 86% coverage: 71:846/906 of query aligns to 58:699/753 of 1b0kA
- active site: D99 (= D123), H100 (= H124), D164 (= D203), R446 (= R543), A641 (≠ S788), R643 (= R790)
- binding citrate anion: Q71 (= Q84), H100 (= H124), D164 (= D203), S165 (= S204), R446 (= R543), R451 (= R548), R579 (≠ N714), A641 (≠ S788), S642 (= S789), R643 (= R790)
- binding oxygen atom: D164 (= D203), H166 (= H205)
- binding iron/sulfur cluster: H100 (= H124), D164 (= D203), H166 (= H205), S356 (= S443), C357 (= C444), C420 (= C510), C423 (= C513)
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)
23% identity, 78% coverage: 123:829/906 of query aligns to 78:658/758 of O14289
- S486 (≠ K589) modified: Phosphoserine
- S488 (≠ I591) modified: Phosphoserine
Query Sequence
>WP_025274291.1 NCBI__GCF_000527155.1:WP_025274291.1
MSKDSFQARDTLSVGGEDFDIYRIDKVDGHDRLPYSFKVLLENLLRTEDGANITADHIRA
LGSWDPKSKPSTEIQFTPARVIMQDFTGVPCIVDLATMREAVRDLGGDPDQINPLAPAEM
VIDHSVVVDFFGQADSFKRNVEREYERNRERYQFLRWGQTAFNEFKVVPPGTGIVHQVNI
EHLARVIMTRNGTAYPDTCVGTDSHTTMENGIGVLGWGVGGIEAEAAMLGQPISMLIPRV
LGFKLTGDLPPGATATDLVLTITEMLREHGVVGKFVEFYGHGVASVPVADRSTLGNMSPE
FGSTCAIFPIDERTTDYLRLTGRDEEHIELVEAYAKAQGLWHDPNHEAEYSEYLELDLST
VVPSIAGPKRPQDRIQLDKADHQWRRDVVNYVEDEAERESFPASDSPAEKGNGDRPHNPQ
TVSSDTGEYQLDHGDVVIAAITSCTNTSNPYVMVGAGLLAKNAVDAGLTTKPWVKTSLAP
GSQVVTGYLKRAGLDAYLDKLGFNLVGYGCTTCIGNSGPLPEEISEAVNAGDLAVTSVLS
GNRNFEGRINPDVKMNYLASPPLVVAYALAGSMDVNITTQPMGQSADGKDIFLSDIWPSP
ESIRDVVDGNIGREMFLDEYSNVFEGDDTWKSLPVPTGNTFDWEENSTYVRKAPYFDGMP
ETPEPVENIEGARLLAKLGDSVTTDHISPASAIKVNSPAGEYLKSQGVSIKDFNSYGSRR
GNHEVMVRGTFANIRLRNQLAPGTEGGWTRDFTQDDAPVTTIYDAAQNYAAENIPLVVMA
GKEYGTGSSRDWAAKGTRLLGVKAVIAESYERIHRSNLIGMGVLPLQFPEGESHSSLGLT
GEETISITGMDQLNDSIPETVRVSAVDASGAETTFDAVVRLDTPGEAAYYRNGGILAYVL
RGLLNK
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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