SitesBLAST
Comparing GFF3491 FitnessBrowser__Marino:GFF3491 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)
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)
57% identity, 100% coverage: 1:919/919 of query aligns to 1:942/943 of A0QX20
- K394 (≠ L399) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
59% identity, 99% coverage: 6:917/919 of query aligns to 1:930/931 of D9X0I3
- SVIAD 125:129 (≠ SVMVD 134:138) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C526) 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 (= R750) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ E754) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
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)
54% identity, 100% coverage: 1:919/919 of query aligns to 1:909/909 of P09339
- M1 (= M1) modified: Initiator methionine, Removed
- C450 (= C460) 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 (= R750) 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.
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)
53% identity, 100% coverage: 1:915/919 of query aligns to 93:987/990 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)
52% identity, 97% coverage: 26:917/919 of query aligns to 21:889/889 of P21399
- C300 (≠ A311) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ K329) to M: in dbSNP:rs150373174
- C437 (= C460) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C526) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C529) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R559) mutation to Q: Strongly reduced RNA binding.
- R541 (= R564) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ H721) mutation to K: No effect on RNA binding.
- S778 (= S801) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R803) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
52% identity, 97% coverage: 26:917/919 of query aligns to 20:888/888 of 2b3xA
- active site: D124 (= D132), H125 (= H133), D204 (= D216), R535 (= R559), S777 (= S801), R779 (= R803)
- binding iron/sulfur cluster: I175 (= I183), H206 (= H218), C436 (= C460), C502 (= C526), C505 (= C529), I506 (= I530), N534 (= N558)
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
51% identity, 95% coverage: 41:917/919 of query aligns to 33:850/850 of 3snpA
- active site: D124 (= D132), H125 (= H133), D186 (= D216), R505 (= R559), S739 (= S801), R741 (= R803)
- binding : H125 (= H133), S126 (= S134), H188 (= H218), L243 (= L273), R250 (= R280), N279 (= N309), E283 (= E313), S352 (≠ A379), P357 (= P384), K360 (≠ R387), T419 (= T461), N420 (= N462), T421 (= T463), N504 (= N558), R505 (= R559), L520 (= L574), S642 (= S703), P643 (= P704), A644 (= A705), G645 (= G706), N646 (≠ S707), R649 (≠ P710), R665 (≠ K726), S669 (= S730), G671 (= G732), R674 (= R735), R741 (= R803)
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, 90% coverage: 83:911/919 of query aligns to 85:772/778 of P19414
- R604 (= R743) 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)
27% identity, 90% coverage: 81:909/919 of query aligns to 60:746/754 of 5acnA
- active site: D100 (= D132), H101 (= H133), D165 (= D216), R447 (= R559), S642 (= S801), R644 (= R803)
- binding fe3-s4 cluster: I145 (= I183), H147 (= H185), H167 (= H218), C358 (= C460), C421 (= C526), C424 (= C529), N446 (= N558)
- binding tricarballylic acid: K198 (≠ L249), G235 (= G286), R666 (= R825)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
27% identity, 90% coverage: 81:909/919 of query aligns to 87:773/781 of P16276
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
27% identity, 90% coverage: 81:909/919 of query aligns to 59:745/753 of 1b0kA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R559), A641 (≠ S801), R643 (= R803)
- binding citrate anion: Q71 (= Q93), H100 (= H133), D164 (= D216), S165 (= S217), R446 (= R559), R451 (= R564), R579 (≠ N729), A641 (≠ S801), S642 (= S802), R643 (= R803)
- binding oxygen atom: D164 (= D216), H166 (= H218)
- binding iron/sulfur cluster: H100 (= H133), D164 (= D216), H166 (= H218), S356 (= S459), C357 (= C460), C420 (= C526), C423 (= C529)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 90% coverage: 81:909/919 of query aligns to 87:773/780 of P20004
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
27% identity, 90% coverage: 81:909/919 of query aligns to 59:745/753 of 8acnA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R559), S641 (= S801), R643 (= R803)
- binding nitroisocitric acid: Q71 (= Q93), T74 (= T96), H100 (= H133), D164 (= D216), S165 (= S217), R446 (= R559), R451 (= R564), R579 (= R743), S641 (= S801), S642 (= S802), R643 (= R803)
- binding iron/sulfur cluster: H100 (= H133), D164 (= D216), H166 (= H218), S356 (= S459), C357 (= C460), C420 (= C526), C423 (= C529), I424 (= I530)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
27% identity, 90% coverage: 81:909/919 of query aligns to 59:745/753 of 1fghA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R559), S641 (= S801), R643 (= R803)
- binding 4-hydroxy-aconitate ion: Q71 (= Q93), T74 (= T96), H100 (= H133), D164 (= D216), S165 (= S217), R446 (= R559), R451 (= R564), R579 (= R743), S641 (= S801), S642 (= S802), R643 (= R803)
- binding iron/sulfur cluster: H100 (= H133), D164 (= D216), H166 (= H218), S356 (= S459), C357 (= C460), C420 (= C526), C423 (= C529), I424 (= I530), R451 (= R564)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
27% identity, 90% coverage: 81:909/919 of query aligns to 59:745/753 of 1amjA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R559), S641 (= S801), R643 (= R803)
- binding iron/sulfur cluster: I144 (= I183), H166 (= H218), C357 (= C460), C420 (= C526), C423 (= C529)
- binding sulfate ion: Q71 (= Q93), R579 (= R743), R643 (= R803)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
27% identity, 90% coverage: 81:909/919 of query aligns to 59:745/753 of 1amiA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R559), S641 (= S801), R643 (= R803)
- binding alpha-methylisocitric acid: Q71 (= Q93), T74 (= T96), H100 (= H133), D164 (= D216), S165 (= S217), R446 (= R559), R451 (= R564), R579 (= R743), S641 (= S801), S642 (= S802), R643 (= R803)
- binding iron/sulfur cluster: H100 (= H133), I144 (= I183), D164 (= D216), H166 (= H218), S356 (= S459), C357 (= C460), C420 (= C526), C423 (= C529), N445 (= N558)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
27% identity, 90% coverage: 81:909/919 of query aligns to 59:745/753 of 1acoA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R559), S641 (= S801), R643 (= R803)
- binding iron/sulfur cluster: H100 (= H133), I144 (= I183), D164 (= D216), H166 (= H218), S356 (= S459), C357 (= C460), C420 (= C526), C423 (= C529), N445 (= N558)
- binding aconitate ion: Q71 (= Q93), D164 (= D216), S165 (= S217), R446 (= R559), R451 (= R564), R579 (= R743), S641 (= S801), S642 (= S802), R643 (= R803)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 95% coverage: 40:911/919 of query aligns to 50:782/789 of P39533
- K610 (≠ R735) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
27% identity, 90% coverage: 81:909/919 of query aligns to 59:745/753 of 1nisA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R559), S641 (= S801), R643 (= R803)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q93), H100 (= H133), D164 (= D216), S165 (= S217), R446 (= R559), R451 (= R564), R579 (= R743), S641 (= S801), S642 (= S802)
- binding iron/sulfur cluster: H100 (= H133), I144 (= I183), H166 (= H218), S356 (= S459), C357 (= C460), C420 (= C526), C423 (= C529)
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, 44% coverage: 211:611/919 of query aligns to 135:492/758 of O14289
- S486 (≠ N605) modified: Phosphoserine
- S488 (≠ V607) modified: Phosphoserine
Query Sequence
>GFF3491 FitnessBrowser__Marino:GFF3491
MSNESLSKDSLNTLSSLDAGGKTFHYYSLPKAADTLGDLNRLPFSLKVLMENLLRNEDGT
TVDRSHIDAMVQWMKDRHSDTEIQFRPARVLMQDFTGVPGVVDLAAMREAVQAAGKDPAM
INPLSPVDLVIDHSVMVDKFGDASSFKDNVAIEMERNQERYEFLRWGQQAFDNFRVVPPG
TGICHQVNLEYLGKTVWQKDQDGKTIAYPDTLVGTDSHTTMINGLGILGWGVGGIEAEAA
MLGQPVSMLIPEVVGFKITGKLREGITATDLVLTVTEMLRKKGVVGKFVEFYGDGLKDMP
VADRATIANMAPEYGATCGFFPVDEQTIKYMRLTGREEEQLELVEAYAKAQGLWREPGHE
PVYTDNLELDMGEVEASLAGPKRPQDRVALKNMKSSFELLMETAEGPAENREANLESEGG
QTAVGVDDSYKHHASQPLEMNGEKSRLDPGAVVIAAITSCTNTSNPSVMMAAGLIAQKAV
QKGLSTKPWVKTSLAPGSKVVTDYLKVGGFQDDLDKLGFNLVGYGCTTCIGNSGPLPDAV
EKAISDGDLTVASVLSGNRNFEGRVHPLVKTNWLASPPLVVAYALAGNVRLDLSQDPLGN
DKDGNPVYLKDLWPSQQEIAEAVEKVKTDMFRKEYAEVFDGDATWKSIKVPESKVYEWSD
KSTYIQHPPFFEGLKEEPDAIDDIKDANILALLGDSVTTDHISPAGSFKPDTPAGKYLQE
HGVEPKDFNSYGSRRGNHEVMMRGTFANVRIRNEMLDGVEGGYTKFVPTGEQMAIYDAAM
KYQEKGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVVAESYERIHRSNLIGMGVMPLQ
FPEGTDRKSLKLTGEETISIEGLSGEIKPGQTLKMTVKYKDGSTETCELKSRIDTANEAV
YFKHGGILHYVVREMLRTA
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