SitesBLAST
Comparing WP_014146819.1 NCBI__GCF_000968535.2:WP_014146819.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
57% identity, 99% coverage: 3:895/899 of query aligns to 9:904/909 of P09339
- C450 (= C441) 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 (= R732) 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
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)
56% identity, 100% coverage: 1:896/899 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)
54% identity, 97% coverage: 22:896/899 of query aligns to 20:887/889 of P21399
- C300 (≠ A306) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ N324) to M: in dbSNP:rs150373174
- C437 (= C441) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C507) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C510) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R540) mutation to Q: Strongly reduced RNA binding.
- R541 (= R545) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ K703) mutation to K: No effect on RNA binding.
- S778 (= S783) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R785) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
54% identity, 97% coverage: 22:896/899 of query aligns to 19:886/888 of 2b3xA
- active site: D124 (= D129), H125 (= H130), D204 (= D211), R535 (= R540), S777 (= S783), R779 (= R785)
- binding iron/sulfur cluster: I175 (= I180), H206 (= H213), C436 (= C441), C502 (= C507), C505 (= C510), I506 (= I511), N534 (= N539)
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)
53% identity, 100% coverage: 2:896/899 of query aligns to 9:938/943 of A0QX20
- K394 (≠ Q395) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
53% identity, 95% coverage: 39:896/899 of query aligns to 33:848/850 of 3snpA
- active site: D124 (= D129), H125 (= H130), D186 (= D211), R505 (= R540), S739 (= S783), R741 (= R785)
- binding : H125 (= H130), S126 (= S131), H188 (= H213), L243 (= L268), R250 (= R275), N279 (= N304), E283 (= E308), S352 (≠ A375), P357 (= P380), K360 (≠ R383), T419 (= T442), N420 (= N443), T421 (= T444), N504 (= N539), R505 (= R540), L520 (= L555), S642 (= S685), P643 (= P686), A644 (= A687), G645 (= G688), N646 (≠ Q689), R649 (≠ P692), R665 (≠ K708), S669 (= S712), G671 (= G714), R674 (= R717), R741 (= R785)
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, 84% coverage: 72:825/899 of query aligns to 74:708/778 of P19414
- R604 (= R717) 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)
26% identity, 91% coverage: 77:892/899 of query aligns to 83:782/789 of P39533
- K610 (≠ R725) 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)
26% identity, 90% coverage: 83:889/899 of query aligns to 65:745/754 of 5acnA
- active site: D100 (= D129), H101 (= H130), D165 (= D211), R447 (= R540), S642 (= S783), R644 (= R785)
- binding fe3-s4 cluster: I145 (= I180), H147 (= H182), H167 (= H213), C358 (= C441), C421 (= C507), C424 (= C510), N446 (= N539)
- binding tricarballylic acid: K198 (≠ L244), G235 (= G281), R666 (= R807)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
26% identity, 90% coverage: 83:889/899 of query aligns to 92:772/781 of P16276
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
26% identity, 90% coverage: 83:889/899 of query aligns to 64:744/753 of 1b0kA
- active site: D99 (= D129), H100 (= H130), D164 (= D211), R446 (= R540), A641 (≠ S783), R643 (= R785)
- binding citrate anion: Q71 (= Q90), H100 (= H130), D164 (= D211), S165 (= S212), R446 (= R540), R451 (= R545), R579 (= R725), A641 (≠ S783), S642 (= S784), R643 (= R785)
- binding oxygen atom: D164 (= D211), H166 (= H213)
- binding iron/sulfur cluster: H100 (= H130), D164 (= D211), H166 (= H213), S356 (= S440), C357 (= C441), C420 (= C507), C423 (= C510)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
26% identity, 90% coverage: 83:889/899 of query aligns to 92:772/780 of P20004
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
26% identity, 90% coverage: 83:889/899 of query aligns to 64:744/753 of 8acnA
- active site: D99 (= D129), H100 (= H130), D164 (= D211), R446 (= R540), S641 (= S783), R643 (= R785)
- binding nitroisocitric acid: Q71 (= Q90), T74 (= T93), H100 (= H130), D164 (= D211), S165 (= S212), R446 (= R540), R451 (= R545), R579 (= R725), S641 (= S783), S642 (= S784), R643 (= R785)
- binding iron/sulfur cluster: H100 (= H130), D164 (= D211), H166 (= H213), S356 (= S440), C357 (= C441), C420 (= C507), C423 (= C510), I424 (= I511)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
26% identity, 90% coverage: 83:889/899 of query aligns to 64:744/753 of 1fghA
- active site: D99 (= D129), H100 (= H130), D164 (= D211), R446 (= R540), S641 (= S783), R643 (= R785)
- binding 4-hydroxy-aconitate ion: Q71 (= Q90), T74 (= T93), H100 (= H130), D164 (= D211), S165 (= S212), R446 (= R540), R451 (= R545), R579 (= R725), S641 (= S783), S642 (= S784), R643 (= R785)
- binding iron/sulfur cluster: H100 (= H130), D164 (= D211), H166 (= H213), S356 (= S440), C357 (= C441), C420 (= C507), C423 (= C510), I424 (= I511), R451 (= R545)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
26% identity, 90% coverage: 83:889/899 of query aligns to 64:744/753 of 1amjA
- active site: D99 (= D129), H100 (= H130), D164 (= D211), R446 (= R540), S641 (= S783), R643 (= R785)
- binding iron/sulfur cluster: I144 (= I180), H166 (= H213), C357 (= C441), C420 (= C507), C423 (= C510)
- binding sulfate ion: Q71 (= Q90), R579 (= R725), R643 (= R785)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
26% identity, 90% coverage: 83:889/899 of query aligns to 64:744/753 of 1amiA
- active site: D99 (= D129), H100 (= H130), D164 (= D211), R446 (= R540), S641 (= S783), R643 (= R785)
- binding alpha-methylisocitric acid: Q71 (= Q90), T74 (= T93), H100 (= H130), D164 (= D211), S165 (= S212), R446 (= R540), R451 (= R545), R579 (= R725), S641 (= S783), S642 (= S784), R643 (= R785)
- binding iron/sulfur cluster: H100 (= H130), I144 (= I180), D164 (= D211), H166 (= H213), S356 (= S440), C357 (= C441), C420 (= C507), C423 (= C510), N445 (= N539)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
26% identity, 90% coverage: 83:889/899 of query aligns to 64:744/753 of 1acoA
- active site: D99 (= D129), H100 (= H130), D164 (= D211), R446 (= R540), S641 (= S783), R643 (= R785)
- binding iron/sulfur cluster: H100 (= H130), I144 (= I180), D164 (= D211), H166 (= H213), S356 (= S440), C357 (= C441), C420 (= C507), C423 (= C510), N445 (= N539)
- binding aconitate ion: Q71 (= Q90), D164 (= D211), S165 (= S212), R446 (= R540), R451 (= R545), R579 (= R725), S641 (= S783), S642 (= S784), R643 (= R785)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
26% identity, 90% coverage: 83:889/899 of query aligns to 64:744/753 of 1nisA
- active site: D99 (= D129), H100 (= H130), D164 (= D211), R446 (= R540), S641 (= S783), R643 (= R785)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q90), H100 (= H130), D164 (= D211), S165 (= S212), R446 (= R540), R451 (= R545), R579 (= R725), S641 (= S783), S642 (= S784)
- binding iron/sulfur cluster: H100 (= H130), I144 (= I180), H166 (= H213), S356 (= S440), C357 (= C441), C420 (= C507), C423 (= C510)
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, 43% coverage: 206:590/899 of query aligns to 135:490/758 of O14289
- S486 (≠ D586) modified: Phosphoserine
- S488 (≠ V588) modified: Phosphoserine
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
24% identity, 50% coverage: 126:571/899 of query aligns to 61:418/423 of 4kp1A
- active site: D64 (= D129), H65 (= H130), D121 (= D211), R387 (= R540)
- binding 2,4-dimethylpentane-2,4-diol: F299 (≠ L397), S302 (= S440), S383 (≠ E522), F389 (= F542)
- binding magnesium ion: C303 (= C441), T304 (= T442), R387 (= R540)
Query Sequence
>WP_014146819.1 NCBI__GCF_000968535.2:WP_014146819.1
MNSKDPFGARQLLNPDRASPLSYYRLACLESAGAADLARLPHTIKILLESLLRNCDGYSI
TEDHVLGLAAWQAQGSRREIPYKPARVILQDFTGVPALVDLAAMRDAMNELGGDPKKINP
FIPCDLVIDHSVQVDYFGKANALPMNEAVEFQRNQERYEFLKWGQSAFQNLRVVPPSTGI
VHQVNLEYLAQVVFHNKNSDLCYPDSCVGTDSHTPMVNGLGVLAWGVGGIEAEAVILDQP
IYMLEPDVVGIKLTGKLPPGVTATDLVLRITELCRQFGVVGQFVEFYGSGLSQLSIPDRA
TISNMAPEQGSTVSFFPVDKAALNYMRLTGRSPEQIELTERYAKLQGLFRTDDAPEPEFT
RTLEVDLGEIEPALAGPKRPQDRIPLSQVGPTYRQTLIAPVGIRGMGLAESDLDRCGVVS
NKGACETITHGAVVIAAITSCTNTSNPSVMLGAGLVAKKAVEKGLKVKNYVKTSLAPGSQ
VVTEYLKQSGLLPYLEALGFYLVGYGCTTCIGNSGPLDVAVEEAIVDNDLVVSAVLSGNR
NFEGRVHPLTKTNYLASPPLVVAYALAGSTVVDMTREAIGQGSDGDPVFLRDIWPTTEEI
DDVVQKFVTPEMFRERYADVFTGTQAWQAIAVAGSERYQWNEQSTYIRKPPFFEGLGGGP
ETIGRLADMRVLALFGDSVTTDHISPAGQIAPDSPAALYLLEKGVERKDWNSYGSRRGND
QVMCRGTFANVRIHNLLVPGAEGNVTIHHPSGERMTFFDAAMKYKESGMPLCILAGKEYG
SGSSRDWAAKGPFMQGVKAVIAESYERIHRSNLIGMGILPLQFMSGESAQSLGLKGDETV
TVDIADDTVPQQVVDVTASAPDGSVTAFKAVSRIDTPIEIQYYRDGGILRTVLKKLRAG
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