SitesBLAST
Comparing WP_011386009.1 NCBI__GCF_000009985.1:WP_011386009.1 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)
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, 98% coverage: 18:900/903 of query aligns to 24:906/909 of P09339
- C450 (= C438) 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 (= R728) 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)
52% identity, 98% coverage: 15:899/903 of query aligns to 110:987/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
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)
49% identity, 100% coverage: 4:902/903 of query aligns to 12:941/943 of A0QX20
- K394 (vs. gap) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
50% identity, 97% coverage: 28:899/903 of query aligns to 24:887/889 of P21399
- C300 (≠ A304) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ R322) to M: in dbSNP:rs150373174
- C437 (= C438) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C504) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C507) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R537) mutation to Q: Strongly reduced RNA binding.
- R541 (= R542) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ H699) mutation to K: No effect on RNA binding.
- S778 (= S785) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R787) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
50% identity, 97% coverage: 28:899/903 of query aligns to 23:886/888 of 2b3xA
- active site: D124 (= D129), H125 (= H130), D204 (= D209), R535 (= R537), S777 (= S785), R779 (= R787)
- binding iron/sulfur cluster: I175 (= I180), H206 (= H211), C436 (= C438), C502 (= C504), C505 (= C507), I506 (= I508), N534 (= N536)
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
48% identity, 97% coverage: 20:899/903 of query aligns to 18:848/850 of 3snpA
- active site: D124 (= D129), H125 (= H130), D186 (= D209), R505 (= R537), S739 (= S785), R741 (= R787)
- binding : H125 (= H130), S126 (= S131), H188 (= H211), L243 (= L266), R250 (= R273), N279 (= N302), E283 (= E306), S352 (≠ A373), P357 (= P378), K360 (≠ R381), T419 (= T439), N420 (= N440), T421 (= T441), N504 (= N536), R505 (= R537), L520 (= L552), S642 (= S681), P643 (= P682), A644 (= A683), G645 (= G684), N646 (≠ S685), R649 (≠ V688), R665 (≠ G704), S669 (= S708), G671 (= G710), R674 (= R713), R741 (= R787)
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)
28% identity, 86% coverage: 123:898/903 of query aligns to 117:775/778 of P19414
- R604 (= R721) 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)
29% identity, 82% coverage: 86:827/903 of query aligns to 68:684/754 of 5acnA
- active site: D100 (= D129), H101 (= H130), D165 (= D209), R447 (= R537), S642 (= S785), R644 (= R787)
- binding fe3-s4 cluster: I145 (= I180), H147 (= H182), H167 (= H211), C358 (= C438), C421 (= C504), C424 (= C507), N446 (= N536)
- binding tricarballylic acid: K198 (≠ L242), G235 (= G279), R666 (= R809)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
29% identity, 82% coverage: 86:827/903 of query aligns to 95:711/781 of P16276
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
28% identity, 82% coverage: 86:827/903 of query aligns to 67:683/753 of 8acnA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R537), S641 (= S785), R643 (= R787)
- binding nitroisocitric acid: Q71 (= Q90), T74 (= T93), H100 (= H130), D164 (= D209), S165 (= S210), R446 (= R537), R451 (= R542), R579 (= R721), S641 (= S785), S642 (= S786), R643 (= R787)
- binding iron/sulfur cluster: H100 (= H130), D164 (= D209), H166 (= H211), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507), I424 (= I508)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 82% coverage: 86:827/903 of query aligns to 67:683/753 of 1fghA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R537), S641 (= S785), R643 (= R787)
- binding 4-hydroxy-aconitate ion: Q71 (= Q90), T74 (= T93), H100 (= H130), D164 (= D209), S165 (= S210), R446 (= R537), R451 (= R542), R579 (= R721), S641 (= S785), S642 (= S786), R643 (= R787)
- binding iron/sulfur cluster: H100 (= H130), D164 (= D209), H166 (= H211), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507), I424 (= I508), R451 (= R542)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
29% identity, 82% coverage: 86:827/903 of query aligns to 67:683/753 of 1b0kA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R537), A641 (≠ S785), R643 (= R787)
- binding citrate anion: Q71 (= Q90), H100 (= H130), D164 (= D209), S165 (= S210), R446 (= R537), R451 (= R542), R579 (= R721), A641 (≠ S785), S642 (= S786), R643 (= R787)
- binding oxygen atom: D164 (= D209), H166 (= H211)
- binding iron/sulfur cluster: H100 (= H130), D164 (= D209), H166 (= H211), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 82% coverage: 86:827/903 of query aligns to 67:683/753 of 1amjA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R537), S641 (= S785), R643 (= R787)
- binding iron/sulfur cluster: I144 (= I180), H166 (= H211), C357 (= C438), C420 (= C504), C423 (= C507)
- binding sulfate ion: Q71 (= Q90), R579 (= R721), R643 (= R787)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 82% coverage: 86:827/903 of query aligns to 67:683/753 of 1amiA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R537), S641 (= S785), R643 (= R787)
- binding alpha-methylisocitric acid: Q71 (= Q90), T74 (= T93), H100 (= H130), D164 (= D209), S165 (= S210), R446 (= R537), R451 (= R542), R579 (= R721), S641 (= S785), S642 (= S786), R643 (= R787)
- binding iron/sulfur cluster: H100 (= H130), I144 (= I180), D164 (= D209), H166 (= H211), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507), N445 (= N536)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 82% coverage: 86:827/903 of query aligns to 67:683/753 of 1acoA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R537), S641 (= S785), R643 (= R787)
- binding iron/sulfur cluster: H100 (= H130), I144 (= I180), D164 (= D209), H166 (= H211), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507), N445 (= N536)
- binding aconitate ion: Q71 (= Q90), D164 (= D209), S165 (= S210), R446 (= R537), R451 (= R542), R579 (= R721), S641 (= S785), S642 (= S786), R643 (= R787)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 82% coverage: 86:827/903 of query aligns to 67:683/753 of 1nisA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R537), S641 (= S785), R643 (= R787)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q90), H100 (= H130), D164 (= D209), S165 (= S210), R446 (= R537), R451 (= R542), R579 (= R721), S641 (= S785), S642 (= S786)
- binding iron/sulfur cluster: H100 (= H130), I144 (= I180), H166 (= H211), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
29% identity, 82% coverage: 86:827/903 of query aligns to 95:711/780 of P20004
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 78% coverage: 122:825/903 of query aligns to 117:711/789 of P39533
- K610 (≠ R721) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
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, 48% coverage: 179:608/903 of query aligns to 118:520/758 of O14289
- S486 (≠ K583) modified: Phosphoserine
- S488 (≠ V585) modified: Phosphoserine
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
24% identity, 53% coverage: 88:567/903 of query aligns to 32:417/423 of 4kp1A
- active site: D64 (= D129), H65 (= H130), D121 (= D209), R387 (= R537)
- binding 2,4-dimethylpentane-2,4-diol: F299 (≠ A434), S302 (= S437), S383 (≠ L533), F389 (= F539)
- binding magnesium ion: C303 (= C438), T304 (= T439), R387 (= R537)
Query Sequence
>WP_011386009.1 NCBI__GCF_000009985.1:WP_011386009.1
MLPDPFGALRDLSLGHERLSRYYALAALDAVTDGPVSRLPVSIRIVLESVLRNCDGKRIT
EEHVRQLANWRPDAPRTQEIPFVVARIVLQDFTGVPLLCDLAAMRGVAQAFGKNPKIIEP
LVPVDLVVDHSVQVDHYGEADSLDLNMRREFQRNAERYRFIKWGMQAFDTFRVVPPGIGI
VHQVNLEFLARGVLEKDGITYPDTLVGTDSHTTMINALGVAGWGVGGIEAEAGMLGQPLV
FLTPDVVGVHLHGRLPEGATATDLVLFLTERLRRAKVVGKFVEFFGEGTRSLAVPDRATI
ANMAPEYGATMGFFPVDKETVRYLEATGRTDSEIEVFRAYYSAQGLFGMPMPGDIDYSEV
IEFDLGSVQPSIAGPKRPQDRLNLSDMRRAFTSLFSAPAKDDGYGRPAEALGRRHRVETT
AAADIGHGDVLIAAITSCTNTSNPGVMLAAGLLARKAVALGLKVGPRVKTSLAPGSRVVT
EYLAKAGLLGDLESLGFGVVAYGCTTCIGNSGPLMPDLEQAIAADDLVCAAVLSGNRNFE
ARIHPAIKANFLMSPPLVVAFAIAGRIAIDMTQEPLGTGKDGKPVMLKDIWPSGREVADA
LLVATDPELYRRLYSDFVHGNPLWNDIPTQTGPAYAWETSTYIAEPPFFERFSPQPAGVG
DIIGARALAIFGDSVTTDHISPAGSIAVSSPAGQYLLAHGVAAGDFNSYGARRGNHEVMM
RGTFANVRIRNLMLPAKVDGSRVEGGLTLHQPEGSEMPIFDAASRYQEAGIPSIVFAGTE
YGTGSSRDWAAKGPKLLGVRAVVAQSFERIHRSNLVGMGVLPLQFRDGESAASLGIAGDE
EFHVRGLSGVLRPRQEVVLEIVNRQGRSRAISLQLRVDTAIELDYLSHGGILPYVLRDLL
AAG
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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