SitesBLAST
Comparing WP_011814195.1 NCBI__GCF_000015585.1:WP_011814195.1 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)
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)
58% identity, 99% coverage: 3:910/914 of query aligns to 12:938/943 of A0QX20
- K394 (≠ Q393) 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: 3:910/914 of query aligns to 4:928/931 of D9X0I3
- SVIAD 125:129 (≠ SVMVD 127:131) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C524) 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 (= R748) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ K752) 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)
56% identity, 99% coverage: 3:908/914 of query aligns to 11:903/909 of P09339
- C450 (= C458) 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 (= R748) 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)
54% identity, 98% coverage: 15:911/914 of query aligns to 115:988/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
53% identity, 99% coverage: 11:911/914 of query aligns to 14:887/888 of 2b3xA
- active site: D124 (= D125), H125 (= H126), D204 (= D209), R535 (= R557), S777 (= S799), R779 (= R801)
- binding iron/sulfur cluster: I175 (= I176), H206 (= H211), C436 (= C458), C502 (= C524), C505 (= C527), I506 (= I528), N534 (= N556)
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)
53% identity, 99% coverage: 11:911/914 of query aligns to 15:888/889 of P21399
- C300 (≠ A304) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ A322) to M: in dbSNP:rs150373174
- C437 (= C458) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C524) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C527) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R557) mutation to Q: Strongly reduced RNA binding.
- R541 (= R562) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ Q719) mutation to K: No effect on RNA binding.
- S778 (= S799) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R801) mutation to Q: Nearly abolishes RNA binding.
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
51% identity, 98% coverage: 12:911/914 of query aligns to 15:849/850 of 3snpA
- active site: D124 (= D125), H125 (= H126), D186 (= D209), R505 (= R557), S739 (= S799), R741 (= R801)
- binding : H125 (= H126), S126 (= S127), H188 (= H211), L243 (= L266), R250 (= R273), N279 (= N302), E283 (= E306), S352 (≠ A373), P357 (= P378), K360 (≠ R381), T419 (= T459), N420 (= N460), T421 (= T461), N504 (= N556), R505 (= R557), L520 (= L572), S642 (= S701), P643 (= P702), A644 (= A703), G645 (= G704), N646 (≠ A705), R649 (≠ P708), R665 (≠ K724), S669 (= S728), G671 (= G730), R674 (= R733), R741 (= R801)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
26% identity, 91% coverage: 73:904/914 of query aligns to 59:746/754 of 5acnA
- active site: D100 (= D125), H101 (= H126), D165 (= D209), R447 (= R557), S642 (= S799), R644 (= R801)
- binding fe3-s4 cluster: I145 (= I176), H147 (= H178), H167 (= H211), C358 (= C458), C421 (= C524), C424 (= C527), N446 (= N556)
- binding tricarballylic acid: K198 (≠ L242), G235 (= G279), R666 (= R823)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
26% identity, 91% coverage: 73:904/914 of query aligns to 86:773/781 of P16276
- Q99 (= Q86) binding substrate
- DSH 192:194 (= DSH 209:211) binding substrate
- C385 (= C458) binding [4Fe-4S] cluster
- C448 (= C524) binding [4Fe-4S] cluster
- C451 (= C527) binding [4Fe-4S] cluster
- R474 (= R557) binding substrate
- R479 (= R562) binding substrate
- R607 (≠ Q719) binding substrate
- SR 670:671 (= SR 800:801) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
26% identity, 91% coverage: 73:904/914 of query aligns to 58:745/753 of 1b0kA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R557), A641 (≠ S799), R643 (= R801)
- binding citrate anion: Q71 (= Q86), H100 (= H126), D164 (= D209), S165 (= S210), R446 (= R557), R451 (= R562), R579 (≠ Q719), A641 (≠ S799), S642 (= S800), R643 (= R801)
- binding oxygen atom: D164 (= D209), H166 (= H211)
- binding iron/sulfur cluster: H100 (= H126), D164 (= D209), H166 (= H211), S356 (= S457), C357 (= C458), C420 (= C524), C423 (= C527)
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
26% identity, 91% coverage: 73:904/914 of query aligns to 58:745/753 of 8acnA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R557), S641 (= S799), R643 (= R801)
- binding nitroisocitric acid: Q71 (= Q86), T74 (= T89), H100 (= H126), D164 (= D209), S165 (= S210), R446 (= R557), R451 (= R562), R579 (≠ Q719), S641 (= S799), S642 (= S800), R643 (= R801)
- binding iron/sulfur cluster: H100 (= H126), D164 (= D209), H166 (= H211), S356 (= S457), C357 (= C458), C420 (= C524), C423 (= C527), I424 (= I528)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
26% identity, 91% coverage: 73:904/914 of query aligns to 58:745/753 of 1fghA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R557), S641 (= S799), R643 (= R801)
- binding 4-hydroxy-aconitate ion: Q71 (= Q86), T74 (= T89), H100 (= H126), D164 (= D209), S165 (= S210), R446 (= R557), R451 (= R562), R579 (≠ Q719), S641 (= S799), S642 (= S800), R643 (= R801)
- binding iron/sulfur cluster: H100 (= H126), D164 (= D209), H166 (= H211), S356 (= S457), C357 (= C458), C420 (= C524), C423 (= C527), I424 (= I528), R451 (= R562)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
26% identity, 91% coverage: 73:904/914 of query aligns to 58:745/753 of 1amjA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R557), S641 (= S799), R643 (= R801)
- binding iron/sulfur cluster: I144 (= I176), H166 (= H211), C357 (= C458), C420 (= C524), C423 (= C527)
- binding sulfate ion: Q71 (= Q86), R579 (≠ Q719), R643 (= R801)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
26% identity, 91% coverage: 73:904/914 of query aligns to 58:745/753 of 1amiA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R557), S641 (= S799), R643 (= R801)
- binding alpha-methylisocitric acid: Q71 (= Q86), T74 (= T89), H100 (= H126), D164 (= D209), S165 (= S210), R446 (= R557), R451 (= R562), R579 (≠ Q719), S641 (= S799), S642 (= S800), R643 (= R801)
- binding iron/sulfur cluster: H100 (= H126), I144 (= I176), D164 (= D209), H166 (= H211), S356 (= S457), C357 (= C458), C420 (= C524), C423 (= C527), N445 (= N556)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
26% identity, 91% coverage: 73:904/914 of query aligns to 58:745/753 of 1acoA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R557), S641 (= S799), R643 (= R801)
- binding iron/sulfur cluster: H100 (= H126), I144 (= I176), D164 (= D209), H166 (= H211), S356 (= S457), C357 (= C458), C420 (= C524), C423 (= C527), N445 (= N556)
- binding aconitate ion: Q71 (= Q86), D164 (= D209), S165 (= S210), R446 (= R557), R451 (= R562), R579 (≠ Q719), S641 (= S799), S642 (= S800), R643 (= R801)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
26% identity, 91% coverage: 73:904/914 of query aligns to 58:745/753 of 1nisA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R557), S641 (= S799), R643 (= R801)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q86), H100 (= H126), D164 (= D209), S165 (= S210), R446 (= R557), R451 (= R562), R579 (≠ Q719), S641 (= S799), S642 (= S800)
- binding iron/sulfur cluster: H100 (= H126), I144 (= I176), H166 (= H211), S356 (= S457), C357 (= C458), C420 (= C524), C423 (= C527)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
26% identity, 91% coverage: 73:904/914 of query aligns to 86:773/780 of P20004
- Q99 (= Q86) binding substrate
- DSH 192:194 (= DSH 209:211) binding substrate
- C385 (= C458) binding [4Fe-4S] cluster
- C448 (= C524) binding [4Fe-4S] cluster
- C451 (= C527) binding [4Fe-4S] cluster
- R474 (= R557) binding substrate
- R479 (= R562) binding substrate
- R607 (≠ Q719) binding substrate
- SR 670:671 (= SR 800:801) binding substrate
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)
32% identity, 33% coverage: 76:378/914 of query aligns to 85:352/778 of P19414
Sites not aligning to the query:
- 1:16 modified: transit peptide, Mitochondrion
- 604 R→K: Strongly diminishes the catalytic activity towards both known substrates, aconitate and homoaconitate.
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 33% coverage: 76:378/914 of query aligns to 86:355/789 of P39533
Sites not aligning to the query:
- 610 K→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)
26% identity, 42% coverage: 204:588/914 of query aligns to 135:473/758 of O14289
Sites not aligning to the query:
- 486 modified: Phosphoserine
- 488 modified: Phosphoserine
Query Sequence
>WP_011814195.1 NCBI__GCF_000015585.1:WP_011814195.1
MTDSFNARTTLQAGGKAYEIYSLDGPRRDYDVDRLPFSLKILLENLLRKEDGVNVTREHI
EAVLNWDPKATPKDQIAFTPARVVLQDFTGVPAVVDLAAMRDAMKNLGGDPSRINPLSPA
DLVIDHSVMVDHFGNRQALQLNTEIEYQRNRERYEFLRWGQTAFSNFRVVPPGTGIVHQV
NLEYLGQVVFRNENGDTPQAYPDTLVGTDSHTTMINGLGILGWGVGGIEAEAAMLGQPIS
MLVPEVVGFRLEGKLPEGATATDLVLTVTEMLRKKGVVGKFVEFFGDGLDHLPLADRATI
ANMAPEYGATCGIFPVDKETLAYMELSGREQELIDLTEQYAKAQGMWRETGSREAEYSDT
LSLDLSTVVPSLAGPKRPQDRVSLDAAKASFKQTLQDHLRAHHTVPTDAAEEHFESEGGH
SAPGIDDAHERGAVEIEIGGRKEMLKHGDVVIAAITSCTNTSNPAVLVAAGLVAKKARER
GLMPKPWVKTSLAPGSQVVPAYLEQAGLLDDLEHLGFSVVGFGCTTCIGNSGPLPEAVAE
GIREGDLCVTSVLSGNRNFEGRIHQDVRANYLASPPLVVAYALAGTMARDLYKEPLGTDN
QGRDVYLKDIWPSQQEVADLVRGNISAEMYREQYANVFDGDAAWQSIDAPSGELYDWRES
TYVKNPPYFQGMNQTPQPLQDIRGARCLIYVGDSITTDHISPAGAIHPDSPAGQYLQEQG
VAPKDFNSYGSRRGNHEVMMRGTFANVRLRNKMAPGTEGGWTTHVPSGEQTSVYDASMRY
QQADTPLIVLAGKEYGTGSSRDWAAKGTNLLGIKAVIAESYERIHRSNLVGFGVLPLQFQ
DGENAETLGLKGDEAFDIEGITEQPRTVRVLARRDDGTETTFEARVRVDTPQEWEYYRHG
SILHYVLRGLAGTA
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