SitesBLAST
Comparing WP_012709719.1 NCBI__GCF_000018545.1:WP_012709719.1 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)
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)
56% identity, 99% coverage: 4:894/896 of query aligns to 10:938/943 of A0QX20
- K394 (≠ T399) 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)
56% identity, 99% coverage: 4:894/896 of query aligns to 2:928/931 of D9X0I3
- SVIAD 125:129 (≠ SVIVD 133:137) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C503) 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 (= R728) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ H732) 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)
55% identity, 99% coverage: 6:893/896 of query aligns to 11:904/909 of P09339
- C450 (= C437) 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)
55% identity, 97% coverage: 23:895/896 of query aligns to 117:988/990 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)
52% identity, 96% coverage: 39:895/896 of query aligns to 33:887/888 of 2b3xA
- active site: D124 (= D131), H125 (= H132), D204 (= D215), R535 (= R536), S777 (= S781), R779 (= R783)
- binding iron/sulfur cluster: I175 (= I182), H206 (= H217), C436 (= C437), C502 (= C503), C505 (= C506), I506 (= I507), N534 (= N535)
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, 96% coverage: 39:895/896 of query aligns to 34:888/889 of P21399
- C300 (≠ G310) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ N328) to M: in dbSNP:rs150373174
- C437 (= C437) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C503) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C506) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R536) mutation to Q: Strongly reduced RNA binding.
- R541 (= R541) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ H699) mutation to K: No effect on RNA binding.
- S778 (= S781) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R783) 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)
50% identity, 96% coverage: 39:895/896 of query aligns to 33:849/850 of 3snpA
- active site: D124 (= D131), H125 (= H132), D186 (= D215), R505 (= R536), S739 (= S781), R741 (= R783)
- binding : H125 (= H132), S126 (= S133), H188 (= H217), L243 (= L272), R250 (= R279), N279 (= N308), E283 (= E312), S352 (≠ A379), P357 (= P384), K360 (≠ R387), T419 (= T438), N420 (= N439), T421 (= T440), N504 (= N535), R505 (= R536), L520 (= L551), S642 (= S681), P643 (= P682), A644 (= A683), G645 (= G684), N646 (≠ S685), R649 (≠ A688), R665 (≠ A704), S669 (≠ Q708), G671 (= G710), R674 (= R713), R741 (= R783)
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: 82:848/896 of query aligns to 85:731/778 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
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 91% coverage: 50:868/896 of query aligns to 53:754/780 of P20004
- Q99 (= Q92) binding substrate
- DSH 192:194 (= DSH 215:217) binding substrate
- C385 (= C437) binding [4Fe-4S] cluster
- C448 (= C503) binding [4Fe-4S] cluster
- C451 (= C506) binding [4Fe-4S] cluster
- R474 (= R536) binding substrate
- R479 (= R541) binding substrate
- R607 (= R721) binding substrate
- SR 670:671 (= SR 782:783) binding substrate
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
28% identity, 91% coverage: 50:868/896 of query aligns to 25:726/753 of 8acnA
- active site: D99 (= D131), H100 (= H132), D164 (= D215), R446 (= R536), S641 (= S781), R643 (= R783)
- binding nitroisocitric acid: Q71 (= Q92), T74 (= T95), H100 (= H132), D164 (= D215), S165 (= S216), R446 (= R536), R451 (= R541), R579 (= R721), S641 (= S781), S642 (= S782), R643 (= R783)
- binding iron/sulfur cluster: H100 (= H132), D164 (= D215), H166 (= H217), S356 (= S436), C357 (= C437), C420 (= C503), C423 (= C506), I424 (= I507)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 91% coverage: 50:868/896 of query aligns to 25:726/753 of 1fghA
- active site: D99 (= D131), H100 (= H132), D164 (= D215), R446 (= R536), S641 (= S781), R643 (= R783)
- binding 4-hydroxy-aconitate ion: Q71 (= Q92), T74 (= T95), H100 (= H132), D164 (= D215), S165 (= S216), R446 (= R536), R451 (= R541), R579 (= R721), S641 (= S781), S642 (= S782), R643 (= R783)
- binding iron/sulfur cluster: H100 (= H132), D164 (= D215), H166 (= H217), S356 (= S436), C357 (= C437), C420 (= C503), C423 (= C506), I424 (= I507), R451 (= R541)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 91% coverage: 50:868/896 of query aligns to 25:726/753 of 1amjA
- active site: D99 (= D131), H100 (= H132), D164 (= D215), R446 (= R536), S641 (= S781), R643 (= R783)
- binding iron/sulfur cluster: I144 (= I182), H166 (= H217), C357 (= C437), C420 (= C503), C423 (= C506)
- binding sulfate ion: Q71 (= Q92), R579 (= R721), R643 (= R783)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 91% coverage: 50:868/896 of query aligns to 25:726/753 of 1amiA
- active site: D99 (= D131), H100 (= H132), D164 (= D215), R446 (= R536), S641 (= S781), R643 (= R783)
- binding alpha-methylisocitric acid: Q71 (= Q92), T74 (= T95), H100 (= H132), D164 (= D215), S165 (= S216), R446 (= R536), R451 (= R541), R579 (= R721), S641 (= S781), S642 (= S782), R643 (= R783)
- binding iron/sulfur cluster: H100 (= H132), I144 (= I182), D164 (= D215), H166 (= H217), S356 (= S436), C357 (= C437), C420 (= C503), C423 (= C506), N445 (= N535)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 91% coverage: 50:868/896 of query aligns to 25:726/753 of 1acoA
- active site: D99 (= D131), H100 (= H132), D164 (= D215), R446 (= R536), S641 (= S781), R643 (= R783)
- binding iron/sulfur cluster: H100 (= H132), I144 (= I182), D164 (= D215), H166 (= H217), S356 (= S436), C357 (= C437), C420 (= C503), C423 (= C506), N445 (= N535)
- binding aconitate ion: Q71 (= Q92), D164 (= D215), S165 (= S216), R446 (= R536), R451 (= R541), R579 (= R721), S641 (= S781), S642 (= S782), R643 (= R783)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 91% coverage: 50:868/896 of query aligns to 25:726/753 of 1nisA
- active site: D99 (= D131), H100 (= H132), D164 (= D215), R446 (= R536), S641 (= S781), R643 (= R783)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q92), H100 (= H132), D164 (= D215), S165 (= S216), R446 (= R536), R451 (= R541), R579 (= R721), S641 (= S781), S642 (= S782)
- binding iron/sulfur cluster: H100 (= H132), I144 (= I182), H166 (= H217), S356 (= S436), C357 (= C437), C420 (= C503), C423 (= C506)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
28% identity, 91% coverage: 50:868/896 of query aligns to 26:727/754 of 5acnA
- active site: D100 (= D131), H101 (= H132), D165 (= D215), R447 (= R536), S642 (= S781), R644 (= R783)
- binding fe3-s4 cluster: I145 (= I182), H147 (= H184), H167 (= H217), C358 (= C437), C421 (= C503), C424 (= C506), N446 (= N535)
- binding tricarballylic acid: K198 (≠ L248), G235 (≠ S285), R666 (= R805)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 91% coverage: 50:868/896 of query aligns to 53:754/781 of P16276
- Q99 (= Q92) binding substrate
- DSH 192:194 (= DSH 215:217) binding substrate
- C385 (= C437) binding [4Fe-4S] cluster
- C448 (= C503) binding [4Fe-4S] cluster
- C451 (= C506) binding [4Fe-4S] cluster
- R474 (= R536) binding substrate
- R479 (= R541) binding substrate
- R607 (= R721) binding substrate
- SR 670:671 (= SR 782:783) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
28% identity, 91% coverage: 50:868/896 of query aligns to 25:726/753 of 1b0kA
- active site: D99 (= D131), H100 (= H132), D164 (= D215), R446 (= R536), A641 (≠ S781), R643 (= R783)
- binding citrate anion: Q71 (= Q92), H100 (= H132), D164 (= D215), S165 (= S216), R446 (= R536), R451 (= R541), R579 (= R721), A641 (≠ S781), S642 (= S782), R643 (= R783)
- binding oxygen atom: D164 (= D215), H166 (= H217)
- binding iron/sulfur cluster: H100 (= H132), D164 (= D215), H166 (= H217), S356 (= S436), C357 (= C437), C420 (= C503), C423 (= C506)
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: 40:840/896 of query aligns to 54:729/789 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)
25% identity, 42% coverage: 210:583/896 of query aligns to 135:487/758 of O14289
- S486 (≠ K582) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
Query Sequence
>WP_012709719.1 NCBI__GCF_000018545.1:WP_012709719.1
MSKSLDSFNCRSTLTVNGVDYVYYSLPKAEANGLAGVSKLPYSMKVLLENLLRNEDDRSV
TKKDIENVAAWLSDKGTAENEIAYRPARVLMQDFTGVPAVVDLAAMRDAMVSLGGDPEKI
NPLVPVDLVIDHSVIVDEFGTPQAFARNVELEYQRNGERYRFLKWGQQAFKNFRVVPPGT
GICHQVNLEYLGQTVWTREENGEITAYPDTCVGTDSHTTMINGLGVLGWGVGGIEAEAAM
LGQPVSMLLPEVIGFKLTGKLKEGVTATDLVLTVVQMLRKKGVVSKFVEFFGPGLDNMTL
ADRATIGNMGPEYGATCGFFPVDAETINYLTMSGREEQRIALVEAYSKAQGMWREGDGSE
LVFTDTLELDLGDVVPSMAGPKRPEGRIALENIASGFATALENDYKKPGQLANRYAVEGT
DFDLGHGDVAIAAITSCTNTSNPSVLIAAGLLARNAVAKGLKTKPWVKTSLAPGSQVVGE
YLAKSGLQTDLDALGFNLVGFGCTTCIGNSGPLPAPISKTINDKGLIAAGVLSGNRNFEG
RISPDVQANYLASPPLVVAYALAGTVQKDLTKEPIGEDRDGKPVYLKDIWPTSQEIQEFI
FKYVTRDLYASKYADVFKGDENWQAVQVPAGQTYAWDEGSTYVQNPPYFVGMGKKGAGIS
DIKGARVLGLFGDKITTDHISPAGSIKAASPAGSYLLGHGVTVADFNQYGTRRGNHEVMM
RGTFANIRIRNHMLGPNGKEGGYTIHYPSKEEISIYDAAMTYKEEGVPLVIFAGVEYGNG
SSRDWAAKGTNLLGVKAVIAQSFERIHRSNLVGMGVIPFVFEAGMTWESLALKGDEVVTI
EGLANVQPREKRVAKITYGDGSVKEVPLICRIDTLDEVTYVNNGGILQTVLRDLAA
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