SitesBLAST
Comparing WP_037570303.1 NCBI__GCF_000744815.1:WP_037570303.1 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)
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)
34% identity, 90% coverage: 35:626/661 of query aligns to 85:737/778 of P19414
- R604 (= R510) 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)
30% identity, 97% coverage: 14:655/661 of query aligns to 55:779/789 of P39533
- K610 (≠ R510) 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)
32% identity, 93% coverage: 37:652/661 of query aligns to 64:742/754 of 5acnA
- active site: D100 (= D74), H101 (= H75), D165 (= D129), R447 (= R389), S642 (= S553), R644 (= R555)
- binding fe3-s4 cluster: I145 (≠ V109), H147 (= H111), H167 (= H131), C358 (≠ S307), C421 (= C367), C424 (= C370), N446 (≠ P388)
- binding tricarballylic acid: K198 (≠ V162), G235 (= G199), R666 (= R577)
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
32% identity, 93% coverage: 37:652/661 of query aligns to 63:741/753 of 8acnA
- active site: D99 (= D74), H100 (= H75), D164 (= D129), R446 (= R389), S641 (= S553), R643 (= R555)
- binding nitroisocitric acid: Q71 (= Q45), T74 (= T48), H100 (= H75), D164 (= D129), S165 (= S130), R446 (= R389), R451 (= R394), R579 (= R510), S641 (= S553), S642 (= S554), R643 (= R555)
- binding iron/sulfur cluster: H100 (= H75), D164 (= D129), H166 (= H131), S356 (= S306), C357 (≠ S307), C420 (= C367), C423 (= C370), I424 (= I371)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
32% identity, 93% coverage: 37:652/661 of query aligns to 63:741/753 of 1fghA
- active site: D99 (= D74), H100 (= H75), D164 (= D129), R446 (= R389), S641 (= S553), R643 (= R555)
- binding 4-hydroxy-aconitate ion: Q71 (= Q45), T74 (= T48), H100 (= H75), D164 (= D129), S165 (= S130), R446 (= R389), R451 (= R394), R579 (= R510), S641 (= S553), S642 (= S554), R643 (= R555)
- binding iron/sulfur cluster: H100 (= H75), D164 (= D129), H166 (= H131), S356 (= S306), C357 (≠ S307), C420 (= C367), C423 (= C370), I424 (= I371), R451 (= R394)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
32% identity, 93% coverage: 37:652/661 of query aligns to 63:741/753 of 1amjA
- active site: D99 (= D74), H100 (= H75), D164 (= D129), R446 (= R389), S641 (= S553), R643 (= R555)
- binding iron/sulfur cluster: I144 (≠ V109), H166 (= H131), C357 (≠ S307), C420 (= C367), C423 (= C370)
- binding sulfate ion: Q71 (= Q45), R579 (= R510), R643 (= R555)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
32% identity, 93% coverage: 37:652/661 of query aligns to 63:741/753 of 1amiA
- active site: D99 (= D74), H100 (= H75), D164 (= D129), R446 (= R389), S641 (= S553), R643 (= R555)
- binding alpha-methylisocitric acid: Q71 (= Q45), T74 (= T48), H100 (= H75), D164 (= D129), S165 (= S130), R446 (= R389), R451 (= R394), R579 (= R510), S641 (= S553), S642 (= S554), R643 (= R555)
- binding iron/sulfur cluster: H100 (= H75), I144 (≠ V109), D164 (= D129), H166 (= H131), S356 (= S306), C357 (≠ S307), C420 (= C367), C423 (= C370), N445 (≠ P388)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
32% identity, 93% coverage: 37:652/661 of query aligns to 63:741/753 of 1acoA
- active site: D99 (= D74), H100 (= H75), D164 (= D129), R446 (= R389), S641 (= S553), R643 (= R555)
- binding iron/sulfur cluster: H100 (= H75), I144 (≠ V109), D164 (= D129), H166 (= H131), S356 (= S306), C357 (≠ S307), C420 (= C367), C423 (= C370), N445 (≠ P388)
- binding aconitate ion: Q71 (= Q45), D164 (= D129), S165 (= S130), R446 (= R389), R451 (= R394), R579 (= R510), S641 (= S553), S642 (= S554), R643 (= R555)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
32% identity, 93% coverage: 37:652/661 of query aligns to 63:741/753 of 1b0kA
- active site: D99 (= D74), H100 (= H75), D164 (= D129), R446 (= R389), A641 (≠ S553), R643 (= R555)
- binding citrate anion: Q71 (= Q45), H100 (= H75), D164 (= D129), S165 (= S130), R446 (= R389), R451 (= R394), R579 (= R510), A641 (≠ S553), S642 (= S554), R643 (= R555)
- binding oxygen atom: D164 (= D129), H166 (= H131)
- binding iron/sulfur cluster: H100 (= H75), D164 (= D129), H166 (= H131), S356 (= S306), C357 (≠ S307), C420 (= C367), C423 (= C370)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
33% identity, 93% coverage: 37:652/661 of query aligns to 91:769/780 of P20004
- Q99 (= Q45) binding substrate
- DSH 192:194 (= DSH 129:131) binding substrate
- C385 (≠ S307) binding [4Fe-4S] cluster
- C448 (= C367) binding [4Fe-4S] cluster
- C451 (= C370) binding [4Fe-4S] cluster
- R474 (= R389) binding substrate
- R479 (= R394) binding substrate
- R607 (= R510) binding substrate
- SR 670:671 (= SR 554:555) binding substrate
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
32% identity, 93% coverage: 37:652/661 of query aligns to 63:741/753 of 1nisA
- active site: D99 (= D74), H100 (= H75), D164 (= D129), R446 (= R389), S641 (= S553), R643 (= R555)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q45), H100 (= H75), D164 (= D129), S165 (= S130), R446 (= R389), R451 (= R394), R579 (= R510), S641 (= S553), S642 (= S554)
- binding iron/sulfur cluster: H100 (= H75), I144 (≠ V109), H166 (= H131), S356 (= S306), C357 (≠ S307), C420 (= C367), C423 (= C370)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
32% identity, 93% coverage: 37:652/661 of query aligns to 91:769/781 of P16276
- Q99 (= Q45) binding substrate
- DSH 192:194 (= DSH 129:131) binding substrate
- C385 (≠ S307) binding [4Fe-4S] cluster
- C448 (= C367) binding [4Fe-4S] cluster
- C451 (= C370) binding [4Fe-4S] cluster
- R474 (= R389) binding substrate
- R479 (= R394) binding substrate
- R607 (= R510) binding substrate
- SR 670:671 (= SR 554:555) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
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)
27% identity, 91% coverage: 58:661/661 of query aligns to 223:986/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
29% identity, 62% coverage: 14:423/661 of query aligns to 3:421/423 of 4kp1A
- active site: D64 (= D74), H65 (= H75), D121 (= D129), R387 (= R389)
- binding 2,4-dimethylpentane-2,4-diol: F299 (≠ V303), S302 (= S306), S383 (≠ R385), F389 (= F391)
- binding magnesium ion: C303 (≠ S307), T304 (≠ A308), R387 (= R389)
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)
26% identity, 95% coverage: 34:660/661 of query aligns to 85:903/909 of P09339
- C450 (≠ S307) 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 (= R523) 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
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)
28% identity, 77% coverage: 82:593/661 of query aligns to 148:818/889 of P21399
- C300 (≠ G224) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ D242) to M: in dbSNP:rs150373174
- C437 (vs. gap) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C367) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C370) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R389) mutation to Q: Strongly reduced RNA binding.
- R541 (= R394) mutation to Q: Strongly reduced RNA binding.
- R699 (= R510) mutation to K: No effect on RNA binding.
- S778 (= S553) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R555) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
28% identity, 77% coverage: 82:593/661 of query aligns to 147:817/888 of 2b3xA
Sites not aligning to the query:
4nqyA The reduced form of mj0499 (see paper)
27% identity, 62% coverage: 14:423/661 of query aligns to 2:408/409 of 4nqyA
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, 84% coverage: 37:591/661 of query aligns to 31:655/758 of O14289
- S486 (≠ Y433) modified: Phosphoserine
- S488 (≠ R435) modified: Phosphoserine
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
28% identity, 79% coverage: 73:593/661 of query aligns to 123:779/850 of 3snpA
- active site: D124 (= D74), H125 (= H75), D186 (= D129), R505 (= R389), S739 (= S553), R741 (= R555)
- binding : H125 (= H75), S126 (≠ N76), H188 (= H131), L243 (= L186), R250 (≠ G193), N279 (= N222), E283 (= E226), S352 (≠ A280), P357 (= P285), K360 (≠ V288), T419 (≠ A308), N420 (= N309), T421 (≠ P310), N504 (≠ R385), R505 (= R389), L520 (= L404), S642 (= S500), P643 (= P501), A644 (= A502), G645 (= G503), N646 (vs. gap), R649 (vs. gap), R665 (≠ K515), S669 (vs. gap), G671 (vs. gap), R674 (vs. gap), R741 (= R555)
Query Sequence
>WP_037570303.1 NCBI__GCF_000744815.1:WP_037570303.1
MTAEQEARSAQNGSLAYRLIADHLVEGRMTAGEEIALRVDQTLTQDATGTLVMQELEALG
LDRAQTEVSVQYVDHNLLQADERNAEDHAFLRSAAHRYGLWYSKPGNGVSHPVHMQRFGV
PGRSLAGSDSHTCAAGALGMLAVGVGGLEVALAIAGQPLHLVMPRIRGIRLTGQLPPWVS
AKDVILELLRRHGVKGGVGWILEYHGPGLDHLSAMDRHVIANMGAELGATASVFPSDRVT
RDFLRAQGRGEDFAMLTAGPDARYDETEEIDLSTLEPLIARPSSPGDVVPVGEVEGEEIA
QSVIGSSANPGLRDFAVAAGIVAGRQTAPGVSLDVNPTSRELLQDLARSGAVLDLIAAGA
RLHQAGCLGCIGMGQAPAAGRNSLRTFPRNFPGRSGTEEDAVWLCSPETAAVSALTGRIT
DPRRWAEENKAEYPRFTEPDRYTVNLTSLEEPPPHQRAVDTELERGPNISALPELEPLPD
RLALRVLLKAGDDVSTDEISPAGAKALPYRSNLPKLAEFTLTRIDPDYPERAAASREDGG
HAIVAGENWGQGSSREHAAICPRLLGLHAVLAKSFARIHWQNLVNFGVLPLEFEDVADYD
RLDRDDELILDDLHQSLAEDAPPVILATGADGTEYRLRHRLSTRQRAVVRAGGIIPSLAR
S
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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