SitesBLAST
Comparing WP_028997591.1 NCBI__GCF_000430725.1:WP_028997591.1 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)
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, 99% coverage: 3:903/907 of query aligns to 97:987/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
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, 99% coverage: 14:907/907 of query aligns to 20:909/909 of P09339
- C450 (= C436) 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
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)
51% identity, 96% coverage: 33:907/907 of query aligns to 36:942/943 of A0QX20
- K394 (≠ E393) 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)
52% identity, 96% coverage: 37:905/907 of query aligns to 32:930/931 of D9X0I3
- SVIAD 125:129 (≠ SVMVD 130:134) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C502) 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 (≠ L732) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
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)
49% identity, 100% coverage: 1:903/907 of query aligns to 1:887/889 of P21399
- C300 (≠ A304) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ E322) to M: in dbSNP:rs150373174
- C437 (= C436) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C502) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C505) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R535) mutation to Q: Strongly reduced RNA binding.
- R541 (= R540) mutation to Q: Strongly reduced RNA binding.
- R699 (= R699) mutation to K: No effect on RNA binding.
- S778 (= S789) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R791) 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: 21:903/907 of query aligns to 19:886/888 of 2b3xA
- active site: D124 (= D128), H125 (= H129), D204 (= D209), R535 (= R535), S777 (= S789), R779 (= R791)
- binding iron/sulfur cluster: I175 (= I179), H206 (= H211), C436 (= C436), C502 (= C502), C505 (= C505), I506 (= I506), N534 (= N534)
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
47% identity, 99% coverage: 9:903/907 of query aligns to 7:848/850 of 3snpA
- active site: D124 (= D128), H125 (= H129), D186 (= D209), R505 (= R535), S739 (= S789), R741 (= R791)
- binding : H125 (= H129), S126 (= S130), H188 (= H211), L243 (= L266), R250 (= R273), N279 (= N302), E283 (= E306), S352 (≠ A373), P357 (= P378), K360 (≠ R381), T419 (= T437), N420 (= N438), T421 (= T439), N504 (= N534), R505 (= R535), L520 (= L550), S642 (= S681), P643 (= P682), A644 (= A683), G645 (= G684), N646 (≠ S685), R649 (≠ E688), R665 (≠ P704), S669 (= S708), G671 (= G710), R674 (= R713), R741 (= R791)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 89% coverage: 94:899/907 of query aligns to 86:782/789 of P39533
- K610 (≠ R721) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
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, 85% coverage: 122:896/907 of query aligns to 117:769/778 of P19414
- R604 (= R699) 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
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
28% identity, 90% coverage: 85:896/907 of query aligns to 67:744/753 of 8acnA
- active site: D99 (= D128), H100 (= H129), D164 (= D209), R446 (= R535), S641 (= S789), R643 (= R791)
- binding nitroisocitric acid: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D209), S165 (= S210), R446 (= R535), R451 (= R540), R579 (= R721), S641 (= S789), S642 (= S790), R643 (= R791)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D209), H166 (= H211), S356 (= S435), C357 (= C436), C420 (= C502), C423 (= C505), I424 (= I506)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 90% coverage: 85:896/907 of query aligns to 67:744/753 of 1fghA
- active site: D99 (= D128), H100 (= H129), D164 (= D209), R446 (= R535), S641 (= S789), R643 (= R791)
- binding 4-hydroxy-aconitate ion: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D209), S165 (= S210), R446 (= R535), R451 (= R540), R579 (= R721), S641 (= S789), S642 (= S790), R643 (= R791)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D209), H166 (= H211), S356 (= S435), C357 (= C436), C420 (= C502), C423 (= C505), I424 (= I506), R451 (= R540)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 90% coverage: 85:896/907 of query aligns to 67:744/753 of 1amjA
- active site: D99 (= D128), H100 (= H129), D164 (= D209), R446 (= R535), S641 (= S789), R643 (= R791)
- binding iron/sulfur cluster: I144 (= I179), H166 (= H211), C357 (= C436), C420 (= C502), C423 (= C505)
- binding sulfate ion: Q71 (= Q89), R579 (= R721), R643 (= R791)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 90% coverage: 85:896/907 of query aligns to 67:744/753 of 1amiA
- active site: D99 (= D128), H100 (= H129), D164 (= D209), R446 (= R535), S641 (= S789), R643 (= R791)
- binding alpha-methylisocitric acid: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D209), S165 (= S210), R446 (= R535), R451 (= R540), R579 (= R721), S641 (= S789), S642 (= S790), R643 (= R791)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), D164 (= D209), H166 (= H211), S356 (= S435), C357 (= C436), C420 (= C502), C423 (= C505), N445 (= N534)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 90% coverage: 85:896/907 of query aligns to 67:744/753 of 1acoA
- active site: D99 (= D128), H100 (= H129), D164 (= D209), R446 (= R535), S641 (= S789), R643 (= R791)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), D164 (= D209), H166 (= H211), S356 (= S435), C357 (= C436), C420 (= C502), C423 (= C505), N445 (= N534)
- binding aconitate ion: Q71 (= Q89), D164 (= D209), S165 (= S210), R446 (= R535), R451 (= R540), R579 (= R721), S641 (= S789), S642 (= S790), R643 (= R791)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 90% coverage: 85:896/907 of query aligns to 67:744/753 of 1nisA
- active site: D99 (= D128), H100 (= H129), D164 (= D209), R446 (= R535), S641 (= S789), R643 (= R791)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q89), H100 (= H129), D164 (= D209), S165 (= S210), R446 (= R535), R451 (= R540), R579 (= R721), S641 (= S789), S642 (= S790)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), H166 (= H211), S356 (= S435), C357 (= C436), C420 (= C502), C423 (= C505)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 90% coverage: 85:896/907 of query aligns to 95:772/780 of P20004
- Q99 (= Q89) binding substrate
- DSH 192:194 (= DSH 209:211) binding substrate
- C385 (= C436) binding [4Fe-4S] cluster
- C448 (= C502) binding [4Fe-4S] cluster
- C451 (= C505) binding [4Fe-4S] cluster
- R474 (= R535) binding substrate
- R479 (= R540) binding substrate
- R607 (= R721) binding substrate
- SR 670:671 (= SR 790:791) binding substrate
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
30% identity, 82% coverage: 85:829/907 of query aligns to 68:682/754 of 5acnA
- active site: D100 (= D128), H101 (= H129), D165 (= D209), R447 (= R535), S642 (= S789), R644 (= R791)
- binding fe3-s4 cluster: I145 (= I179), H147 (= H181), H167 (= H211), C358 (= C436), C421 (= C502), C424 (= C505), N446 (= N534)
- binding tricarballylic acid: K198 (≠ L242), G235 (= G279), R666 (= R813)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
29% identity, 82% coverage: 85:829/907 of query aligns to 67:681/753 of 1b0kA
- active site: D99 (= D128), H100 (= H129), D164 (= D209), R446 (= R535), A641 (≠ S789), R643 (= R791)
- binding citrate anion: Q71 (= Q89), H100 (= H129), D164 (= D209), S165 (= S210), R446 (= R535), R451 (= R540), R579 (= R721), A641 (≠ S789), S642 (= S790), R643 (= R791)
- binding oxygen atom: D164 (= D209), H166 (= H211)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D209), H166 (= H211), S356 (= S435), C357 (= C436), C420 (= C502), C423 (= C505)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
30% identity, 82% coverage: 85:829/907 of query aligns to 95:709/781 of P16276
- Q99 (= Q89) binding substrate
- DSH 192:194 (= DSH 209:211) binding substrate
- C385 (= C436) binding [4Fe-4S] cluster
- C448 (= C502) binding [4Fe-4S] cluster
- C451 (= C505) binding [4Fe-4S] cluster
- R474 (= R535) binding substrate
- R479 (= R540) binding substrate
- R607 (= R721) binding substrate
- SR 670:671 (= SR 790:791) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
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: 148:540/907 of query aligns to 96:448/758 of O14289
Sites not aligning to the query:
- 486 modified: Phosphoserine
- 488 modified: Phosphoserine
Query Sequence
>WP_028997591.1 NCBI__GCF_000430725.1:WP_028997591.1
MAHAFANTLTEFSTPSGRTGRFFSLPKLAERWPAVRRLPVSLRIVLESVLRNCDGKKVTP
AHVEQLAGWQPAAQREEEIPFVVARVVLQDFTGVPLLADLAAMRNVAADQGRNPKLIEPL
VPVDLVVDHSVMVDHYGTPAALDLNMKLEFERNRERYEFMKWGMQAFETFRVVPPGFGIV
HQVNLEYLARGLHRDADGVSYPDTLVGTDSHTTMINGLGVVAWGVGGIEAEAAMLGQPVY
LLTPDVVGFELTGALREGVTATDLVLTVTEILRKHRVVGKFVEFFGEGTRSLALPDRATI
GNMAPEYGATMGFFPVDERTVEYLRGTGRPEADLELFEAYWKAQGLFGVSRAGEIDYSQV
VSLDLSSVQPSVAGPKRPQDRIELGKLSSTFTELFSKPVPQNGFNQPPEKLGQAFTTSNG
LEIHNGDVLIAAITSCTNTSNPGVLLAAGLLAKKAVEAGLSVQPHIKTSLAPGSRVVTEY
LTRAGLLPYLEKLGFAVAAYGCTTCIGNAGDLTQELNEVIWRNDLVCAAVLSGNRNFEAR
IHPNLKANFLASPPLVVAYAIAGTVLRDLMTEPVGTGHGGKPVYLGDIWPSSDEVHALMK
YAMDPEAFKANYAKVESAPGPLWQAIKGVSGQVYDWPASTYIARPPFFEGFTMQPQALVS
GVKGARVMALFGDSITTDHISPAGSIKEASPTGQWLIERHVLKPDFNSYGSRRGNHEVMM
RGTFANVRIKNLMLPPKPDGAIEEGGLTLFQLDGPDQGEKMFIYDAAMKYQAAGVPTVIF
AGEEYGTGSSRDWAAKGTQLLGIKAVVARSFERIHRSNLIGMGVLPLQFRGEDSWQTLGL
RGDEVIDIELPPGEPRPLSEATLVIRRGDSSTQRVTLTLRIDTPIEVDYYKHGGILPFVL
RQLLQAA
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