SitesBLAST
Comparing WP_041765781.1 NCBI__GCF_000020045.1:WP_041765781.1 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)
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)
43% identity, 98% coverage: 11:861/865 of query aligns to 23:909/909 of P09339
- C450 (= C406) 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 (≠ T691) 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)
42% identity, 96% coverage: 23:851/865 of query aligns to 12:881/889 of P21399
- C300 (≠ A295) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ D313) to M: in dbSNP:rs150373174
- C437 (= C406) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C472) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C475) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R505) mutation to Q: Strongly reduced RNA binding.
- R541 (= R510) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ M662) mutation to K: No effect on RNA binding.
- S778 (= S746) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R748) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
42% identity, 96% coverage: 23:851/865 of query aligns to 11:880/888 of 2b3xA
- active site: D124 (= D119), H125 (= H120), D204 (= D200), R535 (= R505), S777 (= S746), R779 (= R748)
- binding iron/sulfur cluster: I175 (= I171), H206 (= H202), C436 (= C406), C502 (= C472), C505 (= C475), I506 (≠ N476), N534 (= N504)
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)
42% identity, 95% coverage: 32:850/865 of query aligns to 129:980/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
42% identity, 95% coverage: 31:851/865 of query aligns to 31:842/850 of 3snpA
- active site: D124 (= D119), H125 (= H120), D186 (= D200), R505 (= R505), S739 (= S746), R741 (= R748)
- binding : H125 (= H120), S126 (= S121), H188 (= H202), L243 (= L257), R250 (= R264), N279 (= N293), E283 (= E297), S352 (≠ A363), P357 (= P368), K360 (≠ R371), T419 (= T407), N420 (= N408), T421 (= T409), N504 (= N504), R505 (= R505), L520 (= L520), S642 (= S644), P643 (= P645), A644 (≠ S646), G645 (≠ N647), N646 (≠ A648), R649 (≠ A651), R665 (≠ E667), S669 (= S671), G671 (≠ A673), R674 (= R676), R741 (= R748)
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)
47% identity, 53% coverage: 392:851/865 of query aligns to 458:922/931 of D9X0I3
- C538 (= C472) 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 (≠ T691) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ E695) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
Sites not aligning to the query:
- 125:129 mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
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)
45% identity, 54% coverage: 396:862/865 of query aligns to 468:943/943 of A0QX20
Sites not aligning to the query:
- 394 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
29% identity, 91% coverage: 74:856/865 of query aligns to 89:775/778 of P19414
- R604 (≠ M662) 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)
27% identity, 90% coverage: 74:851/865 of query aligns to 90:780/789 of P39533
- K610 (≠ M662) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 93% coverage: 54:855/865 of query aligns to 74:777/780 of P20004
- Q99 (≠ H80) binding substrate
- DSH 192:194 (= DSH 200:202) binding substrate
- C385 (= C406) binding [4Fe-4S] cluster
- C448 (= C472) binding [4Fe-4S] cluster
- C451 (= C475) binding [4Fe-4S] cluster
- R474 (= R505) binding substrate
- R479 (= R510) binding substrate
- R607 (≠ M662) binding substrate
- SR 670:671 (= SR 747:748) binding substrate
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
28% identity, 93% coverage: 54:855/865 of query aligns to 46:749/753 of 8acnA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R505), S641 (= S746), R643 (= R748)
- binding nitroisocitric acid: Q71 (≠ H80), T74 (≠ L83), H100 (= H120), D164 (= D200), S165 (= S201), R446 (= R505), R451 (= R510), R579 (≠ M662), S641 (= S746), S642 (= S747), R643 (= R748)
- binding iron/sulfur cluster: H100 (= H120), D164 (= D200), H166 (= H202), S356 (= S405), C357 (= C406), C420 (= C472), C423 (= C475), I424 (≠ N476)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 93% coverage: 54:855/865 of query aligns to 46:749/753 of 1fghA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R505), S641 (= S746), R643 (= R748)
- binding 4-hydroxy-aconitate ion: Q71 (≠ H80), T74 (≠ L83), H100 (= H120), D164 (= D200), S165 (= S201), R446 (= R505), R451 (= R510), R579 (≠ M662), S641 (= S746), S642 (= S747), R643 (= R748)
- binding iron/sulfur cluster: H100 (= H120), D164 (= D200), H166 (= H202), S356 (= S405), C357 (= C406), C420 (= C472), C423 (= C475), I424 (≠ N476), R451 (= R510)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 93% coverage: 54:855/865 of query aligns to 46:749/753 of 1amjA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R505), S641 (= S746), R643 (= R748)
- binding iron/sulfur cluster: I144 (= I171), H166 (= H202), C357 (= C406), C420 (= C472), C423 (= C475)
- binding sulfate ion: Q71 (≠ H80), R579 (≠ M662), R643 (= R748)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 93% coverage: 54:855/865 of query aligns to 46:749/753 of 1amiA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R505), S641 (= S746), R643 (= R748)
- binding alpha-methylisocitric acid: Q71 (≠ H80), T74 (≠ L83), H100 (= H120), D164 (= D200), S165 (= S201), R446 (= R505), R451 (= R510), R579 (≠ M662), S641 (= S746), S642 (= S747), R643 (= R748)
- binding iron/sulfur cluster: H100 (= H120), I144 (= I171), D164 (= D200), H166 (= H202), S356 (= S405), C357 (= C406), C420 (= C472), C423 (= C475), N445 (= N504)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 93% coverage: 54:855/865 of query aligns to 46:749/753 of 1acoA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R505), S641 (= S746), R643 (= R748)
- binding iron/sulfur cluster: H100 (= H120), I144 (= I171), D164 (= D200), H166 (= H202), S356 (= S405), C357 (= C406), C420 (= C472), C423 (= C475), N445 (= N504)
- binding aconitate ion: Q71 (≠ H80), D164 (= D200), S165 (= S201), R446 (= R505), R451 (= R510), R579 (≠ M662), S641 (= S746), S642 (= S747), R643 (= R748)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 93% coverage: 54:855/865 of query aligns to 46:749/753 of 1nisA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R505), S641 (= S746), R643 (= R748)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (≠ H80), H100 (= H120), D164 (= D200), S165 (= S201), R446 (= R505), R451 (= R510), R579 (≠ M662), S641 (= S746), S642 (= S747)
- binding iron/sulfur cluster: H100 (= H120), I144 (= I171), H166 (= H202), S356 (= S405), C357 (= C406), C420 (= C472), C423 (= C475)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
28% identity, 93% coverage: 54:855/865 of query aligns to 47:750/754 of 5acnA
- active site: D100 (= D119), H101 (= H120), D165 (= D200), R447 (= R505), S642 (= S746), R644 (= R748)
- binding fe3-s4 cluster: I145 (= I171), H147 (= H173), H167 (= H202), C358 (= C406), C421 (= C472), C424 (= C475), N446 (= N504)
- binding tricarballylic acid: K198 (≠ R233), G235 (= G270), R666 (= R770)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
28% identity, 93% coverage: 54:855/865 of query aligns to 46:749/753 of 1b0kA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R505), A641 (≠ S746), R643 (= R748)
- binding citrate anion: Q71 (≠ H80), H100 (= H120), D164 (= D200), S165 (= S201), R446 (= R505), R451 (= R510), R579 (≠ M662), A641 (≠ S746), S642 (= S747), R643 (= R748)
- binding oxygen atom: D164 (= D200), H166 (= H202)
- binding iron/sulfur cluster: H100 (= H120), D164 (= D200), H166 (= H202), S356 (= S405), C357 (= C406), C420 (= C472), C423 (= C475)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 93% coverage: 54:855/865 of query aligns to 74:777/781 of P16276
- Q99 (≠ H80) binding substrate
- DSH 192:194 (= DSH 200:202) binding substrate
- C385 (= C406) binding [4Fe-4S] cluster
- C448 (= C472) binding [4Fe-4S] cluster
- C451 (= C475) binding [4Fe-4S] cluster
- R474 (= R505) binding substrate
- R479 (= R510) binding substrate
- R607 (≠ M662) binding substrate
- SR 670:671 (= SR 747:748) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
4nqyA The reduced form of mj0499 (see paper)
24% identity, 42% coverage: 170:535/865 of query aligns to 86:404/409 of 4nqyA
Sites not aligning to the query:
Query Sequence
>WP_041765781.1 NCBI__GCF_000020045.1:WP_041765781.1
MNTAYRKPLPGTSLDYFDTRAAVDAIQPGAYDKLPYTSRVHAENLVRRCDPATLNDSLKQ
IVERKRELDFPWFPARVVCHDILGQTALVDLAGLRDAIADQGGDPAKVNPVVPVQLIVDH
SLAVECGGFDPDAFAKNRAIEDRRNEDRFDFINWTKKAFKNVDVIPPGNGIMHQINLERM
SPVIHAADGVAYPDTLVGTDSHTPHVDALGVIAVGVGGLEAENVMLGRASWMRLPDIVGV
ELSGKRQPGITATDIVLALTEFLRKEKVVGAYLEFRGEGASSLTLGDRATISNMAPEYGA
TAAMFFIDEQTIDYLRLTGRDDAQVKLVETYAKTAGLWADTLKHAEYERILSFDLSTVVR
NMAGPSNPHRRLPTSDLAERGIAGKWEEVPGQMPDGAVIIAAITSCTNTSNPRNVIAAAL
LARNANARGLTRKPWVKSSLAPGSKAVELYLQEANLLPELEKLGFGIVAFACTTCNGMSG
ALDPAIQQEIVDRDLYATAVLSGNRNFDGRIHPYAKQAFLASPPLVVAYAIAGTIRFDIE
RDVLGTDRDGKPVYLKDIWPSDEEIDAIVKQSVKPEQFRKVYEPMFAVTAASGEPISPLY
DWRAQSTYIRRPPYWEGALAGERTLKGMRPLAVLGDNITTDHLSPSNAILANSAAGEYLT
KMGLPEEDFNSYATHRGDHLTAQRATFANPTLINEMAVVDGQLKKGSLARIEPEGKVTRM
WEAIETYMDRKQPLIIIAGADYGQGSSRDWAAKGVRLAGVEAIVAEGFERIHRTNLIGMG
VLPLEFKRGVNRLALGIDGTETYDVIGERRPRADLTLVIHRKNGERVDVPVTCRLDTAEE
VSIYEAGGVLQRFAQDFLESSKAAA
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