SitesBLAST
Comparing WP_012406048.1 NCBI__GCF_000020045.1:WP_012406048.1 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)
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)
45% identity, 98% coverage: 12:870/874 of query aligns to 19:907/909 of P09339
- C450 (= C416) 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 (≠ T703) 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)
43% identity, 97% coverage: 20:867/874 of query aligns to 116:986/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
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, 97% coverage: 20:867/874 of query aligns to 20:886/889 of P21399
- C300 (≠ A303) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ D321) to M: in dbSNP:rs150373174
- C437 (= C416) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C482) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C485) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R515) mutation to Q: Strongly reduced RNA binding.
- R541 (= R520) mutation to Q: Strongly reduced RNA binding.
- R699 (= R674) mutation to K: No effect on RNA binding.
- S778 (= S754) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R756) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
42% identity, 97% coverage: 20:867/874 of query aligns to 19:885/888 of 2b3xA
- active site: D124 (= D124), H125 (= H125), D204 (= D208), R535 (= R515), S777 (= S754), R779 (= R756)
- binding iron/sulfur cluster: I175 (= I175), H206 (= H210), C436 (= C416), C502 (= C482), C505 (= C485), I506 (= I486), N534 (= N514)
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)
41% identity, 95% coverage: 35:866/874 of query aligns to 33:926/931 of D9X0I3
- SVIAD 125:129 (≠ SLAVE 126:130) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C482) 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 (≠ T703) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ S707) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
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)
39% identity, 96% coverage: 33:873/874 of query aligns to 39:943/943 of A0QX20
- K394 (vs. gap) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
40% identity, 97% coverage: 20:867/874 of query aligns to 19:847/850 of 3snpA
- active site: D124 (= D124), H125 (= H125), D186 (= D208), R505 (= R515), S739 (= S754), R741 (= R756)
- binding : H125 (= H125), S126 (= S126), H188 (= H210), L243 (= L265), R250 (= R272), N279 (= N301), E283 (= E305), S352 (≠ A371), P357 (= P376), K360 (≠ L379), T419 (= T417), N420 (= N418), T421 (= T419), N504 (= N514), R505 (= R515), L520 (≠ I530), S642 (= S656), P643 (= P657), A644 (= A658), G645 (≠ S659), N646 (≠ A660), R649 (≠ K663), R665 (≠ D679), S669 (≠ V683), G671 (≠ A685), R674 (= R688), R741 (= R756)
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: 75:864/874 of query aligns to 86:782/789 of P39533
- K610 (≠ R688) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
29% identity, 89% coverage: 75:851/874 of query aligns to 61:736/753 of 8acnA
- active site: D99 (= D124), H100 (= H125), D164 (= D208), R446 (= R515), S641 (= S754), R643 (= R756)
- binding nitroisocitric acid: Q71 (≠ H85), T74 (= T88), H100 (= H125), D164 (= D208), S165 (= S209), R446 (= R515), R451 (= R520), R579 (= R674), S641 (= S754), S642 (= S755), R643 (= R756)
- binding iron/sulfur cluster: H100 (= H125), D164 (= D208), H166 (= H210), S356 (= S415), C357 (= C416), C420 (= C482), C423 (= C485), I424 (= I486)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
29% identity, 89% coverage: 75:851/874 of query aligns to 61:736/753 of 1fghA
- active site: D99 (= D124), H100 (= H125), D164 (= D208), R446 (= R515), S641 (= S754), R643 (= R756)
- binding 4-hydroxy-aconitate ion: Q71 (≠ H85), T74 (= T88), H100 (= H125), D164 (= D208), S165 (= S209), R446 (= R515), R451 (= R520), R579 (= R674), S641 (= S754), S642 (= S755), R643 (= R756)
- binding iron/sulfur cluster: H100 (= H125), D164 (= D208), H166 (= H210), S356 (= S415), C357 (= C416), C420 (= C482), C423 (= C485), I424 (= I486), R451 (= R520)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
29% identity, 89% coverage: 75:851/874 of query aligns to 61:736/753 of 1amjA
- active site: D99 (= D124), H100 (= H125), D164 (= D208), R446 (= R515), S641 (= S754), R643 (= R756)
- binding iron/sulfur cluster: I144 (= I175), H166 (= H210), C357 (= C416), C420 (= C482), C423 (= C485)
- binding sulfate ion: Q71 (≠ H85), R579 (= R674), R643 (= R756)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
29% identity, 89% coverage: 75:851/874 of query aligns to 61:736/753 of 1amiA
- active site: D99 (= D124), H100 (= H125), D164 (= D208), R446 (= R515), S641 (= S754), R643 (= R756)
- binding alpha-methylisocitric acid: Q71 (≠ H85), T74 (= T88), H100 (= H125), D164 (= D208), S165 (= S209), R446 (= R515), R451 (= R520), R579 (= R674), S641 (= S754), S642 (= S755), R643 (= R756)
- binding iron/sulfur cluster: H100 (= H125), I144 (= I175), D164 (= D208), H166 (= H210), S356 (= S415), C357 (= C416), C420 (= C482), C423 (= C485), N445 (= N514)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
29% identity, 89% coverage: 75:851/874 of query aligns to 61:736/753 of 1acoA
- active site: D99 (= D124), H100 (= H125), D164 (= D208), R446 (= R515), S641 (= S754), R643 (= R756)
- binding iron/sulfur cluster: H100 (= H125), I144 (= I175), D164 (= D208), H166 (= H210), S356 (= S415), C357 (= C416), C420 (= C482), C423 (= C485), N445 (= N514)
- binding aconitate ion: Q71 (≠ H85), D164 (= D208), S165 (= S209), R446 (= R515), R451 (= R520), R579 (= R674), S641 (= S754), S642 (= S755), R643 (= R756)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
29% identity, 89% coverage: 75:851/874 of query aligns to 61:736/753 of 1nisA
- active site: D99 (= D124), H100 (= H125), D164 (= D208), R446 (= R515), S641 (= S754), R643 (= R756)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (≠ H85), H100 (= H125), D164 (= D208), S165 (= S209), R446 (= R515), R451 (= R520), R579 (= R674), S641 (= S754), S642 (= S755)
- binding iron/sulfur cluster: H100 (= H125), I144 (= I175), H166 (= H210), S356 (= S415), C357 (= C416), C420 (= C482), C423 (= C485)
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, 87% coverage: 75:836/874 of query aligns to 85:745/778 of P19414
- R604 (= R688) 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
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
29% identity, 89% coverage: 75:851/874 of query aligns to 62:737/754 of 5acnA
- active site: D100 (= D124), H101 (= H125), D165 (= D208), R447 (= R515), S642 (= S754), R644 (= R756)
- binding fe3-s4 cluster: I145 (= I175), H147 (= H177), H167 (= H210), C358 (= C416), C421 (= C482), C424 (= C485), N446 (= N514)
- binding tricarballylic acid: K198 (≠ R241), G235 (= G278), R666 (= R778)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
29% identity, 89% coverage: 75:851/874 of query aligns to 89:764/780 of P20004
- Q99 (≠ H85) binding substrate
- DSH 192:194 (= DSH 208:210) binding substrate
- C385 (= C416) binding [4Fe-4S] cluster
- C448 (= C482) binding [4Fe-4S] cluster
- C451 (= C485) binding [4Fe-4S] cluster
- R474 (= R515) binding substrate
- R479 (= R520) binding substrate
- R607 (= R674) binding substrate
- SR 670:671 (= SR 755:756) binding substrate
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
29% identity, 89% coverage: 75:851/874 of query aligns to 89:764/781 of P16276
- Q99 (≠ H85) binding substrate
- DSH 192:194 (= DSH 208:210) binding substrate
- C385 (= C416) binding [4Fe-4S] cluster
- C448 (= C482) binding [4Fe-4S] cluster
- C451 (= C485) binding [4Fe-4S] cluster
- R474 (= R515) binding substrate
- R479 (= R520) binding substrate
- R607 (= R674) binding substrate
- SR 670:671 (= SR 755:756) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
29% identity, 89% coverage: 75:851/874 of query aligns to 61:736/753 of 1b0kA
- active site: D99 (= D124), H100 (= H125), D164 (= D208), R446 (= R515), A641 (≠ S754), R643 (= R756)
- binding citrate anion: Q71 (≠ H85), H100 (= H125), D164 (= D208), S165 (= S209), R446 (= R515), R451 (= R520), R579 (= R674), A641 (≠ S754), S642 (= S755), R643 (= R756)
- binding oxygen atom: D164 (= D208), H166 (= H210)
- binding iron/sulfur cluster: H100 (= H125), D164 (= D208), H166 (= H210), S356 (= S415), C357 (= C416), C420 (= C482), C423 (= C485)
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)
24% identity, 50% coverage: 80:520/874 of query aligns to 34:448/758 of O14289
Sites not aligning to the query:
- 486 modified: Phosphoserine
- 488 modified: Phosphoserine
Query Sequence
>WP_012406048.1 NCBI__GCF_000020045.1:WP_012406048.1
MENTYSPTEARLSVDGVSHRYVDLPGLFGDKLRELPVVLRLLLENVIRNTQGEERRQAVE
GILAWTARATSEAEIAFQPNRVLMHDTTSTPALVDIAGMRDALAEAGADPATLNPVLPVD
SSVDHSLAVEYFAQRDAAPLNLKLELRRNAERYRFLRWASKALKGVRIHPPGTGIMHTIN
LEQLATVVTSVERDGEKWAVPDTLIGTDSHTPMINGIGVLGWGVGGLEAQTVMFGMPVMQ
RIPDVIGVRLTGAMQPGVLATDLALTVTQRLRAIGVSGEFVEFFGPGVTTLSAGDRAVVA
NMAPEYGASTGFFPIDQHTLDYLRSTNRAETSIKLVEAFARRTGTWFEPQAEPRYTRTID
IDLASIGMHIAGPRRPQDLIDYSQTATTLAKLDFQSAQPHRSMPKHPVAIAAITSCTNTS
DPALLIAAGLLARKARALGLSVPSWVKTSLGPGSPAAAAYLERAGLIDDLSAVGFDIVGY
GCTTCIGNSGPLTEPIRAALAQKSIYPVAMLSGNRNFPGRIHPDLDLGFIMSPPLVIAFA
LAADAEKDLSVDPIQQTSDGKPVYLRDLWPTRDEVDALVRAAADPQDYPRAFALASQNPA
WHDLDAPDNARFPWNPASTALRRPPFASATQGSQLGRYSAYPLLVLGDDVTTDHISPASA
IPKDSFVADFLVSRGDDRDDLNVFASRRGNWEVMMRAAFYNRTLVNSLRAGMPVAHTLHV
PSGDVMPIFEAAQRYRDDGDSVVLVAGERYGTGSSRDWAAKGQRLLGIRAVLAVSFERIH
RSNLIGMGILPLRFAGGANPNTLELQPGDKLEVDAVSDTLSPRCRVAVRVVRANGSVQPI
EATAAVETQLECTLLRSGGVIPLILQKSLQAQEA
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