SitesBLAST
Comparing WP_028487612.1 NCBI__GCF_000621325.1:WP_028487612.1 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, 97% coverage: 11:855/867 of query aligns to 23:899/909 of P09339
- C450 (= C411) 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 (≠ K695) 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)
41% identity, 96% coverage: 34:863/867 of query aligns to 41:940/943 of A0QX20
- K394 (vs. gap) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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: 34:854/867 of query aligns to 131:980/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
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)
43% identity, 95% coverage: 32:855/867 of query aligns to 31:922/931 of D9X0I3
- SVIAD 125:129 (≠ SLAVE 121:125) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C477) 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 (≠ K695) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ E699) 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)
42% identity, 98% coverage: 10:855/867 of query aligns to 17:881/889 of P21399
- C300 (≠ T295) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ D313) to M: in dbSNP:rs150373174
- C437 (= C411) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C477) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C480) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R510) mutation to Q: Strongly reduced RNA binding.
- R541 (= R515) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ M666) mutation to K: No effect on RNA binding.
- S778 (= S750) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R752) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
42% identity, 98% coverage: 10:855/867 of query aligns to 16:880/888 of 2b3xA
- active site: D124 (= D119), H125 (= H120), D204 (= D200), R535 (= R510), S777 (= S750), R779 (= R752)
- binding iron/sulfur cluster: I175 (= I171), H206 (= H202), C436 (= C411), C502 (= C477), C505 (= C480), I506 (≠ N481), N534 (= N509)
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
41% identity, 95% coverage: 31:855/867 of query aligns to 31:842/850 of 3snpA
- active site: D124 (= D119), H125 (= H120), D186 (= D200), R505 (= R510), S739 (= S750), R741 (= R752)
- binding : H125 (= H120), S126 (= S121), H188 (= H202), L243 (= L257), R250 (= R264), N279 (= N293), E283 (= E297), S352 (≠ A363), P357 (= P368), K360 (≠ R371), T419 (= T412), N420 (= N413), T421 (= T414), N504 (= N509), R505 (= R510), L520 (= L525), S642 (= S648), P643 (= P649), A644 (≠ S650), G645 (≠ N651), N646 (≠ A652), R649 (≠ M655), R665 (≠ E671), S669 (= S675), G671 (≠ A677), R674 (= R680), R741 (= R752)
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: 74:860/867 of query aligns to 89:775/778 of P19414
- R604 (≠ M666) 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)
29% identity, 93% coverage: 54:859/867 of query aligns to 74:777/780 of P20004
- Q99 (≠ H80) binding substrate
- DSH 192:194 (= DSH 200:202) binding substrate
- C385 (= C411) binding [4Fe-4S] cluster
- C448 (= C477) binding [4Fe-4S] cluster
- C451 (= C480) binding [4Fe-4S] cluster
- R474 (= R510) binding substrate
- R479 (= R515) binding substrate
- R607 (≠ M666) binding substrate
- SR 670:671 (= SR 751:752) binding substrate
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 94% coverage: 40:855/867 of query aligns to 55:780/789 of P39533
- K610 (≠ M666) 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)
28% identity, 93% coverage: 54:859/867 of query aligns to 46:749/753 of 8acnA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R510), S641 (= S750), R643 (= R752)
- binding nitroisocitric acid: Q71 (≠ H80), T74 (≠ L83), H100 (= H120), D164 (= D200), S165 (= S201), R446 (= R510), R451 (= R515), R579 (≠ M666), S641 (= S750), S642 (= S751), R643 (= R752)
- binding iron/sulfur cluster: H100 (= H120), D164 (= D200), H166 (= H202), S356 (= S410), C357 (= C411), C420 (= C477), C423 (= C480), I424 (≠ N481)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 93% coverage: 54:859/867 of query aligns to 46:749/753 of 1fghA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R510), S641 (= S750), R643 (= R752)
- binding 4-hydroxy-aconitate ion: Q71 (≠ H80), T74 (≠ L83), H100 (= H120), D164 (= D200), S165 (= S201), R446 (= R510), R451 (= R515), R579 (≠ M666), S641 (= S750), S642 (= S751), R643 (= R752)
- binding iron/sulfur cluster: H100 (= H120), D164 (= D200), H166 (= H202), S356 (= S410), C357 (= C411), C420 (= C477), C423 (= C480), I424 (≠ N481), R451 (= R515)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 93% coverage: 54:859/867 of query aligns to 46:749/753 of 1amjA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R510), S641 (= S750), R643 (= R752)
- binding iron/sulfur cluster: I144 (= I171), H166 (= H202), C357 (= C411), C420 (= C477), C423 (= C480)
- binding sulfate ion: Q71 (≠ H80), R579 (≠ M666), R643 (= R752)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 93% coverage: 54:859/867 of query aligns to 46:749/753 of 1amiA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R510), S641 (= S750), R643 (= R752)
- binding alpha-methylisocitric acid: Q71 (≠ H80), T74 (≠ L83), H100 (= H120), D164 (= D200), S165 (= S201), R446 (= R510), R451 (= R515), R579 (≠ M666), S641 (= S750), S642 (= S751), R643 (= R752)
- binding iron/sulfur cluster: H100 (= H120), I144 (= I171), D164 (= D200), H166 (= H202), S356 (= S410), C357 (= C411), C420 (= C477), C423 (= C480), N445 (= N509)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 93% coverage: 54:859/867 of query aligns to 46:749/753 of 1acoA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R510), S641 (= S750), R643 (= R752)
- binding iron/sulfur cluster: H100 (= H120), I144 (= I171), D164 (= D200), H166 (= H202), S356 (= S410), C357 (= C411), C420 (= C477), C423 (= C480), N445 (= N509)
- binding aconitate ion: Q71 (≠ H80), D164 (= D200), S165 (= S201), R446 (= R510), R451 (= R515), R579 (≠ M666), S641 (= S750), S642 (= S751), R643 (= R752)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
28% identity, 93% coverage: 54:859/867 of query aligns to 47:750/754 of 5acnA
- active site: D100 (= D119), H101 (= H120), D165 (= D200), R447 (= R510), S642 (= S750), R644 (= R752)
- binding fe3-s4 cluster: I145 (= I171), H147 (= H173), H167 (= H202), C358 (= C411), C421 (= C477), C424 (= C480), N446 (= N509)
- binding tricarballylic acid: K198 (≠ R233), G235 (≠ S270), R666 (= R774)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 93% coverage: 54:859/867 of query aligns to 46:749/753 of 1nisA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R510), S641 (= S750), R643 (= R752)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (≠ H80), H100 (= H120), D164 (= D200), S165 (= S201), R446 (= R510), R451 (= R515), R579 (≠ M666), S641 (= S750), S642 (= S751)
- binding iron/sulfur cluster: H100 (= H120), I144 (= I171), H166 (= H202), S356 (= S410), C357 (= C411), C420 (= C477), C423 (= C480)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
28% identity, 93% coverage: 54:859/867 of query aligns to 46:749/753 of 1b0kA
- active site: D99 (= D119), H100 (= H120), D164 (= D200), R446 (= R510), A641 (≠ S750), R643 (= R752)
- binding citrate anion: Q71 (≠ H80), H100 (= H120), D164 (= D200), S165 (= S201), R446 (= R510), R451 (= R515), R579 (≠ M666), A641 (≠ S750), S642 (= S751), R643 (= R752)
- binding oxygen atom: D164 (= D200), H166 (= H202)
- binding iron/sulfur cluster: H100 (= H120), D164 (= D200), H166 (= H202), S356 (= S410), C357 (= C411), C420 (= C477), C423 (= C480)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 93% coverage: 54:859/867 of query aligns to 74:777/781 of P16276
- Q99 (≠ H80) binding substrate
- DSH 192:194 (= DSH 200:202) binding substrate
- C385 (= C411) binding [4Fe-4S] cluster
- C448 (= C477) binding [4Fe-4S] cluster
- C451 (= C480) binding [4Fe-4S] cluster
- R474 (= R510) binding substrate
- R479 (= R515) binding substrate
- R607 (≠ M666) binding substrate
- SR 670:671 (= SR 751:752) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
4nqyA The reduced form of mj0499 (see paper)
25% identity, 43% coverage: 170:540/867 of query aligns to 86:404/409 of 4nqyA
Sites not aligning to the query:
Query Sequence
>WP_028487612.1 NCBI__GCF_000621325.1:WP_028487612.1
MNTEYRKNLPGTKLDYFDTRAAIEAIQPGSYATLPYTSRVLAEQLVRRCEPEMLTDSLKQ
LIEGKQDLDFPWYPARVVCHDILGQTALVDLAGLRDAIADQGGNPAKVNPVVPTQLIVDH
SLAVECGGFDPDAFAKNRAIEDRRNEDRFHFIEWTKTAFKNVDVIPAGNGIMHQINLEKM
SPVIQARDGVAFPDTCVGTDSHTPHVDALGVIAIGVGGLEAETVMLGLPSMMRLPDIIGV
KLVGKRQPGITATDIVLAITEFLRKERVVSAWLEFFGEGAKNLTIGDRATISNMTPEFGA
SAGMFYIDEQTIDYLKLTGREPEQVALVENYAKATGLWADSLVDATYPRVLEFDLSSVVR
NMAGPSNPHRRLPTADLAERGIAVNLAAAQAEEAEGKMPDGAVIIAAITSCTNTSNPRNV
VAAALLARNANKLGLVRKPWVKTSFAPGSKVAELYLQEAGLLTELEQLGFGIVGFACTTC
NGMSGALDPVIQQEIIDRDLYATAVLSGNRNFDGRIHPYAKQAFLASPPLVVAYAIAGTI
RFDIEKDVLGTDKDGNPITLKDIWPTDEEIDAIVATSVKPEQFKQIYIPMFDLGTVEEAK
SPLYDWRPMSTYIRRPPYWEGALAGERTLKGMLPLAVLPDNITTDHLSPSNAIMMNSAAG
EYLHKMGLPEEDFNSYATHRGDHLTAQRATFANPKLINEMAVVDGKVKQGSLARVEPEGQ
VMRMWEAIETYMERKQPLIIVAGADYGQGSSRDWAAKGVRLAGVEAIVAEGFERIHRTNL
VGMGVLPLEFKAGETRKTYAIDGTESYDVEGDIAPRTDLTVIMHRRNGETVRIPVTCRLD
TAAEVRVYNAGGVLQRFAQDFLEGDAA
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