Q937N8

PR
Gene name
acnM
Protein name
Aconitate hydratase A
Names
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
Species
Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
KEGG Pathway
EC number
4.2.1.3: Hydro-lyases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

335-415 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q937N8

Entry ID Method Resolution Chain Position Source
AF-Q937N8-F1 Predicted AlphaFoldDB

No variants for Q937N8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q937N8

No associated diseases with Q937N8

5 regional properties for Q937N8

Type Name Position InterPro Accession
domain Aconitase A/isopropylmalate dehydratase small subunit, swivel domain 700 - 827 IPR000573
domain Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha domain 76 - 570 IPR001030
binding_site Aconitase family, 4Fe-4S cluster binding site 435 - 451 IPR018136-1
binding_site Aconitase family, 4Fe-4S cluster binding site 501 - 514 IPR018136-2
domain Aconitase A, swivel domain 676 - 844 IPR044137

Functions

Description
EC Number 4.2.1.3 Hydro-lyases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

7 GO annotations of molecular function

Name Definition
2-methylisocitrate dehydratase activity Catalysis of the reaction: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = cis-2-methylaconitate + H(2)O.
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
aconitate hydratase activity Catalysis of the reaction: citrate = isocitrate. The reaction occurs in two steps: (1) citrate = cis-aconitate + H2O, (2) cis-aconitate + H2O = isocitrate. This reaction is the interconversion of citrate and isocitrate via the labile, enzyme-bound intermediate cis-aconitate. Water is removed from one part of the citrate molecule and added back to a different atom to form isocitrate.
citrate dehydratase activity Catalysis of the reaction: citrate = cis-aconitate + H2O.
metal ion binding Binding to a metal ion.
mRNA 3'-UTR binding Binding to a 3' untranslated region of an mRNA molecule.
mRNA binding Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.

2 GO annotations of biological process

Name Definition
propionate metabolic process, methylcitrate cycle The chemical reactions and pathways involving propionate that occur in the methylcitrate cycle.
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNSANRKPLP GTKLDYFDAR AAVEAIQPGA YDKLPYTSRV LAENLVRRCD PATLTDSLLQ
70 80 90 100 110 120
LVGRKRDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAD QGGDPAKVNP VVPVQLIVDH
130 140 150 160 170 180
SLAVECGGFD PDAFAKNRAI EDRRNEDRFH FIDWTKQAFK NVDVIPPGNG IMHQINLEKM
190 200 210 220 230 240
SPVIHADNGV AYPDTCVGTD SHTPHVDALG VIAIGVGGLE AENVMLGRAS WMRLPDIVGV
250 260 270 280 290 300
ELTGKRQPGI TATDIVLALT EFLRKEKVVG AYLEFRGEGA SSLTLGDRAT ISNMAPEYGA
310 320 330 340 350 360
TAAMFFIDEQ TIDYLRLTGR TDEQLKLVET YARTAGLWAD SLKNAEYERV LKFDLSSVVR
370 380 390 400 410 420
NMAGPSNPHK RLPTSALAER GIAVDLDKAS AQEAEGLMPD GAVIIAAITS CTNTSNPRNV
430 440 450 460 470 480
IAAALLARNA NARGLARKPW VKSSLAPGSK AVELYLEEAN LLPDLEKLGF GIVAFACTTC
490 500 510 520 530 540
NGMSGALDPK IQQEIIDRDL YATAVLSGNR NFDGRIHPYA KQAFLASPPL VVAYAIAGTI
550 560 570 580 590 600
RFDIEKDVLG TDQDGKPVYL KDIWPSDEEI DAIVAKSVKP EQFRKVYEPM FAITAASGES
610 620 630 640 650 660
VSPLYDWRPQ STYIRRPPYW EGALAGERTL KALRPLAVLG DNITTDHLSP SNAIMLNSAA
670 680 690 700 710 720
GEYLARMGLP EEDFNSYATH RGDHLTAQRA TFANPTLINE MAVVDGQVKK GSLARIEPEG
730 740 750 760 770 780
KVVRMWEAIE TYMDRKQPLI IIAGADYGQG SSRDWAAKGV RLAGVEVIVA EGFERIHRTN
790 800 810 820 830 840
LIGMGVLPLE FKPGVNRLTL GLDGTETYDV IGERQPRATL TLVVNRKNGE RVEVPVTCRL
850 860
DSDEEVSIYE AGGVLHFAQD FLESSRATA