Q4JVM4
Gene name |
acn (jk0969) |
Protein name |
Aconitate hydratase A |
Names |
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 |
Species |
Corynebacterium jeikeium (strain K411) |
KEGG Pathway |
cjk:jk0969 |
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)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q4JVM4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q4JVM4-F1 | Predicted | AlphaFoldDB |
No variants for Q4JVM4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q4JVM4 | |||||
No associated diseases with Q4JVM4
5 regional properties for Q4JVM4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aconitase A/isopropylmalate dehydratase small subunit, swivel domain | 728 - 858 | IPR000573 |
| domain | Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha domain | 66 - 599 | IPR001030 |
| binding_site | Aconitase family, 4Fe-4S cluster binding site | 464 - 480 | IPR018136-1 |
| binding_site | Aconitase family, 4Fe-4S cluster binding site | 530 - 543 | IPR018136-2 |
| domain | Aconitase A, swivel domain | 705 - 877 | 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 |
| MAESINSFDS | KSTLQVGEKS | YDYFALDAVP | GMEKLPYSLK | VLGENLLRNE | DGKNITREHI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EAIANWDPSA | EPNFEIQFTP | ARVIMQDFTG | VACIVDLATI | RDAVVALGGD | ADDVNPLNPA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EMVIDHSVII | EAFGDSDALE | KNVEIEYQRN | DERYKFLRWG | TGAFENFRVV | PPGTGIVHQV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NIEYLARSVF | DNNGLAYPDT | CVGTDSHTTM | ENGLGILGWG | VGGIEAEAAM | LGQPISMLIP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RVVGFKLTGE | IPTGVTATDV | VLTITDMLRQ | HGVVGKFVEF | YGKGVGELPL | ANRATIGNMS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PEFGSTAAMF | PIDEETVKYL | ELTGRDQETL | ERVEAYAKAQ | GMWLDPEKEV | EYSEYLELDL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| STVVPSIAGP | KRPQDRIELN | DSKAQFRKDL | HNYVEADASA | VTPDFDAEGP | ATENTSAQTA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GTPASAADAK | GNIPSAAAGA | EGRPSNPVTV | NYNGEDIELD | HGMVAIASIT | SCTNTSNPSV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| MVGAGLLARN | AAAKGLKSAP | WVKTSMAPGS | QVVNGYYEKA | GLWKDLEAMG | FYLVGYGCTT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| CIGNSGPLPE | EISAGINEGD | LAATAVLSGN | RNFEGRINPD | VKMNYLASPI | LVIAYAIAGT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| MDFDFETQPL | GQDQDGNDVF | LKDIWPSTED | IEEVIASSIT | KDLYAEDYAN | VFEGDERWRS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LDVPSGKTFD | WDPKSTYIRK | APYFDGMSKE | PEAVNDVKGA | RVLALLGDSV | TTDHISPAST |
| 730 | 740 | 750 | 760 | 770 | 780 |
| IKPGTPAAQY | LDANGVERKD | YNSLGARRGN | HEVMVRGTFA | NIRLQNQLLD | GVSGGYTRDF |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TQEGGPQSFI | YDAAMNYQKE | NTPLVVLGGK | EYGTGSSRDW | AAKGTLLLGV | KAVIAESFER |
| 850 | 860 | 870 | 880 | 890 | 900 |
| IHRSNLIGMG | VVPLQFPEGE | SWKSLGIEGT | ETFDIEGIEE | LNNGSTPKTV | KVTATKENGE |
| 910 | 920 | 930 | |||
| KIEFDAVTRI | DTPGEADYYR | NGGILQFVLR | NMMSGK |