P09339
Gene name |
citB (BSU18000) |
Protein name |
Aconitate hydratase A |
Names |
ACN, Aconitase, Aconitate/2-methylaconitate hydratase, Iron-responsive protein-like, IRP-like, RNA-binding protein |
Species |
Bacillus subtilis (strain 168) |
KEGG Pathway |
bsu:BSU18000 |
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 P09339
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P09339-F1 | Predicted | AlphaFoldDB |
No variants for P09339
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P09339 | |||||
No associated diseases with P09339
5 regional properties for P09339
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aconitase A/isopropylmalate dehydratase small subunit, swivel domain | 707 - 834 | IPR000573 |
| domain | Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha domain | 85 - 577 | IPR001030 |
| binding_site | Aconitase family, 4Fe-4S cluster binding site | 442 - 458 | IPR018136-1 |
| binding_site | Aconitase family, 4Fe-4S cluster binding site | 508 - 521 | IPR018136-2 |
| domain | Aconitase A, swivel domain | 683 - 853 | 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 | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
8 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. |
| iron-responsive element binding | Binding to an iron-responsive element, a regulatory sequence found in the 5'- and 3'-untranslated regions of mRNAs encoding many iron-binding proteins. |
| 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. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| citrate metabolic process | The chemical reactions and pathways involving citrate, 2-hydroxy-1,2,3-propanetricarboyxlate. Citrate is widely distributed in nature and is an important intermediate in the TCA cycle and the glyoxylate cycle. |
| propionate metabolic process, methylcitrate cycle | The chemical reactions and pathways involving propionate that occur in the methylcitrate cycle. |
| regulation of sporulation | Any process that modulates the frequency, rate or extent of sporulation, the process whose specific outcome is the progression of a spore over time, from its initiation to the mature structure. |
| 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 |
| MANEQKTAAK | DVFQARKTFT | TNGKTYHYYS | LKALEDSGIG | KVSKLPYSIK | VLLESVLRQV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DGFVIKKEHV | ENLAKWGTAE | LKDIDVPFKP | SRVILQDFTG | VPAVVDLASL | RKAMAAVGGD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PDKINPEIPV | DLVIDHSVQV | DKAGTEDALA | VNMDLEFERN | AERYKFLSWA | KKAFNNYQAV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PPATGIVHQV | NLEFLASVVH | AIEEDGELVT | YPDTLVGTDS | HTTMINGIGV | LGWGVGGIEA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EAGMLGQPSY | FPVPEVIGAK | LVGKLPNGTT | ATDLALKVTQ | VLREKGVVGK | FVEFFGPGIA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ELPLADRATI | ANMAPEYGAT | CGFFPVDEEA | LNYLRLTGRD | PEHIDVVEAY | CRSNGLFYTP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DAEDPQFTDV | VEIDLSQIEA | NLSGPKRPQD | LIPLSAMQET | FKKQLVSPAG | NQGFGLNAEE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ENKEIKFKLL | NGEETVMKTG | AIAIAAITSC | TNTSNPYVLI | GAGLVAKKAV | ELGLKVPNYV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KTSLAPGSKV | VTGYLVNSGL | LPYMKELGFN | LVGYGCTTCI | GNSGPLSPEI | EEAVAKNDLL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ITSVLSGNRN | FEGRIHPLVK | GNYLASPPLV | VAYALAGTVN | INLKTDPIGV | GKDGQNVYFN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DIWPSMDEIN | ALVKQTVTPE | LFRKEYETVF | DDNKRWNEIE | TTDEALYKWD | NDSTYIQNPP |
| 670 | 680 | 690 | 700 | 710 | 720 |
| FFEEMSVEPG | KVEPLKGLRV | VGKFGDSVTT | DHISPAGAIG | KDTPAGKYLQ | EKGVSPRDFN |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SYGSRRGNHE | VMMRGTFANI | RIKNQIAPGT | EGGFTTYWPT | GEVTSIYDAC | MKYKEDKTGL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| VVLAGKDYGM | GSSRDWAAKG | TNLLGIRTVI | AESFERIHRS | NLVFMGVLPL | QFKQGENADT |
| 850 | 860 | 870 | 880 | 890 | 900 |
| LGLTGKEVIE | VDVDETVRPR | DLVTVRAINE | DGNVTTFEAV | VRFDSEVEID | YYRHGGILQM |
| VLREKMKQS |