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

3 structures for Q01059

Entry ID Method Resolution Chain Position Source
3SN2 X-ray 299 A A 2-889 PDB
3SNP X-ray 280 A A/B 2-889 PDB
AF-Q01059-F1 Predicted AlphaFoldDB

No variants for Q01059

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q01059

No associated diseases with Q01059

5 regional properties for Q01059

Type Name Position InterPro Accession
domain Aconitase A/isopropylmalate dehydratase small subunit, swivel domain 693 - 818 IPR000573
domain Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha domain 63 - 564 IPR001030
binding_site Aconitase family, 4Fe-4S cluster binding site 429 - 445 IPR018136-1
binding_site Aconitase family, 4Fe-4S cluster binding site 495 - 508 IPR018136-2
domain Aconitase A, swivel domain 670 - 839 IPR044137

Functions

Description
EC Number 4.2.1.3 Hydro-lyases
Subcellular Localization
  • Cytoplasm, cytosol
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.

5 GO annotations of molecular function

Name Definition
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.

4 GO annotations of biological process

Name Definition
cellular iron ion homeostasis Any process involved in the maintenance of an internal steady state of iron ions at the level of a cell.
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.
response to iron(II) ion Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an iron(II) ion stimulus.
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
MSNPFAYLAE PLDPAQPGKK FFNLNKLDYS RYGRLPFSIR VLLEAAVRNC DKFLVKKEDI
70 80 90 100 110 120
ENILNWNVTQ HMNIEVPFKP ARVILQDFTG VPSVVDFAAM RDAVKKLGGD PEKINPICPV
130 140 150 160 170 180
DLVIDHSIQV DFNRRADSLQ KNQDLEFERN RERFEFLKWG SKAFRNMRII PPGSGIIHQV
190 200 210 220 230 240
NLEYLARVVF DQDGYYYPDS LVGTDSHTTM IDGLGVLGWG VGGIEAEAVM LGQPISMVLP
250 260 270 280 290 300
QVIGYRLMGK PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGLGVAQLSI ADRATIANMC
310 320 330 340 350 360
PEYGATATFF PVDEVSIKYL VQTGRDESKV KQIRKYLQAV GMFRDYSDPS QDPDFTQVVE
370 380 390 400 410 420
LDLKTVVPCC SGPKRPQDKV AVSDMKKDFE SCLGAKQGFK GFQVAPDHHN DHKTFIYNDS
430 440 450 460 470 480
EFTLSHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVDAG LNVKPYVKTS LSPGSGVVTY
490 500 510 520 530 540
YLRESGVMPY LSQLGFDVVG YGCMTCIGNS GPLPEPVVEA ITQGDLVAVG VLSGNRNFEG
550 560 570 580 590 600
RVHPNTRANY LASPPLVIAY AIAGTIRIDF EKEPLGTNAK GQQVFLRDIW PTREEIQAVE
610 620 630 640 650 660
RQYVIPGMFT EVYQKIETVN ASWNALAAPS DKLYLWNPKS TYIKSPPFFE NLTLDLQPPK
670 680 690 700 710 720
SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG LTPREFNSYG SRRGNDAIMA
730 740 750 760 770 780
RGTFANIRLL NRFLNKQAPQ TIHLPSGETL DVFDAAERYQ QEGHPLIVLA GKEYGSGSSR
790 800 810 820 830 840
DWAAKGPFLL GIKAVLAESY ERIHRSNLVG MGVIPLEYLP GENADSLGLT GRERYTIIIP
850 860 870 880
ENLTPRMHVQ VKLDTGKTFQ AVIRFDTDVE LTYLHNGGIL NYMIRKMAK