P99148

PR
Gene name
acnA (citB, SA1184)
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
Staphylococcus aureus (strain N315)
KEGG Pathway
sau:SA1184
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)

364-449 (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 P99148

Entry ID Method Resolution Chain Position Source
AF-P99148-F1 Predicted AlphaFoldDB

No variants for P99148

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P99148

No associated diseases with P99148

2 regional properties for P99148

Type Name Position InterPro Accession
conserved_site Aliphatic acid kinase, short-chain, conserved site 5 - 16 IPR023865-1
conserved_site Aliphatic acid kinase, short-chain, conserved site 203 - 220 IPR023865-2

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
MAANFKEQSK KHFDLNGQSY TYYDLKAVEE QGITKVSNLP YSIRVLLESL LRQEDDFVIT
70 80 90 100 110 120
DDHIKALSQF GKDGNEGEVP FKPSRVILQD FTGVPAVVDL ASLRKAMDDV GGDITKINPE
130 140 150 160 170 180
VPVDLVIDHS VQVDSYANPE ALERNMKLEF ERNYERYQFL NWATKAFDNY NAVPPATGIV
190 200 210 220 230 240
HQVNLEYLAS VVHVRDVDGE KTAFPDTLVG TDSHTTMING IGVLGWGVGG IEAEAGMLGQ
250 260 270 280 290 300
PSYFPIPEVI GVRLVNSLPQ GATATDLALR VTQELRKKGV VGKFVEFFGP GVQHLPLADR
310 320 330 340 350 360
ATIANMAPEY GATCGFFPVD DESLKYMKLT GRSDEHIALV KEYLKQNHMF FDVEKEDPNY
370 380 390 400 410 420
TDVIELDLST VEASLSGPKR PQDLIFLSDM KSSFENSVTA PAGNQGHGLD KSEFDKKAEI
430 440 450 460 470 480
NFKDGSKATM KTGDIAIAAI TSCTNTSNPY VMLGAGLVAK KAVEKGLKVP EYVKTSLAPG
490 500 510 520 530 540
SKVVTGYLRD AGLQPYLDDL GFNLVGYGCT TCIGNSGPLL PEIEKAIADE DLLVTSVLSG
550 560 570 580 590 600
NRNFEGRIHP LVKANYLASP QLVVAYALAG TVDIDLQNEP IGKGNDGEDV YLKDIWPSIK
610 620 630 640 650 660
EVSDTVDSVV TPELFIEEYN NVYNNNELWN EIDVTDQPLY DFDPNSTYIQ NPSFFQGLSK
670 680 690 700 710 720
EPGTIVPLNG LRVMGKFGDS VTTDHISPAG AIGKDTPAGK YLQDHQVPIR EFNSYGSRRG
730 740 750 760 770 780
NHEVMVRGTF ANIRIKNQLA PGTEGGFTTY WPTNEVMPIF DAAMKYKEDG TGLVVLAGND
790 800 810 820 830 840
YGMGSSRDWA AKGTNLLGVK TVIAQSYERI HRSNLVMMGV LPLEFKKGES ADSLGLDGTE
850 860 870 880 890 900
EISVNIDENV QPHDYVKVTA KKQDGDLVEF DAMVRFDSLV EMDYYRHGGI LQMVLRNKLA
Q