Reviewed, UniProtKB/Swiss-Prot P82611 (ACON_CANAL)

Names and origin

Protein names

Recommended name:
    Aconitate hydratase, mitochondrial
      Short name=Aconitase
    EC=4.2.1.3
Alternative name(s):
    Citrate hydro-lyase

Gene names

Name:	ACO1
ORF Names:	CaO19.6385, CaO19.13742

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	777 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Citrate = isocitrate.
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aconitate hydratase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 777		Aconitate hydratase, mitochondrial		PRO_0000076648
Sites
	Metal binding	383	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	446	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	449	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Sequence conflict	419 – 421	3	EQV → VQQ AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P82611-1 [UniParc]. Last modified March 3, 2009. Version 2. Checksum: B854CDE375844793	FASTA	777	84,221
	10 20 30 40 50 60 MLSASRTALR APRSVRGLAT ASLTKDSQVN QNLLESHSFI NYKKHLENVE IVKSRLNRPL 70 80 90 100 110 120 TYAEKLLYGH LDDPHNQEIE RGVSYLKLRP DRVACQDATA QMAILQFMSA GIPQVATPST 130 140 150 160 170 180 VHCDHLIQAQ VGGPKDLARA IDLNKEVYDF LSTACAKYNL GFWKPGSGII HQIVLENYAF 190 200 210 220 230 240 PGALLIGTDS HTPNAGGLGQ LAIGVGGADA VDVMSGLPWE LKAPKIIGVK LTGKMSGWTS 250 260 270 280 290 300 PKDIILKLAG ITTVKGGTGS IVEYFGSGVD TFSCTGMGTI CNMGAEIGAT TSVFPFNDSM 310 320 330 340 350 360 VDYLNATGRS EIAQFAQVYK KDFLSADEGA EYDQVIEIDL NTLEPHINGP FTPDLATPVS 370 380 390 400 410 420 KMKETAIANG WPLEVKVGLI GSCTNSSYED MTRAASIIKD AGAHGLKSKA LYTVSPGSEQ 430 440 450 460 470 480 VRATIARDGQ LKTFEDFGGV VMANACGPCI GQWDRQDIKK GDKNTIVSSF NRNFTARNDG 490 500 510 520 530 540 NPATHAFVAS PEMATVYAIS GDLGFNPITD TLVGADGKEF KLKEPQGVGL PPDGYDPGEN 550 560 570 580 590 600 TYQAPPEDRA SVEVVISPTS DRLQKLSPFK PWDGKDAERL PILIKAVGKT TTDHISMAGP 610 620 630 640 650 660 WLKYRGHLEN ISNNYMIGAI NAENGKANEV RNHYTGKYDG VPQTAAAYRD AGHKWVVIGD 670 680 690 700 710 720 ENFGEGSSRE HAALEPRFLG GFAIITKSFA RIHETNLKKQ GLLPLNFKNP ADYDKINFDD 730 740 750 760 770 EVDLIGLTTL APGKDVILRV HPKEGEAWEA VLTHTFNSEQ LEWFKHGSAL NFIKSKY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.
[2]	"Cross-species identification of novel Candida albicans immunogenic proteins by combination of two-dimensional polyacrylamide gel electrophoresis and mass spectrometry." Pardo M., Ward M., Pitarch A., Sanchez M., Nombela C., Blackstock W., Gil C. Electrophoresis 21:2651-2659(2000) [PubMed: 10949142] [Abstract] Cited for: PROTEIN SEQUENCE OF 377-393 AND 412-422, MASS SPECTROMETRY. Strain: SC5314.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AACQ01000073 Genomic DNA. Translation: EAK97138.1. AACQ01000072 Genomic DNA. Translation: EAK97226.1.
RefSeq	XP_716141.1. XP_716225.1.
3D structure databases
HSSP	HSSP built from PDB template 1AMJ based on UniProtKB P20004.
ModBase	Search...
2-D gel databases
COMPLUYEAST-2DPAGE	P82611.
Genome annotation databases
GeneID	3642090. 3642201.
KEGG	cal:CaO19.13742. cal:CaO19.6385.
Organism-specific databases
CGD	CAL0001406. ACO1.
Phylogenomic databases
OMA	PGKPLKC.
Enzyme and pathway databases
BRENDA	4.2.1.3. 1124.
Family and domain databases
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015937. Aconitase-like_core. IPR015928. Aconitase/3IPM_dehydase_swvl. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR006248. Aconitase_mito-like. IPR000573. AconitaseA/IPMdHydase_ssu_swvl. [Graphical view]
Gene3D	G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF5. Aconitase_mito. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
ProDom	PD000511. Aconitase_N. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01340. aconitase_mito. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACON_CANAL

Accession

Primary (citable) accession number: P82611
Secondary accession number(s): Q5A380

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	March 3, 2009
Last modified:	November 3, 2009
This is version 49 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)