ACON_CANAL
ID ACON_CANAL Reviewed; 777 AA.
AC P82611; A0A1D8PTN8; Q5A380;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Aconitate hydratase, mitochondrial;
DE Short=Aconitase;
DE EC=4.2.1.3;
DE AltName: Full=Citrate hydro-lyase;
DE Flags: Precursor;
GN Name=ACO1; OrderedLocusNames=CAALFM_CR08210CA;
GN ORFNames=CaO19.13742, CaO19.6385;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PROTEIN SEQUENCE OF 377-393 AND 412-422, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=10949142;
RX DOI=10.1002/1522-2683(20000701)21:13<2651::aid-elps2651>3.0.co;2-3;
RA Pardo M., Ward M., Pitarch A., Sanchez M., Nombela C., Blackstock W.,
RA Gil C.;
RT "Cross-species identification of novel Candida albicans immunogenic
RT proteins by combination of two-dimensional polyacrylamide gel
RT electrophoresis and mass spectrometry.";
RL Electrophoresis 21:2651-2659(2000).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate, a step in the citric acid cycle. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; CP017630; AOW31505.1; -; Genomic_DNA.
DR RefSeq; XP_716225.1; XM_711132.1.
DR AlphaFoldDB; P82611; -.
DR SMR; P82611; -.
DR BioGRID; 1225184; 2.
DR STRING; 237561.P82611; -.
DR COMPLUYEAST-2DPAGE; P82611; -.
DR PRIDE; P82611; -.
DR GeneID; 3642090; -.
DR KEGG; cal:CAALFM_CR08210CA; -.
DR CGD; CAL0000182282; ACO1.
DR VEuPathDB; FungiDB:CR_08210C_A; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR InParanoid; P82611; -.
DR OMA; GCIGMGQ; -.
DR OrthoDB; 190960at2759; -.
DR UniPathway; UPA00223; UER00718.
DR PRO; PR:P82611; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0003994; F:aconitate hydratase activity; IBA:GO_Central.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR Gene3D; 3.40.1060.10; -; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01340; aconitase_mito; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..777
FT /note="Aconitate hydratase, mitochondrial"
FT /id="PRO_0000076648"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189..191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 605
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 668..669
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 419..421
FT /note="EQV -> VQQ (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 777 AA; 84221 MW; B854CDE375844793 CRC64;
MLSASRTALR APRSVRGLAT ASLTKDSQVN QNLLESHSFI NYKKHLENVE IVKSRLNRPL
TYAEKLLYGH LDDPHNQEIE RGVSYLKLRP DRVACQDATA QMAILQFMSA GIPQVATPST
VHCDHLIQAQ VGGPKDLARA IDLNKEVYDF LSTACAKYNL GFWKPGSGII HQIVLENYAF
PGALLIGTDS HTPNAGGLGQ LAIGVGGADA VDVMSGLPWE LKAPKIIGVK LTGKMSGWTS
PKDIILKLAG ITTVKGGTGS IVEYFGSGVD TFSCTGMGTI CNMGAEIGAT TSVFPFNDSM
VDYLNATGRS EIAQFAQVYK KDFLSADEGA EYDQVIEIDL NTLEPHINGP FTPDLATPVS
KMKETAIANG WPLEVKVGLI GSCTNSSYED MTRAASIIKD AGAHGLKSKA LYTVSPGSEQ
VRATIARDGQ LKTFEDFGGV VMANACGPCI GQWDRQDIKK GDKNTIVSSF NRNFTARNDG
NPATHAFVAS PEMATVYAIS GDLGFNPITD TLVGADGKEF KLKEPQGVGL PPDGYDPGEN
TYQAPPEDRA SVEVVISPTS DRLQKLSPFK PWDGKDAERL PILIKAVGKT TTDHISMAGP
WLKYRGHLEN ISNNYMIGAI NAENGKANEV RNHYTGKYDG VPQTAAAYRD AGHKWVVIGD
ENFGEGSSRE HAALEPRFLG GFAIITKSFA RIHETNLKKQ GLLPLNFKNP ADYDKINFDD
EVDLIGLTTL APGKDVILRV HPKEGEAWEA VLTHTFNSEQ LEWFKHGSAL NFIKSKY
