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Database: UniProt
Entry: A5D9Z7_PICGU
LinkDB: A5D9Z7_PICGU
Original site: A5D9Z7_PICGU 
ID   A5D9Z7_PICGU            Unreviewed;       779 AA.
AC   A5D9Z7;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00015940, ECO:0000256|RuleBase:RU362107};
DE            Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE            EC=4.2.1.- {ECO:0000256|RuleBase:RU362107};
GN   ORFNames=PGUG_00102 {ECO:0000313|EMBL:EDK36004.1};
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK36004.1, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK36004.1, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU362107};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|RuleBase:RU362107};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|RuleBase:RU362107}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU362107}.
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DR   EMBL; CH408155; EDK36004.1; -; Genomic_DNA.
DR   RefSeq; XP_001486725.1; XM_001486675.1.
DR   AlphaFoldDB; A5D9Z7; -.
DR   STRING; 294746.A5D9Z7; -.
DR   GeneID; 5128857; -.
DR   KEGG; pgu:PGUG_00102; -.
DR   VEuPathDB; FungiDB:PGUG_00102; -.
DR   eggNOG; KOG0453; Eukaryota.
DR   HOGENOM; CLU_006714_2_2_1; -.
DR   InParanoid; A5D9Z7; -.
DR   OMA; GCIGMGQ; -.
DR   OrthoDB; 3266779at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd01584; AcnA_Mitochondrial; 1.
DR   Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 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   NCBIfam; TIGR01340; aconitase_mito; 1.
DR   PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR   PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362107};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362107};
KW   Lyase {ECO:0000256|RuleBase:RU362107};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362107};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU362107};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU362107}.
FT   DOMAIN          66..503
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          584..711
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   779 AA;  84458 MW;  D4503A1669712F83 CRC64;
     MLSATRGALK APRTHSIRGL ATAGITRDSQ VNQNLLESHS FINYKKNVET VDIVKKRLNR
     PLTYAEKLLY AHLDDPHGQD IERGVSYLKL RPDRVACQDA TAQMAILQFM SAGMPQVATP
     STVHCDHLIQ AQVGSKKDLA RAIDLNKEVF DFLSSACAKY NLGFWKPGSG IIHQIVLENY
     AFPGALLIGT DSHTPNAGGL GQLAIGVGGA DAVDVMAGLP WELKAPKIIG VKLTGKMSGW
     TSPKDIILKL AGITTVKGGT GAIVEYFGSG VETFSCTGMG TICNMGAEIG ATTSVFPFNN
     SMVDYLNATG RSQIAEFAQL YKKDFLSADE GCEYDQIIEI DLNTLEPHVN GPFTPDLATP
     ISKMKETAKA NDWPMDVKVG LIGSCTNSSY EDMSRAASII KDAAEHGLKA KTIYTVSPGS
     EQVRATIERD GQLKTFEDFG GIVMANACGP CIGQWDRQDI KKGDKNTIVS SFNRNFTSRN
     DGNPATHAFV SSPEMVTAYA IAGDLGFNPI TDTLVGADGK EFKLKEPTGV GLPPNGYDKG
     ENTYQAPPAD RSQVTVEIAP TSDRLQKLSP FKPWNGKDAV GLPILIKALG KTTTDHISMA
     GPWLKYRGHL ENISNNYMIG ATNAENGEAN NLKNRFTGEY KGVPEVAAEY RDAGKPWVVI
     GDENFGEGSS REHAALEPRF LGGFAIITKS FARIHETNLK KQGMLPLNFK NVADYDRINP
     EDTVDILGLT ELAPGKNLIL RVHPQDGGEP WECELTHTYN AEQIEWFKYG SALNKMAAN
//
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