(data stored in SCRATCH zone)

SWISSPROT: B6H215_PENRW

ID   B6H215_PENRW            Unreviewed;       798 AA.
AC   B6H215;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|RuleBase:RU362107};
DE            Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE            EC=4.2.1.- {ECO:0000256|RuleBase:RU362107};
GN   ORFNames=Pc13g03110 {ECO:0000313|EMBL:CAP91380.1}, PCH_Pc13g03110
GN   {ECO:0000313|EMBL:CAP91380.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP91380.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP91380.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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   -!- SUBCELLULAR LOCATION: Mitochondrion
CC       {ECO:0000256|RuleBase:RU362107}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|RuleBase:RU362107}.
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DR   EMBL; AM920428; CAP91380.1; -; Genomic_DNA.
DR   RefSeq; XP_002558749.1; XM_002558703.1.
DR   ProteinModelPortal; B6H215; -.
DR   STRING; 500485.XP_002558749.1; -.
DR   EnsemblFungi; CAP91380; CAP91380; PCH_Pc13g03110.
DR   GeneID; 8314766; -.
DR   KEGG; pcs:Pc13g03110; -.
DR   eggNOG; KOG0453; Eukaryota.
DR   eggNOG; COG1048; LUCA.
DR   HOGENOM; HOG000224293; -.
DR   KO; K17450; -.
DR   OMA; QPRFYGC; -.
DR   OrthoDB; EOG092C0DQS; -.
DR   BioCyc; PCHR:PC13G03110-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
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:0032543; P:mitochondrial translation; IEA:EnsemblFungi.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
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; SSF52016; SSF52016; 1.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR01340; aconitase_mito; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6H215.
DR   SWISS-2DPAGE; B6H215.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Iron {ECO:0000256|RuleBase:RU362107};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU362107};
KW   Lyase {ECO:0000256|RuleBase:RU362107};
KW   Metal-binding {ECO:0000256|RuleBase:RU362107};
KW   Mitochondrion {ECO:0000256|RuleBase:RU362107};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT   DOMAIN       66    516       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   DOMAIN      597    724       Aconitase_C. {ECO:0000259|Pfam:PF00694}.
SQ   SEQUENCE   798 AA;  85141 MW;  78E6C98F78F1F000 CRC64;
     MVSQLVWQRV SASRGMATRL SSQRLLARGL ATEASSSRMP PYPKLVRNLE QVRRVLGSDR
     ALTLAEKILY AHLDNAEESL LTGTNNGRDV RGKANLKLKP DRVAMQDASA QMALLQFMSC
     GLPSTAVPAS IHCDHMIVGE RGADTDLPAS IKGNSEVFDF LESAAKRYGI EFWPPGAGII
     HQSVLENYAA PGLMMLGTDS HTPNGGGLGA IAIGVGGADA VDALVDAPWE LKAPKILGVR
     LEGKLSGWAS PKDIILSLAG KLTVRGGTGS IIEYHGPGVE TLSCTGMATC CNMGAEVGAT
     TSVFPFSPSM VPYLQSTHRG HVADAAAEVA AAGPSSLLRA DTKAEYDQLV TINLSELEPH
     INGPFTPDFS VPLSKFADTV REKKWPETFG AGLIGSCTNS SYEDMTRAED LVKQATAAGL
     KPKADFFITP GSEQIRATLD RDQTLNTFSE AGGVVLANAC GPCIGQWKRT DGVPKDEDNA
     IFTSYNRNFP GRNDGNRRTM NFLASPELVT ALAYSGSTTF NPMTDSLTTP DGSTFKFQPP
     SGFDLPSAGF EEGNPNFLPT AAVPDASAEV IVSPTSDRLA ILEPFEPFPK GDLSGLQVLY
     KVKGQCTTDT ISAAGPWLKY KGHLPNISAN TLIGAVNAAT GETNVAYDEA GNKYGIPELA
     EAWKERGISW LVVAEDNYGE GSAREHAALQ PRYLGGRVIV SKSFARIHET NLKKQGVVPL
     TFANREDYDR IDACDKVDTV GLYDVLQAGG QGEIKLRVTK QKTGEVFDVP VQHTFSQDQC
     AFILAGSALN LLAKKAHS
//

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