(data stored in ACNUC7421 zone)

SWISSPROT: Q13DS6_RHOPS

ID   Q13DS6_RHOPS            Unreviewed;       905 AA.
AC   Q13DS6;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE            Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE            EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN   OrderedLocusNames=RPD_0525 {ECO:0000313|EMBL:ABE37763.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37763.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37763.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37763.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via
CC       cis-aconitate. {ECO:0000256|RuleBase:RU361275}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate = isocitrate; Xref=Rhea:RHEA:10336,
CC         ChEBI:CHEBI:16087, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC         Evidence={ECO:0000256|RuleBase:RU361275};
CC   -!- COFACTOR:
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|RuleBase:RU361275};
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|RuleBase:RU361275}.
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DR   EMBL; CP000283; ABE37763.1; -; Genomic_DNA.
DR   RefSeq; WP_011500950.1; NC_007958.1.
DR   STRING; 316057.RPD_0525; -.
DR   EnsemblBacteria; ABE37763; ABE37763; RPD_0525.
DR   KEGG; rpd:RPD_0525; -.
DR   eggNOG; ENOG4107QM5; Bacteria.
DR   eggNOG; COG1048; LUCA.
DR   HOGENOM; HOG000025704; -.
DR   KO; K01681; -.
DR   OMA; RDFTQEG; -.
DR   OrthoDB; 363064at2; -.
DR   BioCyc; RPAL316057:RPD_RS02690-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.19.10; -; 1.
DR   Gene3D; 3.30.499.10; -; 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; IPR006249; Aconitase/IRP2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   PANTHER; PTHR11670; PTHR11670; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR01341; aconitase_1; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13DS6.
DR   SWISS-2DPAGE; Q13DS6.
KW   4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Iron {ECO:0000256|RuleBase:RU361275};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU361275};
KW   Lyase {ECO:0000256|RuleBase:RU361275, ECO:0000313|EMBL:ABE37763.1};
KW   Metal-binding {ECO:0000256|RuleBase:RU361275}.
FT   DOMAIN       73    569       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   DOMAIN      699    831       Aconitase_C. {ECO:0000259|Pfam:PF00694}.
SQ   SEQUENCE   905 AA;  98202 MW;  78B985A195D4E7C1 CRC64;
     MTSLDSFKCR KILKVGSKSY VYYSLPTAEK NGLKGISRLP YSMKVLLENL LRNEDDRTVK
     KADIQAVAKW MRKKALEHEI AFRPARVLMQ DFTGVPAVVD LAAMRNAMQA LGGDAEKINP
     LVPVDLVIDH SVIVNFFGDN KAFGKNVAEE YKQNQERYEF LKWGQKAFSN FAVVPPGTGI
     CHQVNLEYLA QTVWTRKEKM TIGKKKGTFE VAYPDSLVGT DSHTTMVNGL AVLGWGVGGI
     EAEAAMLGQP LSMLLPEVVG FKLKGALKEG VTATDLVLTV TQMLRKQGVV GKFVEFFGPG
     LDHLSVADKS TIANMAPEYG ATCGFFPVDT ETLDYLKTSG RASARVALVE KYAKAQGLFR
     TAKSADPVFT VTLTLDLASV VPSLAGPKRP EGRVALPAVS EGFTAAMDAE YKKALDGARY
     AVDGRKFDLG HGDVVIAAIT SCTNTSNPSV LIGAGLLARN AAAKGLKAAP WVKTSLAPGS
     QVVAEYLANS GLQKDLDKVG FNLVGFGCTT CIGNSGPLPE DISKSINDNG IVAAAVLSGN
     RNFEGRVSPD VQANYLASPP LVVAYALAGT VTKNLAVEPI GTGKDGKPVY LKDIWPTTKE
     INAFVKKYVT AAIFKKKYAD VFKGDTNWRK IKTVDSETYK WNMSSTYVQN PPYFEGMKMQ
     PEPIVDVVDA RILAVFGDKI TTDHISPAGS IKLTSPAGKY LSEHQVRPAD FNQYGTRRGN
     HEVMMRGTFA NIRIKNHMLK GADGNIPEGG LTKHWPDGDQ MSIYDAAMKY QAEQVPLVVF
     AGAEYGNGSS RDWAAKGTRL LGVRAVICQS FERIHRSNLV GMGVLPLTFE DGTSWASLGI
     KGDEKVTIRG LQGDLKPRQT LTAEIKAGNG KVKRVPLLCR IDTLDELEYY RNGGILHYVL
     RKLAA
//

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