(data stored in SCRATCH zone)

SWISSPROT: Q13S47_PARXL

ID   Q13S47_PARXL            Unreviewed;       905 AA.
AC   Q13S47;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 86.
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   ORFNames=Bxe_B2903 {ECO:0000313|EMBL:ABE33092.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33092.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33092.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33092.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via
CC       cis-aconitate. {ECO:0000256|RuleBase:RU361275}.
CC   -!- CATALYTIC ACTIVITY: Citrate = isocitrate.
CC       {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; CP000271; ABE33092.1; -; Genomic_DNA.
DR   RefSeq; WP_011490476.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13S47; -.
DR   STRING; 266265.Bxe_B2903; -.
DR   EnsemblBacteria; ABE33092; ABE33092; Bxe_B2903.
DR   GeneID; 4006732; -.
DR   KEGG; bxb:DR64_5233; -.
DR   KEGG; bxe:Bxe_B2903; -.
DR   PATRIC; fig|266265.5.peg.4784; -.
DR   eggNOG; ENOG4108I0Z; Bacteria.
DR   eggNOG; COG1048; LUCA.
DR   HOGENOM; HOG000025703; -.
DR   KO; K01681; -.
DR   OMA; MRIIPPG; -.
DR   OrthoDB; POG091H08NL; -.
DR   Proteomes; UP000001817; Chromosome 2.
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   GO; GO:0008152; P:metabolic process; 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; IPR006249; Aconitase/IRP2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
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; SSF52016; SSF52016; 1.
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; Q13S47.
DR   SWISS-2DPAGE; Q13S47.
KW   4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Iron {ECO:0000256|RuleBase:RU361275};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU361275};
KW   Lyase {ECO:0000256|RuleBase:RU361275, ECO:0000256|SAAS:SAAS00638284,
KW   ECO:0000313|EMBL:ABE33092.1};
KW   Metal-binding {ECO:0000256|RuleBase:RU361275};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       69    566       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   DOMAIN      697    829       Aconitase_C. {ECO:0000259|Pfam:PF00694}.
SQ   SEQUENCE   905 AA;  98407 MW;  C67D64D34585C73E CRC64;
     MAHNLHKTLK EFDSGSGKGK FYSLPQLGRA LDIKIDRLPV SIRIVLESVL RNYDGKKIAE
     EHIEQLANWK PTASRVDEIP FVVSRVVLQD FTGVPLLADI AAMRGVAKHM GKDPKSIEPL
     VPVDLVVDHS VQIDHFREKN ALDLNMKLEF QRNNERYQFM KWGMQAFDTF KVVPPGVGIV
     HQVNLEYLAR GVHKKAEGAD TVYYPDSLVG TDSHTTMING IGVVGWGVGG IEAEAGMLGQ
     PVYFLTPDVV GVNLKGKLRE GVTATDLVLT ITELLRKEKV VGKFVEFFGE GTRSLSLPDR
     ATIGNMAPEY GATMGFFPVD EKTIDYFKGT GRTDAEISAF QNYFKAQNLF GIPKEGDIDY
     TKVVTLDLGS VAPSLAGPKR PQDRIEIGNV KATFSDLFSK PVAENGFAKK AEDLEAQYTT
     SNGVDVKNGD VLIAAITSCT NTSNPSVLLA AGLLAKKAVE AGLTVAPHIK TSLAPGSRIV
     TEYLTKTDLM KYLDKLGFTL AAYGCTTCIG NAGDLTPELN EAITKNDIVA AAVLSGNRNF
     EARIHPNIRA NFLASPPLVV AYAIAGNITR DLMTEPVGKG KGGKDIYLGD IWPTSEEVND
     LLKFALDPEA FRKNYSALTK KGDLWSKIEG EEGQVYDWPK STYIAEPPFF GKDFSMTPAD
     SIAAVTNARA LGIFGDSVTT DHISPAGSIK EDSPAGKWLK ENGVQKADFN SYGSRRGNHD
     VMMRGTFANV RIKNLMIPTK ADGSRVEGGL TIHQPSGEQL SIYDAAMKYI EAGTPTIVFA
     GEEYGTGSSR DWAAKGTQLL GVKAVVARSF ERIHRSNLVG MGVLPLQFKG SDSVQSLGIT
     GEETYDIEGL GADFKPQQEV TLVIRGKDGK EKRVQVLLRI DTPIEVDYYK HGGILPFVLR
     SLLAA
//

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