(data stored in SCRATCH zone)

SWISSPROT: B8I9G7_METNO

ID   B8I9G7_METNO            Unreviewed;       900 AA.
AC   B8I9G7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 59.
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=Mnod_0174 {ECO:0000313|EMBL:ACL55220.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55220.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55220.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) 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: 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; CP001349; ACL55220.1; -; Genomic_DNA.
DR   RefSeq; WP_015926933.1; NC_011894.1.
DR   ProteinModelPortal; B8I9G7; -.
DR   STRING; 460265.Mnod_0174; -.
DR   EnsemblBacteria; ACL55220; ACL55220; Mnod_0174.
DR   KEGG; mno:Mnod_0174; -.
DR   eggNOG; ENOG4108I0Z; Bacteria.
DR   eggNOG; COG1048; LUCA.
DR   HOGENOM; HOG000025703; -.
DR   KO; K01681; -.
DR   OMA; MRIIPPG; -.
DR   OrthoDB; POG091H08NL; -.
DR   Proteomes; UP000008207; 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   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; B8I9G7.
DR   SWISS-2DPAGE; B8I9G7.
KW   4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Iron {ECO:0000256|RuleBase:RU361275};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU361275};
KW   Lyase {ECO:0000256|RuleBase:RU361275, ECO:0000256|SAAS:SAAS00638284};
KW   Metal-binding {ECO:0000256|RuleBase:RU361275};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207}.
FT   DOMAIN       78    564       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   DOMAIN      694    825       Aconitase_C. {ECO:0000259|Pfam:PF00694}.
SQ   SEQUENCE   900 AA;  97109 MW;  9F7CEBF0674C79CE CRC64;
     MASIDSFKSR QTLQVGSKSY TYYSIAEAEK NGLPDASRLP FSMKVLLENL LRFEDDRSVK
     KADIEAVTAW LGNRGEVETE IAFRPSRVLM QDFTGVPAVV DLAAMRDAMV ALGGDPKKIN
     PLVPVDLVID HSVIVDEFGT PKALADNVAL EYQRNGERYT FLKWGQAAFD NFSVVPPGTG
     ICHQVNLEYL AQTVWTKAFE NGQELAYPDS LVGTDSHTTM VNGLAVLGWG VGGIEAEAAM
     LGQPLSMLIP EVVGFKLSGK LPEGTTATDL VLTVTQMLRK KGVVGKFVEF YGPGLDDMAV
     ADRATISNMA PEYGATCGFF PVDTRTLDYL RVTGRSDERI ALVEAYAKAQ GMWRDAATPD
     PVFTDTLELD LGDVKPSLAG PKRPQDRVLL DSAKPGFAAS METEFRKAAD LAKRYPVEGA
     NFDLGHGDVV IAAITSCTNT SNPSVMIGAG LLARNAIAKG LRSKPWVKTS LAPGSQVVAE
     YLEKAGLQKS LDALGFNLVG FGCTTCIGNS GPLPAPISKA INDNDIVAAA VLSGNRNFEG
     RVNPDVRANY LASPPLVVAY ALAGSLQVDL TRDPIGTGSD GQPVYLKDIW PSSAEVNAFI
     EQTITSSLFK SRYADVFGGD ANWKAVEVTP AQTFSWNSGS TYVQNPPYFV GMQKTPAPVT
     DIVGARILGL FLDSITTDHI SPAGNIRAAS PAGKYLQEHQ VRVQDFNQYG TRRGNHEVMM
     RGTFANIRIK NQMVRDESGN VVEGGWTLYQ PGGEKMFIYD AAMRYQAEGT PLVVFAGKEY
     GTGSSRDWAA KGTKLLGVRA VIAESFERIH RSNLVGMGVV PLVFQGDTTW DSLGLKGDET
     VTIRGLAGDL KPRQTLTAEI TAADGTTKQV PLTCRIDTLD ELEYFRNGGI LPYVLRQLAA
//

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