(data stored in SCRATCH zone)

SWISSPROT: A8FQC8_SHESH

ID   A8FQC8_SHESH            Unreviewed;       865 AA.
AC   A8FQC8;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 81.
DE   RecName: Full=Aconitate hydratase B {ECO:0000256|PIRNR:PIRNR036687};
DE            EC=4.2.1.3 {ECO:0000256|PIRNR:PIRNR036687};
DE            EC=4.2.1.99 {ECO:0000256|PIRNR:PIRNR036687};
DE   AltName: Full=2-methylisocitrate dehydratase {ECO:0000256|PIRNR:PIRNR036687};
GN   OrderedLocusNames=Ssed_0438 {ECO:0000313|EMBL:ABV35051.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35051.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35051.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35051.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate =
CC       (Z)-but-2-ene-1,2,3-tricarboxylate + H(2)O.
CC       {ECO:0000256|PIRNR:PIRNR036687}.
CC   -!- CATALYTIC ACTIVITY: Citrate = isocitrate.
CC       {ECO:0000256|PIRNR:PIRNR036687}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036687-1};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|PIRSR:PIRSR036687-1};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       isocitrate from oxaloacetate: step 2/2.
CC       {ECO:0000256|PIRNR:PIRNR036687}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|PIRNR:PIRNR036687}.
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DR   EMBL; CP000821; ABV35051.1; -; Genomic_DNA.
DR   RefSeq; WP_012140788.1; NC_009831.1.
DR   ProteinModelPortal; A8FQC8; -.
DR   STRING; 425104.Ssed_0438; -.
DR   EnsemblBacteria; ABV35051; ABV35051; Ssed_0438.
DR   KEGG; sse:Ssed_0438; -.
DR   eggNOG; ENOG4107QIJ; Bacteria.
DR   eggNOG; COG1049; LUCA.
DR   HOGENOM; HOG000205991; -.
DR   KO; K01682; -.
DR   OMA; QDTTGAM; -.
DR   OrthoDB; POG091H05IO; -.
DR   BioCyc; SSED425104:GH7Q-460-MONOMER; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd01576; AcnB_Swivel; 1.
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; IPR004406; Aconitase_B.
DR   InterPro; IPR015933; Aconitase_B_HEAT-like_dom.
DR   InterPro; IPR015929; Aconitase_B_swivel.
DR   PANTHER; PTHR43160:SF3; PTHR43160:SF3; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF06434; Aconitase_2_N; 1.
DR   Pfam; PF11791; Aconitase_B_N; 1.
DR   PIRSF; PIRSF036687; AcnB; 1.
DR   SUPFAM; SSF52016; SSF52016; 1.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   SUPFAM; SSF74778; SSF74778; 1.
DR   TIGRFAMs; TIGR00117; acnB; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQC8.
DR   SWISS-2DPAGE; A8FQC8.
KW   4Fe-4S {ECO:0000256|PIRSR:PIRSR036687-1,
KW   ECO:0000256|SAAS:SAAS00640307};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Iron {ECO:0000256|PIRSR:PIRSR036687-1};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR036687-1};
KW   Lyase {ECO:0000256|PIRNR:PIRNR036687, ECO:0000256|SAAS:SAAS00638284};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036687-1};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR036687}.
FT   DOMAIN        4    156       Aconitase_B_N. {ECO:0000259|Pfam:
FT                                PF11791}.
FT   DOMAIN      168    382       Aconitase_2_N. {ECO:0000259|Pfam:
FT                                PF06434}.
FT   DOMAIN      472    818       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   REGION      244    246       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   REGION      414    416       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   METAL       710    710       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR036687-1}.
FT   METAL       769    769       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR036687-1}.
FT   METAL       772    772       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR036687-1}.
FT   BINDING     191    191       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   BINDING     498    498       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   BINDING     791    791       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   BINDING     796    796       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
SQ   SEQUENCE   865 AA;  93978 MW;  5613BCD1394A6B89 CRC64;
     MLEAYRKHVE ERASEGVVPK PLDAHQVAEL VELVKNPPAG EEEFILDLLE NRIPPGVDEA
     AYVKAGFLDA VAKGEAKSSI LSSARAVELL GTMLGGYNIQ PLIAQLDVAE QAPLAVTALS
     KTLLMFDAFH DVAEKMQAGN EFAKQVVHSW AEAQWFLNRP KLEEKISLTV FKVSGETNTD
     DLSPAPDAWS RPDIPLHALA MLKNTREGIV PDEAGVIGPI KEIDQLKTKG FPLVYVGDVV
     GTGSSRKSAT NSVLWFMGDD IPNVPNKRAG GFCLGGKIAP IFFNTMEDAG ALPIELDVSK
     MNMGDVIDIY PYQGVVKRHD SDEVISEFAL KTDVLMDEVR AGGRIPLIIG RGLTARAREV
     LKLEASTVFV LPQDVADTGK GYTLAQKMVG KACGVTGIRP GQYCEPKMTS VGSQDTTGPM
     TRDELKDLAC LGFSADLTMQ SFCHTAAYPK PVDVNTHHTL PDFIMNRGGV SLRPGDGVIH
     SWLNRMLLPD TVGTGGDSHT RFPLGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGEM
     QPGITLRDLV HAIPHKAIEL GLLTVEKQGK INFFSGRVLE IEGLESLKVE QAFELSDASA
     ERSAAGCSIK LDKEPVIEYL NSNIVMLKWM IAEGYGDRRT IERRIIAMQE WLENPELMEA
     DSDAEYAAVI EIDLNDIKEP ILCAPNDPDD AVLLSEVKDT KIDEVFVGSC MTNIGHFRAT
     GKMLDKFATT LPTRLWITPP TKMDRDQLTE EGYYAIFGRV GARVEIPGCS LCMGNQARVA
     DGATVVSTST RNFPNRLGTG ANVYLASAEL AAVAALLGRL PSSDEYQEYA KQLDATAADT
     YRYLNFDKMS SYTEKAGEVI FQSAV
//

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