(data stored in SCRATCH zone)

SWISSPROT: Q3IJ30_PSEHT

ID   Q3IJ30_PSEHT            Unreviewed;       880 AA.
AC   Q3IJ30;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 98.
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   Name=acnB {ECO:0000313|EMBL:CAI85287.1};
GN   OrderedLocusNames=PSHAa0184 {ECO:0000313|EMBL:CAI85287.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85287.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85287.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85287.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q3IJ30; -.
DR   STRING; 326442.PSHAa0184; -.
DR   EnsemblBacteria; CAI85287; CAI85287; PSHAa0184.
DR   KEGG; pha:PSHAa0184; -.
DR   eggNOG; ENOG4107QIJ; Bacteria.
DR   eggNOG; COG1049; LUCA.
DR   HOGENOM; HOG000205991; -.
DR   KO; K01682; -.
DR   OMA; QDTTGAM; -.
DR   OrthoDB; POG091H05IO; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000006843; Chromosome I.
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; Q3IJ30.
DR   SWISS-2DPAGE; Q3IJ30.
KW   4Fe-4S {ECO:0000256|PIRSR:PIRSR036687-1,
KW   ECO:0000256|SAAS:SAAS00640307};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
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   ECO:0000313|EMBL:CAI85287.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036687-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR036687}.
FT   DOMAIN       19    171       Aconitase_B_N. {ECO:0000259|Pfam:
FT                                PF11791}.
FT   DOMAIN      183    397       Aconitase_2_N. {ECO:0000259|Pfam:
FT                                PF06434}.
FT   DOMAIN      487    833       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   REGION      259    261       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   REGION      429    431       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   METAL       725    725       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR036687-1}.
FT   METAL       784    784       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR036687-1}.
FT   METAL       787    787       Iron-sulfur (4Fe-4S). {ECO:0000256|PIRSR:
FT                                PIRSR036687-1}.
FT   BINDING     206    206       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   BINDING     513    513       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   BINDING     806    806       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
FT   BINDING     811    811       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036687-2}.
SQ   SEQUENCE   880 AA;  95502 MW;  8870DA8ECB1FA2EB CRC64;
     MKRYRILSRH QEGNIVLQEY RKHVEERAAL GIVPAPLDAQ QTADLIELIK TPPAGEEEFI
     LDLFANRVPA GVDDAAYIKA GFLAAVAKGE TNSPLLSKEK AAELLGTMLG GYNIAPMIDL
     LDDDTLAPIV VKGLSNTLLM FDAFYDVEEK AKAGNTFAKQ IIESWANAEW FTNKPAVAEK
     ISVTVFKVTG ETNTDDLSPA PDAWSRPDIP LHALAMLKIE RDGITPDKPG EVGPITQLEE
     LKTKGLPLAY VGDVVGTGSS RKSATNSVLW FMGDDIPFVP NKRVGGVCLG NKIAPIFFNT
     MEDSGALPIE LNVDELNMGE QIDIYPYEGV VKQHGTDKVI SKFELKSEVI LDEVRAGGRI
     PLIIGRGLTD KARTSLGLGA TDIFKVPTAT EVSDKGFTLA QKMVGKACNV AGIRPGQYCE
     PKMTTVGSQD TTGPMTRDEL KDLACLGFSA DLTMQSFCHT SAYPKPIDVN THHTLPDFIM
     NRGGVSLRPG DGIIHSWLNR MLLPDTVGTG GDSHTRFPLG ISFPAGSGAV AFAAATGVMP
     LDMPESILVR FKGEMQPGIT LRDLVHAIPY YGIKQGLLTV EKKGKINEFS GRVLEIEGVE
     HLTVEQAFEL SDASAERSAA GCTVKLSKES ISEYLESNIV MLKWMISEGY GDVRTIERRI
     NAMQDWLANP ELMEADKDAE YAHVVEIDLA EIKEPVLCAP NDPDDARLLS DVAGEKIDEV
     FIGSCMTNIG HFRAAGKLLD GFKGQLPTQL WVAPPTKMDK DQLIEEGYYG IFGRVGARIE
     TPGCSLCMGN QARVADKATV VSTSTRNFPN RLGNGANVFL ASSELAAVAA IIGRLPTAAE
     YQEYAAKINA TASDTYRYLN FHRMPAYTKK ADNVIIQQAV
//

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