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Database: UniProt
Entry: Q4JVM4
LinkDB: Q4JVM4
Original site: Q4JVM4 
ID   ACNA_CORJK              Reviewed;         936 AA.
AC   Q4JVM4;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   22-JUL-2015, entry version 74.
DE   RecName: Full=Aconitate hydratase A {ECO:0000250|UniProtKB:Q8NQ98};
DE            Short=ACN {ECO:0000250|UniProtKB:Q8NQ98};
DE            Short=Aconitase {ECO:0000250|UniProtKB:Q8NQ98};
DE            EC=4.2.1.3 {ECO:0000250|UniProtKB:Q8NQ98};
DE   AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE   AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE   AltName: Full=Iron-responsive protein-like {ECO:0000250|UniProtKB:P09339};
DE            Short=IRP-like {ECO:0000250|UniProtKB:P09339};
DE   AltName: Full=Probable 2-methyl-cis-aconitate hydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE            EC=4.2.1.99 {ECO:0000250|UniProtKB:Q8ZP52};
DE   AltName: Full=RNA-binding protein {ECO:0000250|UniProtKB:P09339};
GN   Name=acn; OrderedLocusNames=jk0969;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B.,
RA   Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T.,
RA   Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P.,
RA   Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant
RT   nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring
RT   bacterium of the human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
CC   -!- FUNCTION: Involved in the catabolism of short chain fatty acids
CC       (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route)
CC       and probably via the 2-methylcitrate cycle I (propionate
CC       degradation route). Catalyzes the reversible isomerization of
CC       citrate to isocitrate via cis-aconitate. Could catalyze the
CC       hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-
CC       methylisocitrate. The apo form of AcnA functions as a RNA-binding
CC       regulatory protein. {ECO:0000250|UniProtKB:P09339,
CC       ECO:0000250|UniProtKB:Q8NQ98, ECO:0000250|UniProtKB:Q8ZP52}.
CC   -!- CATALYTIC ACTIVITY: Citrate = isocitrate.
CC       {ECO:0000250|UniProtKB:Q8NQ98}.
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:0000250|UniProtKB:Q8ZP52}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q8NQ98};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:Q8NQ98};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       isocitrate from oxaloacetate: step 2/2.
CC       {ECO:0000250|UniProtKB:Q8NQ98}.
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000250|UniProtKB:Q8NQ98}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8NQ98}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; CR931997; CAI37133.1; -; Genomic_DNA.
DR   RefSeq; WP_011273549.1; NC_007164.1.
DR   ProteinModelPortal; Q4JVM4; -.
DR   STRING; 306537.jk0969; -.
DR   PRIDE; Q4JVM4; -.
DR   EnsemblBacteria; CAI37133; CAI37133; jk0969.
DR   GeneID; 3432029; -.
DR   KEGG; cjk:jk0969; -.
DR   PATRIC; 21512848; VBICorJei31838_0980.
DR   eggNOG; COG1048; -.
DR   HOGENOM; HOG000025704; -.
DR   KO; K01681; -.
DR   OMA; DREIQYR; -.
DR   OrthoDB; EOG67DPHM; -.
DR   BioCyc; CJEI306537:GJ8V-1004-MONOMER; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000000545; Chromosome.
DR   GO; GO:0047456; F:2-methylisocitrate dehydratase activity; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0003994; F:aconitate hydratase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
DR   Gene3D; 3.20.19.10; -; 1.
DR   Gene3D; 3.30.499.10; -; 3.
DR   Gene3D; 3.40.1060.10; -; 1.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR015937; Acoase/IPM_deHydtase.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR015934; Aconitase/AcnD.
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   PANTHER; PTHR11670:SF1; PTHR11670:SF1; 1.
DR   Pfam; PF00330; Aconitase; 2.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF52016; SSF52016; 1.
DR   SUPFAM; SSF53732; SSF53732; 2.
DR   TIGRFAMs; TIGR01341; aconitase_1; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding;
KW   Reference proteome; RNA-binding; Tricarboxylic acid cycle.
FT   CHAIN         1    936       Aconitate hydratase A.
FT                                /FTId=PRO_0000076660.
FT   METAL       472    472       Iron-sulfur (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P36683}.
FT   METAL       538    538       Iron-sulfur (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P36683}.
FT   METAL       541    541       Iron-sulfur (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P36683}.
SQ   SEQUENCE   936 AA;  101295 MW;  55B605AD2F117308 CRC64;
     MAESINSFDS KSTLQVGEKS YDYFALDAVP GMEKLPYSLK VLGENLLRNE DGKNITREHI
     EAIANWDPSA EPNFEIQFTP ARVIMQDFTG VACIVDLATI RDAVVALGGD ADDVNPLNPA
     EMVIDHSVII EAFGDSDALE KNVEIEYQRN DERYKFLRWG TGAFENFRVV PPGTGIVHQV
     NIEYLARSVF DNNGLAYPDT CVGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPISMLIP
     RVVGFKLTGE IPTGVTATDV VLTITDMLRQ HGVVGKFVEF YGKGVGELPL ANRATIGNMS
     PEFGSTAAMF PIDEETVKYL ELTGRDQETL ERVEAYAKAQ GMWLDPEKEV EYSEYLELDL
     STVVPSIAGP KRPQDRIELN DSKAQFRKDL HNYVEADASA VTPDFDAEGP ATENTSAQTA
     GTPASAADAK GNIPSAAAGA EGRPSNPVTV NYNGEDIELD HGMVAIASIT SCTNTSNPSV
     MVGAGLLARN AAAKGLKSAP WVKTSMAPGS QVVNGYYEKA GLWKDLEAMG FYLVGYGCTT
     CIGNSGPLPE EISAGINEGD LAATAVLSGN RNFEGRINPD VKMNYLASPI LVIAYAIAGT
     MDFDFETQPL GQDQDGNDVF LKDIWPSTED IEEVIASSIT KDLYAEDYAN VFEGDERWRS
     LDVPSGKTFD WDPKSTYIRK APYFDGMSKE PEAVNDVKGA RVLALLGDSV TTDHISPAST
     IKPGTPAAQY LDANGVERKD YNSLGARRGN HEVMVRGTFA NIRLQNQLLD GVSGGYTRDF
     TQEGGPQSFI YDAAMNYQKE NTPLVVLGGK EYGTGSSRDW AAKGTLLLGV KAVIAESFER
     IHRSNLIGMG VVPLQFPEGE SWKSLGIEGT ETFDIEGIEE LNNGSTPKTV KVTATKENGE
     KIEFDAVTRI DTPGEADYYR NGGILQFVLR NMMSGK
//
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