ACNA_FRATH
ID ACNA_FRATH Reviewed; 937 AA.
AC Q2A1K3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Aconitate hydratase A {ECO:0000250|UniProtKB:Q8ZP52};
DE Short=ACN {ECO:0000250|UniProtKB:Q8ZP52};
DE Short=Aconitase {ECO:0000250|UniProtKB:Q8ZP52};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:Q8ZP52};
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=FTL_1772;
OS Francisella tularensis subsp. holarctica (strain LVS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=376619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVS;
RA Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S.,
RA Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R.,
RA Garcia E.;
RT "Complete genome sequence of Francisella tularensis LVS (Live Vaccine
RT Strain).";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and probably
CC the 2-methylcitrate cycle I (propionate degradation route). Catalyzes
CC the reversible isomerization of citrate to isocitrate via cis-
CC aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to
CC yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a
CC RNA-binding regulatory protein. {ECO:0000250|UniProtKB:P09339,
CC ECO:0000250|UniProtKB:Q8ZP52}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:Q8ZP52};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000250|UniProtKB:Q8ZP52};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P09339};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P09339};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:Q8ZP52}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000250|UniProtKB:Q8ZP52}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P09339}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AM233362; CAJ80211.1; -; Genomic_DNA.
DR RefSeq; WP_003017291.1; NZ_CP009694.1.
DR AlphaFoldDB; Q2A1K3; -.
DR SMR; Q2A1K3; -.
DR PRIDE; Q2A1K3; -.
DR KEGG; ftl:FTL_1772; -.
DR OMA; NGGIMQY; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
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:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
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; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
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; 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;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; RNA-binding;
KW Tricarboxylic acid cycle.
FT CHAIN 1..937
FT /note="Aconitate hydratase A"
FT /id="PRO_0000235166"
FT REGION 898..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 439
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 505
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 508
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 937 AA; 102704 MW; 3784B39F6F6980C9 CRC64;
MSDIKNITKL QIEDKGKKYS LYSLKKLSQE LGKDVTRLPY SIRVLLENQL RNIDGYKVKE
DDMHKVLDWD AKASSRPEIP HMPARVVMQD FTGVPAVVDL AAMRKAIKDA GGDADKINPL
VDTAMVIDHS VQVDFYGTKT ALAQNVAKEF ERNGERYSLL KWAQKAFDDF IVVPPGMGII
HQVNLEYLAK DALVKNINGE DVIYPDTLVG TDSHTTMING VGAVGWGVGG IEAEAVMLGQ
PYYMVLPDVV GVKFTGKLKT GVTATDLVLK VTEVLRKHGV VGKFVEYYGE GLESLSLPDR
ATIANMTPEY GATIGFFPVD EVTLDFFNNT NRSELVDAAR EMYKEQLLFR ENPAEEPEYS
NIVEIDLSEV ESNLAGPKRP QDRVAFHDMK KAFAEALVHE QGLHGFGLTD EQLQKSAEVK
GLNERITHGS VAIAAITSCT NTSNPSLLLG AGLLAKKANE KGLKVKPFVK TSLAPGSQVV
TQYLEKANLL PELENLGFNL VGYGCTTCIG NSGPLDEPVV EAINEADLIV ASVSSGNRNF
EGRINPHIKA NYLASPIHVV AYALAGTVDF DPVEDAIGKD AEGNDVYLAD IWPTTEEIAA
IQSHVINSDM FKKAYATVLD GTEEWQKLKA PEGKLYEFDS SSTYIQCPNF FEKFAEGNDD
LDIKGARTLL MLGDSVTTDH ISPAGAIPEE YPAGQYLKSH GVEKKDFNSY GSRRGNHEVM
MRGTFANIRI RNLLLDNVEG GFTKYHLDGS QQYVFDAAMK YKEKGIPLVI LAGKEYGTGS
SRDWAAKGTF LLGVKAVIAE SYERIHRSNL VGMGVLPLEY VNGQNAKTLG LDGTEMFNIK
NLNNIKPRQI VIVEAVHPKT AHTTTFEALA RLDADVDVDY LKNGGILQTV LKDIMGDKKE
SKSTQSTTSK GCGSADTSSE TSCPFAKIAN FFKKLFK
