ACNA_DEIRA
ID ACNA_DEIRA Reviewed; 906 AA.
AC Q9RTN7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
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};
DE Flags: Precursor;
GN Name=acn; OrderedLocusNames=DR_1720;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP PROTEIN SEQUENCE OF 3-19.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15249204; DOI=10.1016/j.bbrc.2004.06.062;
RA Joshi B.S., Schmid R., Altendorf K., Apte S.K.;
RT "Protein recycling is a major component of post-irradiation recovery in
RT Deinococcus radiodurans strain R1.";
RL Biochem. Biophys. Res. Commun. 320:1112-1117(2004).
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; AE000513; AAF11276.1; -; Genomic_DNA.
DR PIR; G75362; G75362.
DR RefSeq; NP_295443.1; NC_001263.1.
DR RefSeq; WP_010888355.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RTN7; -.
DR SMR; Q9RTN7; -.
DR STRING; 243230.DR_1720; -.
DR EnsemblBacteria; AAF11276; AAF11276; DR_1720.
DR KEGG; dra:DR_1720; -.
DR PATRIC; fig|243230.17.peg.1931; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_0; -.
DR InParanoid; Q9RTN7; -.
DR OMA; NGGIMQY; -.
DR OrthoDB; 363064at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0030350; F:iron-responsive element binding; IBA:GO_Central.
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:0006101; P:citrate metabolic process; IBA:GO_Central.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Reference proteome; RNA-binding; Tricarboxylic acid cycle.
FT PROPEP 1..2
FT /evidence="ECO:0000269|PubMed:15249204"
FT /id="PRO_0000370734"
FT CHAIN 3..906
FT /note="Aconitate hydratase A"
FT /evidence="ECO:0000269|PubMed:15249204"
FT /id="PRO_0000370735"
FT BINDING 441
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 507
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 510
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 906 AA; 98002 MW; 64058AB470F010F0 CRC64;
MSDKAMNLFG ARDTLQVPGS DKKLYFYNLN KLQGHDVSRL PVSIKVLLES VLREANDYDV
RREDVETVAG WSATNPEVEI PFKPARVILQ DFTGVPAVVD LAAMRSAMVK LGGDPSKINP
LIPVDLVIDH SVQVDEFGTE FALANNMALE FERNRERYEF LRWGQQAFDN FGVVPPASGI
VHQVNLEYLA KGVQSRAEDD GEVVYPDSLV GTDSHTTMIN GLGIVGWGVG GIEAEAVMLG
QPIYMLMPEV IGFKITGAMP EGATATDLAL RVTQMLREKG VVGKFVEFYG AGLSNMTLPD
RATIANMAPE YGATMGFFPV DDEALRYLRR TGRLEDEIGL VEAYYKAQGM FRTDETPDPV
FTDTIELDLA TIVPSLAGPK RPQDRVNLSD MHSVFNEALT APVKNRGFEL GSDKLDAQGT
IGGTDIKIGH GAVTLASITS CTNTSNPSVL IAAGLVAKKA VEKGLKTKPW VKTSLAPGSR
VVTEYLETAG LQQYLDQIGF NTVGYGCMTC IGNSGPLPEP VVEAIQEGDL VVASVLSGNR
NFEGRVNPHI KANYLASPPL VVAYALAGTV VNDIVNDAIG QDSNGQDVFL KDIWPTNAEI
QEAMDRSINA EMFKKVYDGI EKSNADWNAI PVAEGALFDW KEDSTYIQNP PFFDTLAGGA
HEIESIKGAR ALVKVGDSVT TDHISPAGSF KADTPAGRYL TERGIAPKDF NSYGSRRGND
RIMTRGTFAN IRLKNQLAPG TEGGFTTNFL NGEVTSIFDA STAYKEAGVP LVVLAGKDYG
MGSSRDWAAK GTFLLGVKAV IAESFERIHR SNLVGMGVLP LQYKNGETAD SLGINGDETF
EFVLPGDLKP RQDVTVKVTG KDGNTRDITV MCRIDTPVEI DYYKNGGILQ TVLRGILSKS
QGEVKA
