ACNA_THET8
ID ACNA_THET8 Reviewed; 902 AA.
AC Q5SMF6;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Aconitate hydratase A {ECO:0000303|PubMed:23106124};
DE Short=ACN {ECO:0000303|PubMed:23106124};
DE Short=Aconitase {ECO:0000303|PubMed:23106124};
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=acoA; OrderedLocusNames=TTHA0726;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION, FUNCTION, AND PATHWAY.
RC STRAIN=STI11057;
RX PubMed=23106124; DOI=10.1111/mmi.12076;
RA Fazius F., Shelest E., Gebhardt P., Brock M.;
RT "The fungal alpha-aminoadipate pathway for lysine biosynthesis requires two
RT enzymes of the aconitase family for the isomerization of homocitrate to
RT homoisocitrate.";
RL Mol. Microbiol. 86:1508-1530(2012).
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. Also able to catalyze the hydration of cis-homoaconitate to
CC yield (R)-homocitrate, but with a lower efficiency (PubMed:23106124).
CC Could catalyze the hydration of 2-methyl-cis-aconitate to yield
CC (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-
CC binding regulatory protein (By similarity).
CC {ECO:0000250|UniProtKB:P09339, ECO:0000250|UniProtKB:Q8ZP52,
CC ECO:0000269|PubMed:23106124}.
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:0000305|PubMed:23106124}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305|PubMed:23106124}.
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; AP008226; BAD70549.1; -; Genomic_DNA.
DR RefSeq; WP_011228149.1; NC_006461.1.
DR RefSeq; YP_143992.1; NC_006461.1.
DR AlphaFoldDB; Q5SMF6; -.
DR SMR; Q5SMF6; -.
DR STRING; 300852.55772108; -.
DR PRIDE; Q5SMF6; -.
DR EnsemblBacteria; BAD70549; BAD70549; BAD70549.
DR GeneID; 3169911; -.
DR KEGG; ttj:TTHA0726; -.
DR PATRIC; fig|300852.9.peg.719; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_0; -.
DR OMA; NGGIMQY; -.
DR PhylomeDB; Q5SMF6; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000532; 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; IDA:UniProtKB.
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:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; TAS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS: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 3: Inferred from homology;
KW Amino-acid biosynthesis; Iron; Iron-sulfur; Lyase; Lysine biosynthesis;
KW Metal-binding; Reference proteome; RNA-binding; Tricarboxylic acid cycle.
FT CHAIN 1..902
FT /note="Aconitate hydratase A"
FT /id="PRO_0000425285"
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 902 AA; 99768 MW; 4BF9D8F3FBF3EB84 CRC64;
MKNSFQTLKT LTTKSGTYGY YDLQELERKG VAEVSRLPFS IRVMLESLLR NEDGYQVTRE
DIEALARWRP DPGEINVPLK LARVILQDFT GVPAVVDLAA MRDAIKAKGG DPKRINPVVP
ADLVIDHSVQ VDAFGTAYAF FYNVEKEYER NRERYLLLKW AQNALENFRV VPPGTGIVHQ
VNIEYLTKVV MTGKRDGLTL AFPDSLVGTD SHTTMVNGLG VLGWGVGGIE AEAVMLGQPY
YMLAPRVVGF KLYGELPEGA TATDLVLTVT EMLRKHGVVG KFVEFYGPGV AKLSTPDRAT
IANMAPEYGA TMGFFPVDEE TLNYLRQTGR PEELVELVEA YTKAVGLFRT PEAEEKVQYS
EYLELDLSAV EPSLAGPKRP QDRVPLKEVK KSFLAHLTKP VKERGFGLSE DQLQRKVLVK
RRDEEFELTH GSVVIAAITS CTNTSNPSVM LGAGLLAKKA VEAGLDRKPW VKTSLAPGSK
VVTDYLEMSG LMPFLEALGF HLVGYGCTTC IGNSGPLPED IAKAVEEGNL VVAAVLSGNR
NFEGRINPHV KANYLASPML VVAYALAGRM DIDFTTEPLG FDPNGKPIYL KDIWPSMEEI
REAIRKTLDP ELFKKEYSKV FEGDERWQAL PAPTGELYQW DPESTYIQNP PFFEDLGERK
VEDIRGARVL LVLGDSVTTD HISPAGAIPV KSPAGQYLIS KGVKPEDFNS YGSRRGNHEV
MMRGTFANIR IKNLMLDGIE GGYAKKLPEG DVDFVYNVAM RYKAEGTPLL VIAGKEYGTG
SSRDWAAKGT YLLGIRAVLA ESFERIHRSN LVGMGVLPLE FLPGENRETL GLTGYEVYDI
LGLEDLKPRK LVDIVARRED GSEVRFQAIA RLDTPVEVDY YKNGGILQTV LLNMLKEAKA
TE
