ACNA_BRADU
ID ACNA_BRADU Reviewed; 906 AA.
AC P70920;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Aconitate hydratase A {ECO:0000303|PubMed:8892815};
DE Short=ACN {ECO:0000303|PubMed:8892815};
DE Short=Aconitase {ECO:0000303|PubMed:8892815};
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=acnA {ECO:0000303|PubMed:8892815}; OrderedLocusNames=bll0466;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RC STRAIN=USDA 110spc4;
RX PubMed=8892815; DOI=10.1128/jb.178.21.6166-6172.1996;
RA Thoeny-Meyer L., Kuenzler P.;
RT "The Bradyrhizobium japonicum aconitase gene (acnA) is important for free-
RT living growth but not for an effective root nodule symbiosis.";
RL J. Bacteriol. 178:6166-6172(1996).
RN [2]
RP ERRATUM OF PUBMED:8892815.
RA Thoeny-Meyer L., Kuenzler P.;
RL J. Bacteriol. 179:1836-1836(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and probably
CC via the 2-methylcitrate cycle I (propionate degradation route).
CC Catalyzes the reversible isomerization of citrate to isocitrate via
CC cis-aconitate (PubMed:8892815). Could catalyze the hydration of 2-
CC methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form
CC of AcnA functions as a RNA-binding regulatory protein (By similarity).
CC {ECO:0000250|UniProtKB:P09339, ECO:0000250|UniProtKB:Q8ZP52,
CC ECO:0000269|PubMed:8892815}.
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}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P09339}.
CC -!- INDUCTION: Higher under aerobic conditions than under anaerobic
CC conditions. {ECO:0000269|PubMed:8892815}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow more slowly, but
CC also reach a lower cell density than the wild-type. The ability of the
CC mutant to establish an effective root nodule symbiosis with soybean
CC plants is not affected. {ECO:0000269|PubMed:8892815}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; U56817; AAC44562.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC45731.1; -; Genomic_DNA.
DR RefSeq; NP_767106.1; NC_004463.1.
DR RefSeq; WP_011083297.1; NZ_CP011360.1.
DR AlphaFoldDB; P70920; -.
DR SMR; P70920; -.
DR STRING; 224911.27348714; -.
DR EnsemblBacteria; BAC45731; BAC45731; BAC45731.
DR GeneID; 64020325; -.
DR KEGG; bja:bll0466; -.
DR PATRIC; fig|224911.44.peg.8999; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_5; -.
DR InParanoid; P70920; -.
DR OMA; NGGIMQY; -.
DR PhylomeDB; P70920; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000002526; Chromosome.
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; IDA: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 2: Evidence at transcript level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW RNA-binding; Tricarboxylic acid cycle.
FT CHAIN 1..906
FT /note="Aconitate hydratase A"
FT /id="PRO_0000076656"
FT BINDING 443
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 509
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 512
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT CONFLICT 596
FT /note="W -> C (in Ref. 1; AAC44562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 906 AA; 98322 MW; E1A9C4AFA0614104 CRC64;
MTSLDSFKCK KTLKVGAKTY VYYSLPTAEK NGLKGISKLP YSMKVLLENL LRNEDGRSVK
KADIVAVSKW LRKKSLEHEI AFRPARVLMQ DFTGVPAVVD LAAMRNAMQK LGGDAEKINP
LVPVDLVIDH SVIVNFFGDN KAFAKNVTEE YKQNQERYEF LKWGQAAFSN FSVVPPGTGI
CHQVNLEYLS QTVWTKKEKM TVGKKTGTFE VAYPDSLVGT DSHTTMVNGL AVLGWGVGGI
EAEACMLGQP LSMLLPNVVG FKLKGAMKEG VTATDLVLTV TQMLRKLGVV GKFVEFFGPG
LDHLSVADKA TIANMAPEYG ATCGFFPVDA AAIDYLKTSG RAAPRVALVQ AYAKAQGLFR
TAKSADPVFT ETLTLDLADV VPSMAGPKRP EGRIALPSVA EGFSVALANE YKKTEEPAKR
FAVEGKKYEI GHGDVVIAAI TSCTNTSNPS VLIGAGLLAR NAAAKGLKAK PWVKTSLAPG
SQVVAAYLAD SGLQAHLDKV GFNLVGFGCT TCIGNSGPLP EEISKSINDN GIVAAAVLSG
NRNFEGRVSP DVQANYLASP PLVVAHALAG SVTKNLAVEP LGEGKDGKPV YLKDIWPTSK
EINAFMKKFV TASIFKKKYA DVFKGDTNWR KIKTVESETY RWNMSSTYVQ NPPYFEGMKK
EPEPVTDIVE ARILAMFGDK ITTDHISPAG SIKLTSPAGK YLSEHQVRPA DFNQYGTRRG
NHEVMMRGTF ANIRIKNFML KGADGNIPEG GLTKHWPDGE QMSIYDAAMK YQQEQVPLVV
FAGAEYGNGS SRDWAAKGTR LLGVRAVICQ SFERIHRSNL VGMGVLPLTF EEGTSWSSLG
LKGDEKVTLR GLVGDLKPRQ KLTAEIVSGD GSLQRVSLLC RIDTLDELDY YRNGGILHYV
LRKLAA
