ID   A9HEZ2_GLUDA            Unreviewed;       897 AA.
AC   A9HEZ2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   04-NOV-2026, entry version 103.
DE   RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE            Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE            EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN   Name=acnA {ECO:0000313|EMBL:CAP55298.1};
GN   OrderedLocusNames=GDI1355 {ECO:0000313|EMBL:CAP55298.1};
OS   Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS   / CIP 103539 / LMG 7603 / PAl5).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Acetobacterales; Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP55298.1, ECO:0000313|Proteomes:UP000001176};
RN   [1] {ECO:0000313|EMBL:CAP55298.1, ECO:0000313|Proteomes:UP000001176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 /
RC   PAl5 {ECO:0000313|Proteomes:UP000001176};
RX   PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA   Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A.,
RA   Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA   Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA   Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA   Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA   Figueiredo D., Montano H., Junior J., Filho G., Flores V., Ferreira B.,
RA   Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J.,
RA   Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G.,
RA   Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C.,
RA   Urmenyi T., Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.;
RT   "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT   Gluconacetobacter diazotrophicus Pal5.";
RL   BMC Genomics 10:450-450(2009).
CC   -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC       aconitate. {ECO:0000256|RuleBase:RU361275}.
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:0000256|ARBA:ARBA00002737}.
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:0000256|ARBA:ARBA00000118};
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:0000256|ARBA:ARBA00023501,
CC         ECO:0000256|RuleBase:RU361275};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000256|ARBA:ARBA00005026}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR   EMBL; AM889285; CAP55298.1; -; Genomic_DNA.
DR   RefSeq; WP_012224601.1; NC_010125.1.
DR   AlphaFoldDB; A9HEZ2; -.
DR   KEGG; gdi:GDI1355; -.
DR   OMA; AACNYMD; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000001176; Chromosome.
DR   GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd01586; AcnA_IRP; 1.
DR   CDD; cd01580; AcnA_IRP_Swivel; 1.
DR   FunFam; 3.20.19.10:FF:000001; Aconitate hydratase; 1.
DR   FunFam; 3.30.499.10:FF:000002; Aconitate hydratase; 1.
DR   FunFam; 3.30.499.10:FF:000020; Aconitate hydratase A; 1.
DR   Gene3D; 6.10.190.10; -; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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   NCBIfam; NF006757; acnA; 1.
DR   NCBIfam; NF009520; acnA; 1.
DR   NCBIfam; TIGR01341; aconitase_1; 1.
DR   PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU361275};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361275};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001176};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          79..564
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          695..822
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   897 AA;  97229 MW;  0C7E05AEDC13D092 CRC64;
     MKSVGHDSIK TGRSLHVDGK TYHYFSIPEA EKTIGDVSRL PVSLKVLLEN ILRFEDGRSY
     SVDDARAIAA WLPKGASTKE VPFKPARILM QDFTGVPAVV DLAAMRDGIL KLKGDPQKVN
     PLVPVNLVID HSVMVDVAGT PDALQKNVTI EFERNGERYA FLRWGQEAFE NFSVVPPGTG
     ICHQVNLEYI AQAVWTAHVD GKDYAYPDTL YGTDSHTTMV NGMGVLGWGV GGIEAEAAML
     GQPIAMLIPD VIGFKLVGKL PEGATATDLV LTVTQMLRKK GVVGKFVEFF GPALDHLPVA
     DRATIANMAP EYGATCGFFP VDELTLHYLR QTGRDEHRIK LTEEYLKAQG MFRTAESPEP
     VFTDTLELDL STVVPSLAGP KRPQDRVPLT NATSAFETEL TGGLGVPAAD AHKKAKVAGT
     NYEIGHGDVV IAAITSCTNT SNPAVLIAAG LVAKKARALG LKPKPWVKTS LAPGSQVVTD
     YLNRAGLTEE LDAMGFNTVG YGCTTCIGNS GPLEDHIVDA IEGNKLVAVS VLSGNRNFEG
     RISPNVRANY LASPPLVVAY SLLGTMREDI TTAPLGTSKD GKPVYLKDIW PTNKEIAELI
     GSSITREEFI KRYSQISKGT KEWQALKVAT GSETYKWDPS STYVQDPPYF QEITPEPKPK
     GDIVGARVLA LLGDNITTDH ISPAGAIKES SPAGVYLKEH QVSKADFNSY GSRRGNDRIM
     VRGTFANIRI KNEMLPGTEG GLSKHFPDGK EGSIYDVAME YKKEGVPLVV FGGKEYGMGS
     SRDWAAKGTL LLGVRAVVAE SFERIHRSNL VGMGVLPLLF KDGVTRKTLG LKGDEKIDIH
     GLDKITPRMT LTMTITRADG SKEDVPLLCR VDTLDEVEYY RHGGILQYVL RGMTKAA
//