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Database: UniProt
Entry: G7UVU4_PSEUP
LinkDB: G7UVU4_PSEUP
Original site: G7UVU4_PSEUP 
ID   G7UVU4_PSEUP            Unreviewed;       871 AA.
AC   G7UVU4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN   Name=acnA {ECO:0000313|EMBL:AER56413.1};
GN   OrderedLocusNames=DSC_08815 {ECO:0000313|EMBL:AER56413.1};
OS   Pseudoxanthomonas spadix (strain BD-a59).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER56413.1, ECO:0000313|Proteomes:UP000005870};
RN   [1] {ECO:0000313|EMBL:AER56413.1, ECO:0000313|Proteomes:UP000005870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD-a59 {ECO:0000313|EMBL:AER56413.1,
RC   ECO:0000313|Proteomes:UP000005870};
RX   PubMed=22207748; DOI=10.1128/JB.06436-11;
RA   Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT   "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT   spadix BD-a59.";
RL   J. Bacteriol. 194:544-544(2012).
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185}.
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DR   EMBL; CP003093; AER56413.1; -; Genomic_DNA.
DR   RefSeq; WP_014160589.1; NC_016147.2.
DR   AlphaFoldDB; G7UVU4; -.
DR   STRING; 1045855.DSC_08815; -.
DR   KEGG; psd:DSC_08815; -.
DR   eggNOG; COG1048; Bacteria.
DR   HOGENOM; CLU_013476_2_1_6; -.
DR   OrthoDB; 9764318at2; -.
DR   Proteomes; UP000005870; Chromosome.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
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; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   NCBIfam; TIGR02333; 2met_isocit_dHY; 1.
DR   PANTHER; PTHR11670:SF43; 2-METHYLCITRATE DEHYDRATASE (2-METHYL-TRANS-ACONITATE FORMING); 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.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005870}.
FT   DOMAIN          66..540
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          664..795
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   871 AA;  94638 MW;  F167BDA94F31343E CRC64;
     MNSAFRKPLP GTDLDYFDAR AAVEALQPGA WDTLPYTSRV HAENLVRRCD PALLDDALQQ
     LIQRRRDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAS QGGDPAQVNP VVPTQLIVDH
     SLAVEYAGFD RNAFAKNRAV EDRRNEDRFH FIDWTSRAFK NVDVIPPGNG IMHQINLERM
     SPVVHAVDGV AYPDTLVGTD SHTPHVDALG VIAIGVGGLE AESVMLGRAS WMRLPDIIGV
     ELTGRPQPGI TATDVVLALT EFLRKEKVVG AYLEFFGQGA DALTIGDRAT ISNMTPEFGA
     TAAMFYIDQQ TIDYLRLTGR EDAQVKLVQT YAKAAGLWAD ALKTAQYERV LRFDLSSVVR
     NMAGPSNPHR RVATTELAAR GIADEAKLEA GKAEQAKGLM PDGAVIIAAI TSCTNTSNPR
     NVIAAGLLAR NANARGLTRK PWVKSSLAPG SKAVQLYLED AKLLSELEQL GFGIVAFACT
     TCNGMSGALD PAIQQEIIDR DLYATAVLSG NRNFDGRIHP YAKQAFLASP PLVVAYAIAG
     TVRFDIEKDV LGLDQAGNPV TLKDIWPSDA QIDAIVAQSV KPEHFRRVYD PMFARTAHSG
     ARIDPLYAWR PRSTYIRRPP YWEGALAGAR TLRGMRPLAV LGDNITTDHL SPSNAILPDS
     AAGEYLAKMG VPEEDFNSYA THRGDHLTAQ RATFANPKLI NEMAVVDGQV KQGSLARIEP
     EGKVTRMWEA IETYMARKQP LIIIAGADYG QGSSRDWAAK GVRLAGVEAI VAEGFERIHR
     TNLVGMGVLP LEFKPGTDRK TLGIDGTETF DVVGTPTPRA DLTLVIHRKD GSQQQVAVTC
     RLDTAEEVAI YEAGGVLQRF AQDFLASSKA A
//
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