ID   A0A285R5P8_9SPHN        Unreviewed;       875 AA.
AC   A0A285R5P8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN   ORFNames=SAMN06297144_2808 {ECO:0000313|EMBL:SOB87672.1};
OS   Sphingomonas guangdongensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1141890 {ECO:0000313|EMBL:SOB87672.1, ECO:0000313|Proteomes:UP000219494};
RN   [1] {ECO:0000313|EMBL:SOB87672.1, ECO:0000313|Proteomes:UP000219494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12672 {ECO:0000313|EMBL:SOB87672.1,
RC   ECO:0000313|Proteomes:UP000219494};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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; OBMI01000003; SOB87672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285R5P8; -.
DR   OrthoDB; 9764318at2; -.
DR   Proteomes; UP000219494; Unassembled WGS sequence.
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:UP000219494}.
FT   DOMAIN          63..538
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          667..797
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   875 AA;  95496 MW;  3F24FD28267BF408 CRC64;
     MNQAHRQPLS GTPHHYFDTR TAVEAIRSGA YDTLPYVSRV LAEQLVRRCD PALLPAALEQ
     IVERRQDLDF PWYPARVVCH DILGQTALVD LAGLRDAIAA EGGDPAKVNP VVPTQLIVDH
     SLAVEHGGFD PDAIARNREI EDRRNADRFH FIEWTKRAFD NVDVVPAGNG IMHQINLEKM
     SPVIQVQDGV AFPDTCVGTD SHTPHVDALG VIAIGVGGLE AETVMLGRPS MMRLPDIVGV
     ELTGRRTPGI TATDIVLALT EFLRTERVVG AWLEFYGEGA DSLSIGDRAT ISNMCPEYGA
     TAAMFHIDSQ TIDYLLLTGR DPEQVRLVET YAKTAGLWGD QLRTAEYPRV LRFDLSSVER
     TMAGPSNPHR RLPTSALHER GIAKDLEGAR AQEREGLMPD GAVIIAAITS CTNTSNPRNV
     VAAGLVAKKA NAFGLTRKPW VKTSFAPGSR VPSLYLEEAD LLRELEQLGF GIVGFACTTC
     NGMSGALDPV IQQEIVDRDL YTVAVLSGNR NFDGRIHPYA KQAFLASPPL VVAYAIAGTV
     RFDIEKDVLG TTPDGREIRL KDLWPTDEEI DAIVSEHVHA EQFRNIYEPM FARSLHGGAP
     VSPLYDWRPQ STYIRRPPYW DTEGLGALAA SPRTLKGMRP LAILPDNITT DHLSPSNAIL
     PTSAAGEYLT SMGVPEEDYN SYATHRGDHL TAMRATFANP QLVNEMAVVD GAVQKGSLAR
     VEPDGTVMRM WEAIETYLGR RQPLIIIAGA DYGQGSSRDW AAKGVRLAGV EAIVAEGFER
     IHRTNLIGMG VLPCEFTHGT TRLGLKLDGT ETYDVIGTPA PRAELTLVIN RKDGRQEQVP
     VTCRLDTAEE VSIYTAGGVL QRFAEDFLAS EAAAA
//