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Database: UniProt
Entry: W7Q5V3_9GAMM
LinkDB: W7Q5V3_9GAMM
Original site: W7Q5V3_9GAMM 
ID   W7Q5V3_9GAMM            Unreviewed;       871 AA.
AC   W7Q5V3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN   ORFNames=Q427_19855 {ECO:0000313|EMBL:EWH00398.1};
OS   Halomonas sp. BC04.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1403540 {ECO:0000313|EMBL:EWH00398.1, ECO:0000313|Proteomes:UP000019279};
RN   [1] {ECO:0000313|EMBL:EWH00398.1, ECO:0000313|Proteomes:UP000019279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC04 {ECO:0000313|EMBL:EWH00398.1,
RC   ECO:0000313|Proteomes:UP000019279};
RA   Farooqui S., Greene A.C., Patel B.K.;
RT   "Draft Genome Sequence of Halomonas Strain BC04, an Aromatic-degrading
RT   moderate Halophilic Bacterium.";
RL   Submitted (DEC-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EWH00398.1}.
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DR   EMBL; AZQX01000234; EWH00398.1; -; Genomic_DNA.
DR   RefSeq; WP_043515814.1; NZ_AZQX01000234.1.
DR   AlphaFoldDB; W7Q5V3; -.
DR   PATRIC; fig|1403540.3.peg.3717; -.
DR   OrthoDB; 9764318at2; -.
DR   Proteomes; UP000019279; 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:UP000019279}.
FT   DOMAIN          66..538
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          661..793
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   871 AA;  95713 MW;  CA50EF99C1F20E0A CRC64;
     MNTDYRKPLP GTELDYFDVR AAVDAIQPGA YDTLPYTSRV LAEQLVRRCE PELLTDALKQ
     LIERRRDLDF PWYPARVVCH DILGQTALVD LAGLRDAIAE QGGDPAKVNP VVPTQLIVDH
     SLAVEHAGFD PDAFDKNRVI EDRRNEDRFH FIEWTKTAFE NVDVIPAGNG IMHQINLEKM
     SPVVQARDGV AYPDTCVGTD SHTPHIDCLG VIAIGVGGLE AETVMLGRPS MMRLPDIVGV
     ELTGKPKPGI TATDIVLAIT EFLRRERVVG AYLEFFGEGA KSLTIGDRAT ISNMTPEYGA
     SAAMFYIDEQ TLDYLTLTGR EPEQVALVET YAKQTGLWAD SLVDAQYERV LTFDLSSVER
     NLAGPSNPHR RLPTSALHER GIAVNYDKAQ AEEKAGRMPD GAVIIAAITS CTNTSNPRNV
     VGAALLAKKA NELGLIRKPW VKSSFAPGSK VARLYLEEAG LLSELEKLGF GIVAYACTTC
     NGMSGALDPK IQQEIIDRDL YATAVLSGNR NFDGRIHPYA KQAFLASPAL VVAYAIAGTV
     RFDIEKDVLG IDHNGNPVTL KDLWPSDEEI DAIVGEFVKP EQFKQVYIPM FDLDAAERAE
     SPLYDWRPQS TYIRRPPYWE GNMAAVRALK GMRPLAILPD NITTDHLSPS NAIMMDSAAG
     EYLHKMGLPE EDFNSYATHR GDHLTALRAT LANPKLFNEM VRDESGEVVQ GSLARIEPEG
     EVTRMWEAIE TYMERKQPLI VIAGADYGQG SSRDWAAKGV ALAGVEAIVA EGFERIHRTN
     LIGMGVMPLQ FREGTTRHTL QLDGTETYDV EGEASPGATL ELVIHRKTGE VDRVPVTCRL
     DTAEEVTVYS AGGVLQRFAK DFLESKGEAV S
//
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