ID   A0A090ICL0_9GAMM        Unreviewed;       867 AA.
AC   A0A090ICL0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN   ORFNames=MVIS_1682 {ECO:0000313|EMBL:CED59656.1}, NVI5450_1245
GN   {ECO:0000313|EMBL:SGY91436.1};
OS   Moritella viscosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=80854 {ECO:0000313|EMBL:CED59656.1, ECO:0000313|Proteomes:UP000032438};
RN   [1] {ECO:0000313|Proteomes:UP000032438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hjerde E.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CED59656.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hjerde Erik;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SGY91436.1, ECO:0000313|Proteomes:UP000183794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NVI 5450 {ECO:0000313|EMBL:SGY91436.1};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; LN554852; CED59656.1; -; Genomic_DNA.
DR   EMBL; FPLD01000040; SGY91436.1; -; Genomic_DNA.
DR   RefSeq; WP_045109973.1; NZ_FRDV01000055.1.
DR   STRING; 80854.MVIS_1682; -.
DR   KEGG; mvs:MVIS_1682; -.
DR   PATRIC; fig|80854.5.peg.1790; -.
DR   HOGENOM; CLU_013476_2_1_6; -.
DR   OrthoDB; 9764318at2; -.
DR   Proteomes; UP000032438; Chromosome complete sequence.
DR   Proteomes; UP000183794; 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:UP000032438}.
FT   DOMAIN          63..533
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          662..792
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   867 AA;  94799 MW;  D01AFD5C8D5ED876 CRC64;
     MNINYRKPLP GSELDYFDTR SAVDSIQPGA YATLPYTSRV FAENLVRRCD PEVLEDSLKQ
     LIERKRDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAE KGGDPSKVNP VVPTQLIVDH
     SLAVEHAGFE PDAFEKNRAI EDRRNDDRFH FINWTKTAFK NIDVIPPGNG ILHQINLERM
     SPVIQSRNGV AFPDTLVGTD SHTPMVDALG VIAIGVGGLE AESVMLGRAS YMRLPDIIGV
     ELTGKPPAGM TATDTVLALT EFLRAQKVVS SYLEFYGTGV AHLTLGDRAT ISNMTPEYGA
     TAALFSIDEQ TIDYLKLTGR EDEQVKLVET YAKETGLWAD DLVNVEYERV LTFDLSTVCR
     NIAGPSNPHN RVPTSELAKR GISGKVENIP GKMPDGSVII AAITSCTNTS NPRNMIAAGL
     IARNANKLGL TRKPWVKTSL APGSKAVELY LQEADLLPEL EQLGFGIVAF ACTSCNGMSG
     ALDPVIQQEI LDRDLYATAV LSGNRNFDGR IHPHANEAFI ASPPLVVAYA IAGTIRFDIE
     RDTLGLDQAG NAITLKDIWP SDEEIDAVLK ASVKPEQFRQ VYNPMFGNDI EYSVDYGEKN
     NPLYDWREMS TYIRRPPYWE GALAGERSLK GMRPLAVLGD NITTDHLSPS NAIMLDSAAG
     AYLGKMGLPE VDFNSYATHR GDHLTAQRAT FANPKLNNEM VLENGQVKQG SLARVEPEGN
     VMRMWEAIET YMGRKQSLII VAGADYGQGS SRDWAAKGVR LAGVEAIVAE GFERIHRTNL
     VGMGVLPLEF KTGESRKTYA IDGSETFDVI GEPTPGSSLT LIITRKNGET LEVPVTCRLD
     TAEEVSIYGA GGVLQRFAQD FLESSEA
//