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Database: UniProt
Entry: A0A1T4KBI2_9GAMM
LinkDB: A0A1T4KBI2_9GAMM
Original site: A0A1T4KBI2_9GAMM 
ID   A0A1T4KBI2_9GAMM        Unreviewed;       870 AA.
AC   A0A1T4KBI2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN   ORFNames=BTE48_05260 {ECO:0000313|EMBL:OPX55974.1};
OS   Oceanospirillum multiglobuliferum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Oceanospirillum.
OX   NCBI_TaxID=64969 {ECO:0000313|EMBL:OPX55974.1, ECO:0000313|Proteomes:UP000191418};
RN   [1] {ECO:0000313|EMBL:OPX55974.1, ECO:0000313|Proteomes:UP000191418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33336 {ECO:0000313|EMBL:OPX55974.1,
RC   ECO:0000313|Proteomes:UP000191418};
RA   Carney J.G., Trachtenberg A.M., Rheaume B.A., Linnane J.D., Pitts N.L.,
RA   Mykles D.L., Maclea K.S.;
RT   "Genome Sequencing of a Marine Spirillum, Oceanospirillum multiglobuliferum
RT   ATCC 33336, from Japan.";
RL   Submitted (JAN-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}.
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:OPX55974.1}.
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DR   EMBL; MTSM01000005; OPX55974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4KBI2; -.
DR   STRING; 64969.SAMN02745127_00011; -.
DR   OrthoDB; 9764318at2; -.
DR   Proteomes; UP000191418; 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:UP000191418}.
FT   DOMAIN          64..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   870 AA;  94834 MW;  7FCC2318D87F51F2 CRC64;
     MNTEYRKSLS GTSLDYFDTR AAVEAIQPGA YATLPYTSRI LAEQLVRRCE PEALTDSLKQ
     LIERKRDLDF PWYPARVVCH DILGQTALVD LAGLRDAIAE QGGDPSKVNP VVPTQLIVDH
     SLAVEAAGFD PDAFEKNRAI EDRRNDDRFH FIEWCKTAFD NVDVIPAGNG IMHQINLEKM
     SPVIQARDGV AFPDTCVGTD SHTPHVDALG VVAIGVGGLE AETVMLGLPS MMRLPDIIGV
     ELVGKRQPGI TATDIVLAIT EFLRNEKVVS AYLEFFGEGA KALSIGDRAT ISNMTPEFGA
     SAGMFYIDEQ TIEYLKLTGR EPEQVALVEQ YAKETGLWAD DLATAEYERV LKFDLSTVVR
     NMAGPSNPHR RLPTSDLASR GIAGDAMLAS AKAEETEGLM PDGAVIIAAI TSCTNTSNPR
     NVVAAGLVAK KANELGLVRK PWVKSSFAPG SKVAKLYLEK AGLLSEMEKL GFGIVAYACT
     TCNGMSGALD PVIEKEIIDR DLYATAVLSG NRNFDGRIHP HAKQAFLASP PLVVAYAIAG
     TIRFDIEKDV LGTDQAGNPV TLKDIWPSDE EIDTLVEQSV TPEQFKQVYI PMFDLGAVER
     SKSPLYDWRP QTTYIRRPPY WEGALAGERT MKGMVPLAVL GDNITTDHLS PSNAIQASSA
     AGEYCAKMGL PEEDFNSYAT HRGDHLTAQR ATFANPKLLN EMCRDENGNV KQGSLARIEP
     EGVESRMWEA IETYMERKQP LIIIAGADYG QGSSRDWAAK GVRLAGVEAI VAEGFERIHR
     TNLVGMGVLP LEFKAGETRM TYGIDGTETY DVVGDLSPRT DLTVVMTRRN GEQVSIPVTC
     RLDTAAEVSV YQAGGVLQRF AKDFLESNAN
//
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