ID   A0A1T5JQ21_9BACT        Unreviewed;       745 AA.
AC   A0A1T5JQ21;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:SKC53547.1};
GN   ORFNames=SAMN06298215_1428 {ECO:0000313|EMBL:SKC53547.1};
OS   Bacteroidales bacterium WCE2008.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1945891 {ECO:0000313|EMBL:SKC53547.1, ECO:0000313|Proteomes:UP000190446};
RN   [1] {ECO:0000313|EMBL:SKC53547.1, ECO:0000313|Proteomes:UP000190446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCE2008 {ECO:0000313|EMBL:SKC53547.1,
RC   ECO:0000313|Proteomes:UP000190446};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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; FUZM01000004; SKC53547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5JQ21; -.
DR   STRING; 1945891.SAMN06298215_1428; -.
DR   OrthoDB; 9764318at2; -.
DR   Proteomes; UP000190446; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR015932; Aconitase_dom2.
DR   PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR   PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00330; Aconitase; 1.
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:UP000190446}.
FT   DOMAIN          38..468
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
SQ   SEQUENCE   745 AA;  81156 MW;  446E5905255F408E CRC64;
     MVDLINHGVY LLDGVVSDAA PGLPSPDEAR ENTITYGILR SHDVDGGKGK KMRIRFDAMV
     SHDITYVGII QTARASGLEK FPLPYAMTNC HNSLCAVGGT INEDDHVFGL SAAKKYGGIY
     VPANQAVIHQ YAREALAKCG NMILGSDSHT RYGSLGNMGV GEGGGELVKQ LLRNTWDINA
     PEVVLVWLEG TPRHGIGPHD VAISLVKAVF ENGFVKNKVL EFAGPGVASL PIDFRNGIDV
     MTTETTCLSS IWITDEKVRE YYEMHGRAAD YKKLEPGKVA YYDSMIRIDL STQESMIALP
     FHPSNAYTIH ELQADPERIL RAVEEDARKR FGDKISIDLL SKIHDGKVVA DQGIIAGCSG
     GTYDNLSEAA TILKGKSIGN DYFTMSAYPQ STPVYLATTR NHIAEELLEA GVVIKPAFCG
     PCFGAGDVPS NNGFSIRHTT RNFPNREGSK PGQGQISLVS LMDARSIAAT AANGGVITAA
     TDIEYNDTHK PYAFDDRIYK SRIYNGFGHA DLSQELRYGP NIKDWPKIYP MEKNMLVELA
     AVIHDPVTTT DELIPSGETS SYRSNPLKLS EFALSRRVPE YVGLSKRIQS EDLRRRAGDV
     PANVAAALAK VGASASDTSF GSCVFANRPG DGSAREQAAS CQKVLGGDAN ICYEYATKRY
     RSNCINWGLV PFTIAPETAF DYKPGDFVFV PGIREAILSG KEEIDAKVIT ASGVSDIHLY
     FNNLTPVERE ILADGCLMNY YMTHK
//