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
//