ID A0A0C1FWH8_9SPHI Unreviewed; 759 AA.
AC A0A0C1FWH8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE AltName: Full=Citrate hydro-lyase {ECO:0000256|ARBA:ARBA00029682};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN ORFNames=OC25_18150 {ECO:0000313|EMBL:KIA92204.1};
OS Pedobacter kyungheensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1069985 {ECO:0000313|EMBL:KIA92204.1, ECO:0000313|Proteomes:UP000031246};
RN [1] {ECO:0000313|EMBL:KIA92204.1, ECO:0000313|Proteomes:UP000031246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 16221 {ECO:0000313|EMBL:KIA92204.1,
RC ECO:0000313|Proteomes:UP000031246};
RA Anderson B.M., Newman J.D.;
RT "Pedobacter Kyungheensis.";
RL Submitted (OCT-2014) 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 -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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:KIA92204.1}.
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DR EMBL; JSYN01000022; KIA92204.1; -; Genomic_DNA.
DR RefSeq; WP_039478960.1; NZ_JSYN01000022.1.
DR AlphaFoldDB; A0A0C1FWH8; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000031246; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01584; AcnA_Mitochondrial; 1.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01340; aconitase_mito; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 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.
DR PROSITE; PS00450; ACONITASE_1; 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}.
FT DOMAIN 34..477
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 558..685
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 759 AA; 81797 MW; 89BD82ACFA3142B9 CRC64;
MAFDIDMIKK VYANFGSRVE AARKVVGRPL TLSEKILYAH LWDGDPKTAF KRGSDYVDFA
PDRVAMQDAT AQMALLQFMQ AGRPQVAVPS TVHCDHLITA KEGAAIDLPH AKTESAEVFD
FLSSVSNKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTVNAGGLG MVAIGVGGAD
ACDVMAGLPW ELKFPKLIGV KLTGKLNGWT AAKDVILKVA GILTVKGGTG AIVEYFGDGA
TSMSCTGKGT ICNMGAEIGA TTSTFGYDES MERYLRATNR NEVADEANKI AAYLTGDPEV
YADPENYFDQ VIEIDLDTLE PYLNGPFTPD LATPVSQMKT EAEKNGWPLK VEWGLIGSCT
NSSYEDLSRA ASIANQAIAK GLVTKAEFGI NPGSEQVRYT ADRDGYLKTF EDLNATIFTN
ACGPCIGMWD RTGAEKAEKN TIVHSFNRNF AKRADGNPNT YAFVASPEMV AAIAISGNLG
FNPLTDTLTN DKGEQVKLDP PTGYELPTKG FAVEDAGFQA PAADGSKVQV LVSPTSHRLQ
LLDPFAPWEG TDLKGLKLLI KAKGKCTTDH ISMAGPWLKF RGHLDNISNN MLIGAVNYFN
DKTDTVKNEL TGEYGPVPAT QRDYKAAGLG SIVVGDENYG EGSSREHAAM EPRHLGVRAV
LVKSFARIHE TNLKKQGMLG LTFADKDDYD KILEDDTIDI LGLTEFAPDK PLTLVLHHAD
GTTEQFPVNH SYNAQQIDWF KAGGALNIIR AEAAAKAAL
//
