ID W8EW69_9BACT Unreviewed; 760 AA.
AC W8EW69;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=Hsw_1203 {ECO:0000313|EMBL:AHJ96798.1};
OS Hymenobacter swuensis DY53.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ96798.1, ECO:0000313|Proteomes:UP000019423};
RN [1] {ECO:0000313|EMBL:AHJ96798.1, ECO:0000313|Proteomes:UP000019423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY53 {ECO:0000313|EMBL:AHJ96798.1,
RC ECO:0000313|Proteomes:UP000019423};
RA Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT "Complete genome sequence of ionizing-radiation resistance bacterium
RT Hymenobacter swuensis DY53.";
RL Submitted (JAN-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}.
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DR EMBL; CP007145; AHJ96798.1; -; Genomic_DNA.
DR RefSeq; WP_044001415.1; NZ_CP007145.1.
DR AlphaFoldDB; W8EW69; -.
DR STRING; 1227739.Hsw_1203; -.
DR KEGG; hsw:Hsw_1203; -.
DR PATRIC; fig|1227739.3.peg.1444; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_006714_2_2_10; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000019423; Chromosome.
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.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:AHJ96798.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019423}.
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..687
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 760 AA; 81275 MW; E77E2A7522E6C02B CRC64;
MAFDLEMIKA VYAGMGSRIE AARTAVGRPL TLTEKILYAH LYGGTVSQAF ERGVSYVDFA
PDRVAMQDAT AQMALLQFMQ AGKPQAAVPS TVHCDHLIQA KEGATEDLAI ANSENKEVYD
FLASVSNKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTPNAGGLG MIAIGVGGAD
AVDVMSGMAW ELKFPKVIGV KLTGKLSGWT SAKDVILKVA GILTVKGGTG AIVEYFGEGA
NNLSATGKGT ICNMGAEIGA TTSVFSYDEK MGDYLRGTGR AEIADLAAGV AAHLRADDEV
LANPAEFYDQ LIEINLSELE PYVNGPFTPD AAWPISQFAA AVKEHGWPEK LEVGLIGSCT
NSSYEDITRA ASIAKQAADK GLTVQAEYTV TPGSELVRYT VERDGLLDTF AQMGGVVLAN
ACGPCIGQWA RHTDDPKRRN SIITSFNRNF AKRNDGNPNT HAFVASPEIV TAFAIAGDLT
FNPLTDTLTT KDGQQVKFDE PVGIELPPRG FAVEDAGFQA PAEDGSGVQV LVDEASDRLQ
LLDPFKAWEG TDLKGLRLLI KAQGKCTTDH ISMAGPWLKY RGHLDNISNN MLIGATNAFN
GEANSVKDQL TSGTPHGTVP QVARNYKAQG IGSVVVGDEN YGEGSSREHA AMEPRHLGVR
AVLVKSFARI HETNLKKQGM LALTFANKAD YDLIEEDDTI DIIGLTTFAP GKPLEVRLHH
SDGDTDLITV NHTYNEGQIE WFKAGSALNL IRLKESGQLA
//