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Database: UniProt
Entry: A0A1H9F8Q0_9BACT
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ID   A0A1H9F8Q0_9BACT        Unreviewed;       759 AA.
AC   A0A1H9F8Q0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=SAMN05444359_108130 {ECO:0000313|EMBL:SEQ34259.1};
OS   Neolewinella agarilytica.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC   Neolewinella.
OX   NCBI_TaxID=478744 {ECO:0000313|EMBL:SEQ34259.1, ECO:0000313|Proteomes:UP000199021};
RN   [1] {ECO:0000313|Proteomes:UP000199021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24740 {ECO:0000313|Proteomes:UP000199021};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FOFB01000008; SEQ34259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9F8Q0; -.
DR   STRING; 478744.SAMN05444359_108130; -.
DR   InParanoid; A0A1H9F8Q0; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000199021; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199021}.
FT   DOMAIN          34..479
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          558..686
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   759 AA;  82218 MW;  B1CC44762594B711 CRC64;
     MAFDIDLIKK VYADLPGKVA EARKVLGRPL TLSEKILYSH LHEESPLANY GRGKDYVMFA
     PDRVAMQDAT AQMALLQFMM AGRDKVAVPS TVHCDHLIQA KIGADADLQH AINTSNEVFN
     FLESVSDKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTVNAGGLG MVAIGVGGAD
     AVDVMAGMAW ELKNPKLIGV KLTGKLSGWS APKDVILKVA DILTVKGGTG AIVEYFGEGA
     KSMSCTGKGT ICNMGAEIGA TTSTFGYDES MDRYLRATGR EDVADAAKEV AEHLTADAEC
     YADPEKYFDQ VIEINLSELK PLINGPFTPD LSTAAGSEMT ERATANDWPL DVEWGLIGSC
     TNSSYEDLSR AASIARQAVA KGLTTKAEFG INPGSEQVRF TTERDGIIKA FEDLNAKIFT
     NACGPCIGQW ARYNDPMNAP KNSIIHSFNR NFSKRADGNP NTHAFVASPE MVAAIAISGR
     LDFNPMTDTL VNDKGEEVML DEPTGYELPP DGFDVEDRGF NAPAEDGSGV EVVVAPTSDR
     LQLLTPFVPI TQDDMTDMRV LIKVKGKCTT DHISMAGPWL KYRGHLENIS ENCYTGAINF
     FNDKANKVLN YVVNDYVAVP DSAKAYQAKG IGTVVFGEEN LGEGSSREHA AMEPRFLGVN
     AVIVKSFARI HETNLKKQGM LALTFVDKDD YDKVRQDDVV TIKGFDQMAP GKNLTIKLDH
     HDGTNDEFEV AHTYNAAQIE WVRAGSALNK IRQDVAAGA
//
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