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Database: UniProt
Entry: A0A257KFY1_9FLAO
LinkDB: A0A257KFY1_9FLAO
Original site: A0A257KFY1_9FLAO 
ID   A0A257KFY1_9FLAO        Unreviewed;       755 AA.
AC   A0A257KFY1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=CFE24_01775 {ECO:0000313|EMBL:OYU85440.1};
OS   Flavobacterium sp. BFFFF2.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2015558 {ECO:0000313|EMBL:OYU85440.1, ECO:0000313|Proteomes:UP000216176};
RN   [1] {ECO:0000313|EMBL:OYU85440.1, ECO:0000313|Proteomes:UP000216176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFFFF2 {ECO:0000313|EMBL:OYU85440.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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:OYU85440.1}.
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DR   EMBL; NKJD01000003; OYU85440.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257KFY1; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000216176; 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.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216176}.
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..686
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   755 AA;  80877 MW;  141269ADA9638C2E CRC64;
     MAFDIEMIKK AYAQMPARVD QARAVVGRPL TLSEKILYAH LWENNPSHAY ARGKDYVDFA
     PDRVACQDAT AQMALLQFMH AGKNKVAVPT TVHCDHLIQA KVGAKTDLEV ASKQSKEVFD
     FLSSVSNKYG IGFWKPGSGI IHQIVLENYA FPGGMMIGTD SHTVNAGGLG MLAIGVGGAD
     AVDVMSGMSW ELKFPKLIGV KLTGKLSGWT APKDVILKVA DILTVKGGTG AIVEYFGEGA
     EAMSCTGKGT ICNMGAEIGA TTSTFGYDDS MRRYLTATGR ADVVAAADEV AAYLTADPEV
     YADPATYFDQ LIEINLSELE PHINGPFTPD RGTPVSKMKQ EAEANGWPLA VEWGLIGSCT
     NSSYEDMARA ASIVEQAVAH GITPKAEFGI NPGSEQIRFT IERDGIIATF EKMGTKVFTN
     ACGPCIGQWD RTGADKGEKN TIVHSFNRNF SKRADGNPNT HAFVTSPEMV AALAISGRLD
     FNPITDTLLN DKGEAVRLLP PTGDELPTRG FDVDDAGFQA PAADGSGIQV AVSVTSDRLQ
     LLEPFQAWDG HNISGAKLLI KAFGKCTTDH ISMAGPWLRY RGHLDNISNN MLIGAVNAYT
     QQSNSVKNQL TGGYDAVPAV QRAYKAANVP SIVVGDHNYG EGSSREHAAM EPRFLGVKAV
     LVKSFARIHE TNLKKQGMLA LTFANEADYD KIQEDDTFNF TDLTSFAPGK PLTLEVVHAD
     GSADTILANH TYNDSQIGWF KAGSALNLIA AAGAA
//
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