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Database: UniProt
Entry: A0A0R2R4N1_9FLAO
LinkDB: A0A0R2R4N1_9FLAO
Original site: A0A0R2R4N1_9FLAO 
ID   A0A0R2R4N1_9FLAO        Unreviewed;       755 AA.
AC   A0A0R2R4N1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=ABR79_03695 {ECO:0000313|EMBL:KRO55235.1};
OS   Cryomorphaceae bacterium BACL11 MAG-121001-bin54.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX   NCBI_TaxID=1655587 {ECO:0000313|EMBL:KRO55235.1, ECO:0000313|Proteomes:UP000051874};
RN   [1] {ECO:0000313|EMBL:KRO55235.1, ECO:0000313|Proteomes:UP000051874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL11 MAG-121001-bin54 {ECO:0000313|EMBL:KRO55235.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) 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:KRO55235.1}.
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DR   EMBL; LIBL01000089; KRO55235.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2R4N1; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000051874; 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   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          40..478
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   755 AA;  82196 MW;  F645BC4826641E24 CRC64;
     MAFDIEMIKK VYQKYPEAIQ AARKITKKPL TLAEKILYAH LWDGNATQEF KRGKDYVDFA
     PDRVAMQDAT AQMALLQFMQ AGKSKVAVPS TTHADHLIQA KIGADKDLQE GINQNNEVFT
     FLSSICNKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTVNAGGLA MVAIGVGGAD
     AVDVMAGMAW ELKFPKLIGV KLTGKLNGWT APKDVILKVA GILTVKGGTG AIVEYFGEGA
     ISLSATGKGT ICNMGAEIGA TTSTFGYDKS MERYLRATDR DDVADAANEI KEHLTGDTEV
     YANPEKYFDQ VIEINLDQLT PHLNGPFTPD LATQVGEMNE KATKNGWPLD IEWALIGSCT
     NSSYEDLTRA ASIVEDAVNK GLKPKAILGI NPGSEQVRFT AERDGLIDIF NKFETTKIFT
     NACGPCIGQW DREGADKKEK NSIVHSFNRN FAKRADGNPN THAFVGSPEM VAAIAISGRL
     DFNPVTDTLT NQNGEQVKLA EPTGHELPPN GFAVEDNGYQ APAEDGSNIE VIVNSESNRL
     QLLTPFKAWN GKNITGAKLL IKAEGKCTTD HISMAGPWLR YRGHLDNISN NCLIGAVNAF
     TGKTNAVLNQ VNGKIDEVPN VARAYRAAGI TSIVVGDHNY GEGSSREHAA MEPRHLGVLA
     VIVKSFARIH ETNLKKQGML GLTFANESDY DLIQEDDTFN FTDLADFKEG KKITLEVKHA
     DKTIDIIMLN HSYNETQIDW FKAGSALNLI REQNS
//
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