ID A0A1P8RUL9_9FLAO Unreviewed; 755 AA.
AC A0A1P8RUL9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BWZ20_04025 {ECO:0000313|EMBL:APY07513.1};
OS Winogradskyella sp. J14-2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1936080 {ECO:0000313|EMBL:APY07513.1, ECO:0000313|Proteomes:UP000187462};
RN [1] {ECO:0000313|EMBL:APY07513.1, ECO:0000313|Proteomes:UP000187462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J14-2 {ECO:0000313|EMBL:APY07513.1,
RC ECO:0000313|Proteomes:UP000187462};
RA Kim J.H., Chi W.-J.;
RT "Genome sequence of Winogradskyella sp. J14-2 isolated from seawater in
RT Jeju island.";
RL Submitted (JAN-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}.
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DR EMBL; CP019388; APY07513.1; -; Genomic_DNA.
DR RefSeq; WP_076616653.1; NZ_CP019388.1.
DR AlphaFoldDB; A0A1P8RUL9; -.
DR STRING; 1936080.BWZ20_04025; -.
DR KEGG; wij:BWZ20_04025; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000187462; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000187462};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 34..479
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 559..687
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 755 AA; 82216 MW; F0069A743670CAC0 CRC64;
MAFDIDMIKK VYANMTERVD AARDIVGKPL TLSEKILYAH LWDGKPTKAF TRGKDYVDFA
PDRVACQDAT AQMALLQFMQ AGKPKVAVPT TVHCDHLIQA KDGAATDLKH ANDTSSEVFN
FLESVSNKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTVNAGGLG MVAIGVGGAD
AVDVMAGMAW ELKFPKLIGV RLTGKLSGWT APKDVILKVA EILTVKGGTG AIVEYFGPGA
LSMSCTGKGT ICNMGAEIGA TTSTFGYDDS MERYLRATDR ADVADEANKI KEYLTADAEV
YANPEQYFDQ VIDINLSELG PLLNGPFTPD LSTTVGKEMT EKAKANEWPM QVEWGLIGSC
TNSSYEDLSR ASSIAQQALD KGLKTKAEFG INPGSEQVRY TAERDGILQV FEKLDAKIFT
NACGPCIGQW ARYSDPKNAP KNSIVHSFNR NFAKRADGNP NTHAFVASPE ITAAIAIAGR
LDFNPMTDTL INENGEEVML DEPTGWELPP KGFDVKENGY LEPLADGTGV EVTVKDDSER
LQLLTPFKPI GNSITGAKLL IKAFGKCTTD HISMAGPWLR FRGHLDNIAN NTLIGAVNAF
NQKTNFVKNQ LTGEYGGVPD TQREYKKNGI WSVVVGDHNY GEGSSREHAA MQPRHLGVAA
VIVKSFARIH ETNLKKQGML GLTFANEADY DLIQEDDTFN FLDLNEFAPD KQLHVEVVHA
DGSKDVIALN HTYNDAQILW YKEGSALNLI KKQNA
//