ID A3J0H1_9FLAO Unreviewed; 754 AA.
AC A3J0H1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=FBBAL38_02010 {ECO:0000313|EMBL:EAZ96155.1};
OS Flavobacteria bacterium BAL38.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX NCBI_TaxID=391598 {ECO:0000313|EMBL:EAZ96155.1, ECO:0000313|Proteomes:UP000003784};
RN [1] {ECO:0000313|EMBL:EAZ96155.1, ECO:0000313|Proteomes:UP000003784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL38 {ECO:0000313|EMBL:EAZ96155.1,
RC ECO:0000313|Proteomes:UP000003784};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2007) 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:EAZ96155.1}.
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DR EMBL; AAXX01000001; EAZ96155.1; -; Genomic_DNA.
DR AlphaFoldDB; A3J0H1; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000003784; 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:UP000003784}.
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 754 AA; 81666 MW; 41FF7488DCF89502 CRC64;
MAFDIEMIEK VYANMVARVD KARELVGKPL TLTEKILYSH LWDETSTNVY KRGVDYVDFA
PDRVACQDAT AQMALLQFMH AGKKTVAVPT TVHCDHLILA KNGAKQDLEL ANKQSKEVFD
FLSSVSNKYG IGFWKPGSGI IHQIVLENYA FPGGMMIGTD SHTVNAGGLG MLAIGVGGAD
AVDVMSGMSW ELKFPKLIGV KLTGKLSGWT APKDVILKVA DILTVKGGTG AIVEYFGEGA
IAMSCTGKGT ICNMGAEIGA TTSTFGYDDS MRRYLAATGR QDVVNAADKV ASYLTADEEV
YANPEHYFDQ LIEINLSELE PHINGPFTPD RGTPVSKMKT EAEANGWPLK VEWGLIGSCT
NSSYEDMSRA ASIVRQAVKH GITPKAEFGI NPGSEQIRFT IERDGIIADF EKMGTKVFTN
ACGPCIGQWD REGADKQEKN TIVHSFNRNF SKRADGNPNT HAFVTSPEMV AALAISGRLD
FNPITDTLLN DKGEAVKLET PFGDELPKRG FDVEDAGFQA PAADGSGVQV VVSPTSDRLQ
LLEPFQPWDG KNYTGAKLLI KAFGKCTTDH ISMAGPWLRF RGHLDNISNN MLIGAENAFN
GKANSVKNQL TGSYDAVPAV QRAYKAAGIS SIVVGDHNYG EGSSREHAAM EPRFLGVKAV
LVKSFARIHE TNLKKQGMLA LTFANEADYD KIQEDDTINF LDLTEFAPGK PLILEFVHAD
GTKDVILANH TYNDSQIGWF VAGSALNLIA AGKA
//
