ID A0A1M6IDI5_9FLAO Unreviewed; 755 AA.
AC A0A1M6IDI5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN04487911_11741 {ECO:0000313|EMBL:SHJ32396.1};
OS Arenibacter nanhaiticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Arenibacter.
OX NCBI_TaxID=558155 {ECO:0000313|EMBL:SHJ32396.1, ECO:0000313|Proteomes:UP000184231};
RN [1] {ECO:0000313|EMBL:SHJ32396.1, ECO:0000313|Proteomes:UP000184231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8863 {ECO:0000313|EMBL:SHJ32396.1,
RC ECO:0000313|Proteomes:UP000184231};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQYX01000017; SHJ32396.1; -; Genomic_DNA.
DR RefSeq; WP_072764839.1; NZ_FQYX01000017.1.
DR AlphaFoldDB; A0A1M6IDI5; -.
DR STRING; 558155.SAMN04487911_11741; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000184231; 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:UP000184231}.
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; 82124 MW; B0F6E110A28E55B6 CRC64;
MAFDIDMIRK VYANMTSRVD KAREVVGRPL TLSEKILYSH LWDGNPNTAY KRGKDYVDFA
PDRIACQDAT AQMALLQFMQ AGKPKVAVPT TVHCDHLIQA KTGAVADLKV ANTTSSEVFN
FLESVSNKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTVNAGGLG MVAIGVGGAD
AVDVMAGMAW ELKFPKLIGV KLTGSISGWT SAKDVILKVA GILTVKGGTG AIIEYFGEGA
KNLSCTGKGT ICNMGAEVGA TTSTFGYDES MERYLRATDR NDVADAANEV KDYLTADPEV
YANPENYFDE IIEIDLDTLR PHLNGPFTPD LATPVGELGE KAKANGWPLK VDWGLIGSCT
NSSYEDLTRA ASIAQQAVDK KIKSKSDFGI NPGSEQIRFT AERDGLLEIF ENLGATIFTN
ACGPCIGQWD RSDLKGDEKN TIVHSFNRNF SKRADGNPNT HAFVGSPEMV AAIAISGRLD
FDPMNDTLIN EDGEEVKLDE PRGIELPPKG FEVEDAGYLA PDEDGSSVVV KVDPSSERLQ
LLEPFVPIKP ENLQGAKLLI KAFGKCTTDH ISMAGPWLRF RGHLDNIANN TLIGAVNAFN
KKTNFVKNQL TGEYVGVPDA QRAYKAAGIK TVVVGDHNYG EGSSREHAAM QPRHLGVAVV
IVKSFARIHE TNLKKQGLLG LTFANENDYD LIQEDDIFNF IDINEFAPDK QLTLELVHAD
GSKDVIKLNH TYNQSQIEWF KEGSALNVIK RENVA
//
