ID A0A023BT86_9FLAO Unreviewed; 755 AA.
AC A0A023BT86;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=ATO12_19650 {ECO:0000313|EMBL:EZH73221.1};
OS Aquimarina atlantica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1317122 {ECO:0000313|EMBL:EZH73221.1, ECO:0000313|Proteomes:UP000023541};
RN [1] {ECO:0000313|EMBL:EZH73221.1, ECO:0000313|Proteomes:UP000023541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-z7 {ECO:0000313|EMBL:EZH73221.1,
RC ECO:0000313|Proteomes:UP000023541};
RA Lai Q.;
RT "Aquimarina sp. 22II-S11-z7 Genome Sequencing.";
RL Submitted (APR-2014) 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:EZH73221.1}.
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DR EMBL; AQRA01000006; EZH73221.1; -; Genomic_DNA.
DR RefSeq; WP_034243052.1; NZ_AQRA01000006.1.
DR AlphaFoldDB; A0A023BT86; -.
DR STRING; 1317122.ATO12_19650; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000023541; 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 Reference proteome {ECO:0000313|Proteomes:UP000023541}.
FT DOMAIN 35..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; 81643 MW; 9E90266BA00168B0 CRC64;
MAFDINMIKK VYSQVADRVN AAREVTGKPL TLAEKILYSH LWDVKTKKAF TRGKDYVDFA
PDRIACQDAT AQMALLQFMQ AGKSKVAVPT TVHCDHLIQA KEGAAADLKN ANDISSEVFN
FLESVSDKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTVNAGGLG MVAIGVGGAD
AVDVMAGMAW ELKFPKLIGV KLTGKLSGWT APKDVILKVA EILTVKGGTG AIVEYFGPGA
TSMSCTGKGT ICNMGAEIGA TTSTFGYDES MERYLRATDR ADVADAANEV KEHLTADPEV
YANPEQYFDQ VIEINLSELG PLLNGPFTPD LSTAVGSTMT EKAKANDWPI QVEWGLIGSC
TNSSYEDLSR ASSIAQQALD KGLKMKAELG INPGSEQVRY TADRDGILGI FEKLDAKIFT
NACGPCIGQW ARYNDPKNAP KNSIVHSFNR NFAKRADGNP NTHAFVASPE LTAAIAVAGR
LDFNPLTDKL INENGEEVMF DEPTGWELPP KGFEVKDNGY LAPVEDGSNV EVKVSPTSER
LQLLTPFVPI GNEIKGAKLL IKAFGKCTTD HISMAGPWLR FRGHLDNISN NCLIGAVNAF
GKKTNFVKNQ LTGEFGGVPD TARAYKAAGV PTIVVGDHNY GEGSSREHAA MEPRHLGVAA
VIVKSFARIH ETNLKKQGML GLTFANESDY DLIQEDDTFN FTDLDQFAAG KQLTLEIVHA
DGSKDTVMLN HTYNDSQIEW FQEGSALNLI KKQNA
//
