ID A0A2A5XU28_9FLAO Unreviewed; 752 AA.
AC A0A2A5XU28;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=CND00_01930 {ECO:0000313|EMBL:PDH52921.1};
OS Cryomorphaceae bacterium MED-G14.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1986260 {ECO:0000313|EMBL:PDH52921.1, ECO:0000313|Proteomes:UP000219038};
RN [1] {ECO:0000313|EMBL:PDH52921.1, ECO:0000313|Proteomes:UP000219038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED-G14 {ECO:0000313|EMBL:PDH52921.1};
RA Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Fine stratification of microbial communities through a metagenomic profile
RT of the photic zone.";
RL Submitted (AUG-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}.
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:PDH52921.1}.
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DR EMBL; NTKN01000008; PDH52921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5XU28; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000219038; 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}.
FT DOMAIN 34..476
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 557..684
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 752 AA; 82621 MW; 06368B3E5A370D4B CRC64;
MVFDIEMIKN VYSSMKDKVD HAKKVCNHPL TLSEKILYSH LWEKTKSTFR RGVDYVDFAP
DRIACQDATA QMALLQFMQA GKNKVAVPTT VHCDHLIQAK IGAGPDLQEA INTSNEVFNF
LESVSNKYGI GFWKPGAGII HQVVLENYAF PGGMMIGTDS HTVNAGGLGM VAIGVGGADA
VDVMAGMAWE LKFPKLIGVK LTGKLSGWTA AKDVILKVAG ILTVKGGTGA IIEYFGPGAQ
NLSCTGKGTI CNMGAEVGAT TSTFGYDESM EKYLRATGRD EIADEANNIK EYLTGDPEVY
QNPEKYFDQV IEINLSELEP HINGPFSPDI ATPISKMAET LEKNNWPRKI EWGLIGSCTN
SSYEDLSRAS SIADQALNKN LSTKAFFGIN PGSEQVRYTA ERDGFLDIFE KLDAKVFTNA
CGPCIGQWAR DGADKQEKNS IIHSFNRNFA KRADGNPNTH AFVASPEIVA AIAISGDLGF
NPKTDSLFNN LGEEVKLEEP TGWELPPKGF EVDDRGYIEP DCDGSNVNVI INPDSKRLEK
LEPFAPWDGK NITGAKLLIK AFGKCTTDHI SMAGPWLRYR GHLDNISNNC LIGAVNAYNK
KTNFIKSQLN GEYGGVPETQ REYKKNNIPT VVVGDHNYGE GSSREHAAME PRHLGVKVVI
VKSFARIHET NLKKQGMLAL TFHNESDYDL IQEDDTFNFI DLENFSPGNQ ITIELIHSDG
SKDVIKTNHT YNSQQIDWYK EGSALNLIKK GA
//
