ID E2N9P7_9BACE Unreviewed; 747 AA.
AC E2N9P7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=BACCELL_00993 {ECO:0000313|EMBL:EEF91358.1};
OS Bacteroides cellulosilyticus DSM 14838.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=537012 {ECO:0000313|EMBL:EEF91358.1, ECO:0000313|Proteomes:UP000003711};
RN [1] {ECO:0000313|EMBL:EEF91358.1, ECO:0000313|Proteomes:UP000003711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF91358.1,
RC ECO:0000313|Proteomes:UP000003711};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEF91358.1, ECO:0000313|Proteomes:UP000003711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF91358.1,
RC ECO:0000313|Proteomes:UP000003711};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides cellulosilyticus (DSM 14838).";
RL Submitted (JAN-2009) 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:EEF91358.1}.
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DR EMBL; ACCH01000094; EEF91358.1; -; Genomic_DNA.
DR RefSeq; WP_007210381.1; NZ_JANSWE010000053.1.
DR AlphaFoldDB; E2N9P7; -.
DR HOGENOM; CLU_006714_2_2_10; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000003711; 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; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:EEF91358.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 34..477
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 554..682
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 747 AA; 82021 MW; A94BEF5B70DFC116 CRC64;
MVYDVTMLKA FYASYKGKME HVRAILQRPL TLAEKILYTH LFDEKGVKDY KRGEDYVNFR
PDRVAMQDAT AQMALLQFMN AGREQVAVPS TVHCDHLIQA YRGAREDIAT ATKTNEEVYD
FLRDVSSRYG IGFWQPGAGI IHQVVLENYA FPGGMMVGTD SHTPNAGGLG MVAIGVGGAD
AVDVMTGMEW ELKMPRLIGV HLKGELSGWA APKDVILKLA GILTVKGGTN AIIEYFGPGT
ASLSATGKAT ICNMGAEVGA TTSLFPYDDR MATYLKATGR EEVAEMADSV AGDLRADADI
MITPEKYYDR VIEIDLSRLE PYINGPFTPD AATPISEFAE KVLVNGYPRK MEVGLIGSCT
NSSYQDLSRA VSLARQVEEK HLKVAAPLIV NPGSERIRAT AERDGMIGTF EKVGATIMAN
ACGPCIGQWK RETDNPTRKN SIVTSFNRNF AKRADGNPNT YAFVASPELT MALTIAGDLC
FNPLTDVLVN REGEKVKLSE PVGEELPPKG FAEGSEGYIA PGSEKVEINV NPHSQRLQLL
QPFPAWEGTD LLNMPLLIKA QGKCTTDHIS MAGPWLRFRG HLENISDNML MGAVNAFNGE
TNSVWNRLTN TYGPVSGTAK MYKSEEISSI VVAEENYGEG SSREHAAMEP RFLNVRVILA
KSFARIHETN LKKQGMLALT FVDKADYDKI QEHDLISVIG LMDFAPGRNL KIIFHHEDGT
KDSFEAQHTY NEQQIGWFRA GSALNAR
//
