ID A0A242A2X2_9ENTE Unreviewed; 898 AA.
AC A0A242A2X2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN ORFNames=A5886_000339 {ECO:0000313|EMBL:OTN75269.1};
OS Enterococcus sp. 8G7_MSG3316.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1834191 {ECO:0000313|EMBL:OTN75269.1, ECO:0000313|Proteomes:UP000195043};
RN [1] {ECO:0000313|EMBL:OTN75269.1, ECO:0000313|Proteomes:UP000195043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8G7_MSG3316 {ECO:0000313|EMBL:OTN75269.1,
RC ECO:0000313|Proteomes:UP000195043};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 8G7_MSG3316.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|RuleBase:RU361275}.
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 ECO:0000256|RuleBase:RU361275};
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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:OTN75269.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NGKU01000001; OTN75269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A242A2X2; -.
DR STRING; 1834191.A5886_000339; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000195043; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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 CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
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; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 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 4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW Lyase {ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 69..561
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 690..815
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 898 AA; 97617 MW; 3AD10FD97E7E6DCE CRC64;
MKWQTKITVN QSEYTYIDLV KLAAQFSADL HRLPYTIRVL LESVARHQDD EITEAYLPYL
ANWSPVAPEG VVPFKPERVV LQDFTGVPAV VDLAAMRDAI VSLGGDAAAI NPEIPVTLVV
DHSVQVDCAG TPQAVAFNTE REFERNQERY QFLKWAQQSF ANFEVVPPET GIIHQVNIES
LSDVILQKQI GEDIYLFPDT LQGTDSHTTM INGLGVLGWG VGGIEAEAAI LGEPSFFPTP
EVIGVRFVHE MPAGTTATDL ALKVTEVLRL EKVVGKFVEY FGPGYSQLSL ADRATLANMA
PEYGATCGFC PIDQETLNYL ATTGRPAALI TLVEAYAKAN HLFYDAQQSP EYSKVITIDL
AEIQPALAGP KRPQDRILLP AVGTDFDDSV TAAVGPKGFG LTADEWDKEA LVLWPDTTER
LTTGDLVLAA ITSCTNTSNP FVMLSAGLLA KNAVEKGLVV PKYVKTSLAP GSQIVTTYLQ
NSGLMPYLEK LGFYLVGYGC TTCIGNSGPL ETPVAEAIEA ENLLVASVLS GNRNFEGRIH
PQIKANYLAS PPLVVAYAIA GTIRKDLTTE PLAIVDGAPV YLADIWPTNE EVNAYVQTYV
GPEAFRAAYA HLFDANERWN AIDTTASAVY DWQEESTYIA HPPYFHTLSK ELPQQGALND
LKVLAKLGDS VTTDHISPAG SIGLDSSAGK FLTDRGVAYR EFNSFGSRRG NHHIMMRGTF
GNIRLQNQLV PGSTGSVTHY FPTGETLSIF DASMQYQEAG DSCIILAGKD YGMGSSRDWA
AKGTQLLGIK VVLAESFERI HRSNLVMMGV IPLEYVSGQT AASLGLDGSE SFFVALPEEP
QVGQRIEVTA KRSDGTALTF PTRLRFDAPA DIRYWKNQGI LPMVIRKKIA ETGGALHV
//
