ID S1NDT1_9ENTE Unreviewed; 891 AA.
AC S1NDT1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=OMK_01290 {ECO:0000313|EMBL:EOT41121.1};
OS Enterococcus dispar ATCC 51266.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1139219 {ECO:0000313|EMBL:EOT41121.1, ECO:0000313|Proteomes:UP000014127};
RN [1] {ECO:0000313|EMBL:EOT41121.1, ECO:0000313|Proteomes:UP000014127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51266 {ECO:0000313|EMBL:EOT41121.1,
RC ECO:0000313|Proteomes:UP000014127};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus dispar ATCC_51266 (Illumina only
RT assembly).";
RL Submitted (MAR-2013) 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:EOT41121.1}.
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DR EMBL; AHYR01000005; EOT41121.1; -; Genomic_DNA.
DR RefSeq; WP_016172466.1; NZ_KE136354.1.
DR AlphaFoldDB; S1NDT1; -.
DR STRING; 44009.RV01_GL002174; -.
DR PATRIC; fig|1139219.3.peg.1250; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_9; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000014127; 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; cd01586; AcnA_IRP; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000014127}.
FT DOMAIN 66..560
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 891 AA; 97154 MW; 61E54CB88F9F9798 CRC64;
MKWKNQLSVA NKVYSYCDLK KVCATFNCDL KKLPYTIRIL LESVARNLDE DITQKNVEIL
ARWQATKPTG VIPFKPARVI LQDFTGVPAV VDLAAMRDAI VALGGDASQI RPAIPVSLVV
DHSVQVDCAK SPAALSYNTK KEFERNTERY QFLKWAQSSF QDFEVIPPET GIIHQVNIEA
LSNVVLVKKE NEANVVFPDT LQGTDSHTTM INGLGVLGWG VGGIEAEAAL LGEASYFPSP
AVIGVKLVGF LAAGTTATDL ALTVTEKLRQ ENVVGKFVEF FGSGYQTLSL SDRATIANMA
PEYGATCGYC PIDKETLDYL AVTGRDKNLI MLVKDYAIAN GLFYDEAEEI EYTKVIEINL
NQVEPSLAGP KRPQDRIALA KVATDFKNSL TAPVGPHGFG LSPREYEKTV SIDGLKKETL
QTGSVVLAAI TSCTNTSNPS VMLAAGLLAK KAVEKGLSVP SYVKTSLAPG SKIVTTYLKE
SGLMVYLEKL GFYLVGYGCT TCIGNSGPLA ENVSNAIEEN ELLTVSVLSG NRNFEGRIHP
LIKANYLASP PLVVAYALAG TVQKDLTTTP LGFDQENKAV MLADIWPTTA EINQTIQNFV
NPRTFKDTYS NLLDANTRWN AIPTTKSDCY AWDCNSTYIA NPPFFDNLTK ALPETRELLE
LAVLAKLGDS VTTDHISPAG AIPLDTPAGR YLQALGVPIS DFNSYGARRG NHEIMMRGTF
ANIRLQNQLI PEKSGGYTRL QPTGKMISIY DAAMHYQTEN KGTIILAGKD YGMGSSRDWA
AKGPQLLGVK AVLAESFERI HRSNLVMMGI VPLEYCDNQN AKTLGLEGSE SFSILLNQTP
QVGDTVSIMA KKPDGREISF IAKLRFDAPA DIRYWQNQGI LPMVIRKKLN T
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