ID E8N484_ANATU Unreviewed; 897 AA.
AC E8N484;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 Name=citB {ECO:0000313|EMBL:BAJ63248.1};
GN OrderedLocusNames=ANT_12140 {ECO:0000313|EMBL:BAJ63248.1};
OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS UNI-1).
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Anaerolinea.
OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ63248.1, ECO:0000313|Proteomes:UP000008922};
RN [1] {ECO:0000313|EMBL:BAJ63248.1, ECO:0000313|Proteomes:UP000008922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC {ECO:0000313|Proteomes:UP000008922};
RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA Fujita N.;
RT "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL Submitted (DEC-2010) 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 -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; AP012029; BAJ63248.1; -; Genomic_DNA.
DR RefSeq; WP_013559636.1; NC_014960.1.
DR AlphaFoldDB; E8N484; -.
DR STRING; 926569.ANT_12140; -.
DR GeneID; 78349647; -.
DR KEGG; atm:ANT_12140; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_0; -.
DR InParanoid; E8N484; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000008922; Chromosome.
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, ECO:0000313|EMBL:BAJ63248.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008922}.
FT DOMAIN 79..567
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 697..823
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 897 AA; 97915 MW; B92C8373E119CC62 CRC64;
MSASRSSAIP AILKTSQGTY FYYPLDQWEG ISRESLQRLP FSIRILLEGY LRNSAHPRVS
QQSISALANW APQATHRPIL QFFPGRVVLQ DFTGVPVMND LAAMRAALVR LGGNPEKINP
VVPVDLVIDH SVQVDYFGIP DALKLNVQLE FERNRERYEF LHWAQKAFKN FRVVPPSSGI
VHQVNLEYLA RGVLTSSQDG TTVVFPETLV GTDSHTTMIN GLGVVGFGVG GIEAVAAMLG
EPLEFVTPDV IGLRLTGKLR EGVTPTDLTL TITQLLRKHG VVDKFVEFFG PGLVNLSLAD
RAMISNMAPE SGATVLYFPV DQQTLAYLAL TGRPTELVEA YYRAQGLFVM PETPEPEYTA
VLHLDLESIE PSLAGPKRPQ DRVPLPQVKK NFRSSLSKPK TERGFGLSSE DLGKEAEYRS
NGYRETLKHG AVVIAAITSC TNTSNPYVML AAGLLARNAV LKGLRVKPYV KTSLAPGSKV
VTAYLEKSGL DKALSALGFD VVGYGCTTCI GNSGPLPQPV IEAIESGGLV AAAVLSGNRN
FEGRVHPYVQ ANYLASPPLV VAYALAGTVD IDLTQEPLGV DRQGNPVYLK DLWPSAEEIE
QLIQDLVQPE LFASEYADLY SANPQWSQIQ SPSSLLYEWN PASTYLQEPP FFENLSKEPQ
FLSDIQNARV LALFGDSITT DHISPAGNIS PTSPAGKYLL EHGVPVSEFN SYGSRRGNDR
VMTRGTFANI RLKNLLLGGK EGGYTIHFPD GEVLPIYDAA MKYREEGVPL IVIAGKEYGT
GSSRDWAAKG VQQLGVRAIL AESFERIHRS NLAGMGVLPL VFKPGENAQS LGLTGREIYT
LKGVSQIQSP GGELTVQVTR EDGSTFEFQV TIRLDTPNEV SYFHHGGILN TILLNWL
//
