ID A0A074KU17_9BACT Unreviewed; 926 AA.
AC A0A074KU17;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=acnA {ECO:0000313|EMBL:KEO72409.1};
GN ORFNames=EL17_16835 {ECO:0000313|EMBL:KEO72409.1};
OS Anditalea andensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Anditalea.
OX NCBI_TaxID=1048983 {ECO:0000313|EMBL:KEO72409.1, ECO:0000313|Proteomes:UP000027821};
RN [1] {ECO:0000313|EMBL:KEO72409.1, ECO:0000313|Proteomes:UP000027821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY1 {ECO:0000313|EMBL:KEO72409.1,
RC ECO:0000313|Proteomes:UP000027821};
RA Yang L., Wei S., Tay Q.X.M.;
RT "Characterization and application of a salt tolerant electro-active
RT bacterium.";
RL Submitted (APR-2014) 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}.
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:KEO72409.1}.
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; JMIH01000024; KEO72409.1; -; Genomic_DNA.
DR RefSeq; WP_035076917.1; NZ_JMIH01000024.1.
DR AlphaFoldDB; A0A074KU17; -.
DR STRING; 1048983.EL17_16835; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000027821; 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.
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:KEO72409.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000027821}.
FT DOMAIN 74..594
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 724..850
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 926 AA; 102791 MW; 8F92F1FF7A3E5922 CRC64;
MSLDPYQIKK TLNTPKGEMT YWSLNELNLK GRNILKLPFS IRILLENTLR NFDDFAITKK
DIETLLNWVP QGSDKDIPFK PARVLMQDFT GVPAVVDIAS LRAEAVRQGK DGQKINPLIP
VDLVIDHSVQ VDYFGTNYSY KKNVDVEYGR NEERYQLLKW AQKSFDNFSV VPPGMGICHQ
VNLEYLAQGV ITRDGMVFPD TLVGTDSHTP MVNGIGVVGW GVGGIEAEAA ILGQPINFIM
PEVVGLKLTG SLPLGTTATD MVLTITQLLR SHGVVGKFVE VFGPGLDHLS VPDRATISNM
SPEFGCTVTY FPIDQRTLDY MEKTNRSEDQ IKLVEEYARE NLLWRKDEDQ VTYSSVVELD
LDSIEPTVAG PKRPQDKILL REFKDKFSEI LREAHGREYI PMDKRDVSRW YEEGGSSQPT
EDKKDVSDEV EIETKTKGGL KTVAVKLHNE KFNLHDGSIV IAAITSCTNT SNPNVMVGAG
LVARKARERG LDVKPWVKTS LAPGSKVVTD YLEKAGVMDD LEALRFHLVG YGCTSCIGNS
GPLPRHIAKA VEENDLIVAS VLSGNRNFEA RVHPQVKMNY LMSPMLVVAY ALAGRIDIDL
INEPIGYDPN LEPVYLQDIW PSNEEIFGLV NKVLSPNDFA KNYGEIFEGN EQWKNLEAPK
DLIYQWNDAS TYIKEAPFFE SMNIDLAASQ DIIEANVLLK LGDSITTDHI SPAGSFSEIS
TAGKYLIERG VPKENFNSYG SRRGNDELMV RGTFANVRIK NQLASKEGGY TTHIPSKEEM
SIYDAAQKYK KEETPLIVLA GKEYGSGSSR DWAAKGTSLL GIKAVIAESY ERIHRSNLVG
MGVLPLMYAN GETAGSLGLS GMEKFSIRGI ADGLHPGKLL AAESIAADGT KKNFELICKL
DSAIEVEYYR NGGILHYVLR EFLKKD
//
