ID A0A0R1VGN6_9LACO Unreviewed; 883 AA.
AC A0A0R1VGN6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=FC89_GL001962 {ECO:0000313|EMBL:KRM04718.1};
OS Liquorilactobacillus ghanensis DSM 18630.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423750 {ECO:0000313|EMBL:KRM04718.1, ECO:0000313|Proteomes:UP000051451};
RN [1] {ECO:0000313|EMBL:KRM04718.1, ECO:0000313|Proteomes:UP000051451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18630 {ECO:0000313|EMBL:KRM04718.1,
RC ECO:0000313|Proteomes:UP000051451};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM04718.1}.
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DR EMBL; AZGB01000026; KRM04718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1VGN6; -.
DR STRING; 1423750.FC89_GL001962; -.
DR PATRIC; fig|1423750.3.peg.2004; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000051451; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051451}.
FT DOMAIN 75..555
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 679..805
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 883 AA; 97492 MW; 6C4C2C64D5ADFFF6 CRC64;
MSGGSKMTET YRNQFTLAGK NYYYYDIAAY LQHEEQEIEA MPYAIRVLLE LTLRHSSKQP
ALKKYLAVFN NWDEQHTNDV PYKPERVILQ DFTGVPALVD LAAMREEVQN QGGDPTAINP
DVPVHLVIDH SVQVDLAGNQ DAFEYNIKQE FKRNRERYLF LKWAQASFKN LTVIPPDTGI
IHQVNLEYLS PVIRHSKAAE PLAFPDTLVG TDSHTTMINA LGVLGWGVGG IEAEASMLGQ
ESYFPMPQVV GVRLTGKMPA TATATDLALT LTHILRKQNV VGKFVEFYGP GLKNLPLANR
ATIANMAPEY GATCGYFPID QQTLSYLRLT DRSAEQIKLV EKYAKVNHLW YQENEDNLRH
YSENVELDLG TITSSVAGPK RPQDLVELSQ LPQNFKKYAE LKNCQVKTAG QTFSLRPGAL
GIAAITSCTN TSNPEILITA GLLAEKAVAA GLKIPAYVKT SFAPGSRVVA DYLQAAQLQT
YLDQLGFNIV GYGCTTCIGN SGKLQPGVQE IINQTNYPLA AIESGNRNFE GRVNPLIKDT
YLASPPLVIA YALAGTLDID LLHQPIGQDQ QGKAVYLSDL WPTTAEVSQV IHQYVKPQLF
SANYQNIFSQ NAAWNALPVT ESVTYPWQAA STYLALPPLF ASRQTDLTGL RVLAKLGDSI
TTDHISPAGF IGQTTPAGKY LQEHGVQPAD FNSYGSRRGN HEVMMRGTLA NIRLQNQLTP
EKQGGFTRSW LTNKETTIYE AAMDYKQHNI GTIILAGKDY GMGSSRDWAA KGVELLGVKA
VIAESFERIH RSNLVMMGVL PLQFMAGDTA DTLGLQGNEK FTIKLTGKTA KVLAESPDRQ
VDFTVRVRFD APIDREYFKA SGILPYVIAR KMAKQNESEG SDD
//
