ID A0A192H2A8_9LACO Unreviewed; 877 AA.
AC A0A192H2A8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-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 Name=acnA {ECO:0000313|EMBL:MDA5387028.1};
GN ORFNames=AYR53_09330 {ECO:0000313|EMBL:ANK62944.1}, OUQ91_002068
GN {ECO:0000313|EMBL:MDA5387028.1};
OS Loigolactobacillus backii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=375175 {ECO:0000313|EMBL:ANK62944.1, ECO:0000313|Proteomes:UP000078582};
RN [1] {ECO:0000313|EMBL:ANK62944.1, ECO:0000313|Proteomes:UP000078582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMW 1.1989 {ECO:0000313|EMBL:ANK62944.1,
RC ECO:0000313|Proteomes:UP000078582};
RA Behr J., Geissler A.J., Vogel R.F.;
RT "Pediococcus and Lactobacillus from brewery environment - whole genome
RT sequencing and assembly.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MDA5387028.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KKP 3565 {ECO:0000313|EMBL:MDA5387028.1};
RG Lg backii sequencing group;
RA Kiousi D.E., Bucka Kolendo J.;
RL Submitted (NOV-2022) 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}.
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DR EMBL; CP014873; ANK62944.1; -; Genomic_DNA.
DR EMBL; JAPTYS010000005; MDA5387028.1; -; Genomic_DNA.
DR RefSeq; WP_068280614.1; NZ_JAPTYT010000005.1.
DR AlphaFoldDB; A0A192H2A8; -.
DR STRING; 375175.AYR53_09330; -.
DR GeneID; 42982457; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000078582; Chromosome.
DR Proteomes; UP001150357; 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, ECO:0000313|EMBL:MDA5387028.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000078582}.
FT DOMAIN 68..550
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 678..805
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 877 AA; 96705 MW; A061275EEF6B09A1 CRC64;
MDSTVKQKLE VANKVYYYWN IATWLGQQKQ QVETFPYTIR ILLEAVLRQS TKRPELKKSL
PSFINWDHAH EQDIPFKPER VILQDFTGIP ALVDLAAMRD KLVAVGGNAN QVNPDVPVDL
VVDHSVQVDR SGDSAAFAYN VKREFERNHE RYSFLKWAQQ AFKNLTIIPP DTGIIHQINL
EYLAQVVATK MSGEEILAYP DTLVGTDSHT TMVNGLGVLG WGVGGIEAEA SMLGEVSYIP
MPKVVGVRLT GQLKPGTTAT DLALTLTHQL RQHDVVGKLV EFYGPALATL AVADRATIAN
MAPEYGATCG FFPVDEQTLA YLKLTNRSPE KIKLIKTYLT ANHLFYQPNE DELRHYSETE
SLDLSTVSAS VAGPSRPQDL VHLAELPNNF TKYAKQSGLQ VSVDQQEFTL RPGALGIAAI
TSCTNTSNPD VLLAAGLLAK KAVELGLKVP QYVKTSLAPG SKVVSDYLAS TGLQDSLDRL
GFNLVGYGCT TCIGNSGKLK PELETTLEKH AYPVAAIESG NRNFEGRVHP LIKDTYLASP
PLVIAYALAG RLDIDLVHEP ITRTVEGQDI YLSDLWPQQS EITRLKQQSL SPERFKANYA
AILTQNKIWN KLPAPTGQLY AWNLHSTYIA KPPFFADLTK QRLTPMTNLR VLAKLGNTIT
TDHISPAGFI GQMTPAGQYL TAHGVATRDF NSYGSRRGNH QVMVRGTLAN IRIQNQLTPD
KVGGFTQYWP TKQTMTIYEA AQHYKEDKVG LIILAGKDYG MGSSRDWAAK GVALLGVKVV
IAESFERIHR SNLAMMGVLP LQFKAGESAT TLKLTGEEQF SLVFLPDRHV KVTAASPAGE
KTAFEVILRF DTPIEQRYFE NHGILPMVVA TKMATAR
//
