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Database: UniProt
Entry: A0A090Z7W0_PAEMA
LinkDB: A0A090Z7W0_PAEMA
Original site: A0A090Z7W0_PAEMA 
ID   A0A090Z7W0_PAEMA        Unreviewed;       905 AA.
AC   A0A090Z7W0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
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:KFN06453.1};
GN   ORFNames=DJ90_4161 {ECO:0000313|EMBL:KFN06453.1}, GNQ08_21950
GN   {ECO:0000313|EMBL:MUG25033.1};
OS   Paenibacillus macerans (Bacillus macerans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=44252 {ECO:0000313|EMBL:KFN06453.1, ECO:0000313|Proteomes:UP000029278};
RN   [1] {ECO:0000313|EMBL:KFN06453.1, ECO:0000313|Proteomes:UP000029278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8244 {ECO:0000313|EMBL:KFN06453.1,
RC   ECO:0000313|Proteomes:UP000029278};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA   Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MUG25033.1, ECO:0000313|Proteomes:UP000442469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3CT49 {ECO:0000313|EMBL:MUG25033.1,
RC   ECO:0000313|Proteomes:UP000442469};
RA   Olajide A.M., Chen S., Lapointe G.;
RT   "Draft genome sequences of five Paenibacillus species of dairy origin.";
RL   Submitted (NOV-2019) 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:KFN06453.1}.
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DR   EMBL; JMQA01000037; KFN06453.1; -; Genomic_DNA.
DR   EMBL; WNZZ01000020; MUG25033.1; -; Genomic_DNA.
DR   RefSeq; WP_036626173.1; NZ_WNZZ01000020.1.
DR   AlphaFoldDB; A0A090Z7W0; -.
DR   STRING; 44252.DJ90_4161; -.
DR   GeneID; 77009554; -.
DR   PATRIC; fig|44252.3.peg.4141; -.
DR   HOGENOM; CLU_013476_2_1_9; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000029278; Unassembled WGS sequence.
DR   Proteomes; UP000442469; 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, ECO:0000313|EMBL:KFN06453.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029278};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          65..571
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          701..828
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   905 AA;  97805 MW;  2D6A39E4780A5435 CRC64;
     MSANDFNSAA RTLEVGGKSY RYFNLQSLEE QGLGKISKLP FSIKVLLEAA VRQFDGRAIT
     QEHVKQIAGW SEGRDDNKEI PFIPARIVLQ DFTGVPVVVD LAAMRDTVKK AGGDPKRINP
     LVPVDLVIDH SVMVDAFGSP EALEYNMKVE FERNEERYRF LRWAQTAFDN FRAVPPATGI
     VHQVNLEYLA SVAATKTVNG ETFVFPDSLV GTDSHTTMIN GLGVVGWGVG GIEAEAGMLG
     QPLYFVAPEV IGFKLTGSLA EGATATDLAL TVTQMLRKKG VVGKFVEFYG PGLSNISLAD
     RATVANMAPE YGATIGYFPV DQETLSYLRS TGRSEEQIAL VEDYYKAQGM FRTDDTEDPV
     FTDLIELDLS TVVPSLAGPK RPQDRIELTA MKESFNSIIR TPIDKGGYGL SEDKIGQSVA
     VKHPDGSTSE LKTGAVVIAA ITSCTNTSNP SVMVGAGLLA KKAVERGLKK PGYVKSSLTP
     GSLVVTEYLQ KAGLIEPLEA LGFHVAGYGC ATCIGNSGPL PEEVSAAIAD NDMTVAAVLS
     GNRNFEGRVH AQVKANYLAS PPLVVAYALA GTVNIDLQND PIGYDGNNQP VYLKDIWPSS
     AEIKEAIAAS LSPDMFRRKY EHVFTQNERW NAIPVPQGEL YEWDEKSTYI QNPPFFEKIG
     EGLSDIADIR GASVLALLGD SVTTDHISPA GNISPSSPAG SYLSERGVER KDFNSYGSRR
     GNHEVMMRGT FANIRIRNQV APGTEGGVTK YLPEGEVMSI YDASMKYQAN GQNLVVIAGK
     EYGTGSSRDW AAKGTYLLGV KAVIAESFER IHRSNLVGMG VLPLQFQEGT SWKTLGIDGT
     ETFDIAGLSN DVKPGQELTV TATRQDGSTF QFPVIARLDS MVDVDYYHNG GILQTVLRQM
     IAAGV
//
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