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Database: UniProt
Entry: W0RMS2_9BACT
LinkDB: W0RMS2_9BACT
Original site: W0RMS2_9BACT 
ID   W0RMS2_9BACT            Unreviewed;       880 AA.
AC   W0RMS2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=J421_4230 {ECO:0000313|EMBL:AHG91767.1};
OS   Gemmatirosa kalamazoonensis.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatirosa.
OX   NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG91767.1, ECO:0000313|Proteomes:UP000019151};
RN   [1] {ECO:0000313|EMBL:AHG91767.1, ECO:0000313|Proteomes:UP000019151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS708 {ECO:0000313|EMBL:AHG91767.1,
RC   ECO:0000313|Proteomes:UP000019151};
RX   PubMed=24699952;
RA   Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA   Fawaz M.N., Korlach J., Tsai Y.C.;
RT   "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT   kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT   Phylum.";
RL   Genome Announc. 2:e00226-14(2014).
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; CP007128; AHG91767.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0RMS2; -.
DR   STRING; 861299.J421_4230; -.
DR   KEGG; gba:J421_4230; -.
DR   PATRIC; fig|861299.3.peg.4287; -.
DR   eggNOG; COG1048; Bacteria.
DR   HOGENOM; CLU_013476_2_1_0; -.
DR   InParanoid; W0RMS2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000019151; 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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019151}.
FT   DOMAIN          32..548
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          678..804
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   880 AA;  94750 MW;  4A0CD7ED3559C370 CRC64;
     MLLENLLRGE DGAFVKRADV EALARWNVAA PSEKEVAYRP ARVLLQDFTG VPCVVDLAAM
     RDAITALGGD AQRINPLQPV DLVIDHSVQA DEYGTPQAFL ENVSFEFERN QERYRFLRWG
     QSAFRNFSVV PPGTGICHQV NLEYLARVVF VGDGNVAYPD SLVGTDSHTT MVNGLGVFGW
     GVGGIEAEAA MLGQPLSMLV PDVVGFKLTG KLPAGATATD LVLTVTEMLR KKKVVGKFVE
     YYGTGLSGLP LADRATIANM APEYGATMGF FPVDEETLKY LRLTGRSAEQ IALVEAYTKA
     QGLFRTDATP DPVYSDTLEL DLSTVEPSIA GPRRPQDRIP LRQSKELFAT HLGEVLAKAG
     SAAGKAEIHA AKEVSAPTEL AESAVATVTA EQEADGVEVE YNGQTFRLRN GAVVIAAITS
     CTNTSNPSVM LGAGLLARKA AAKGLKAKPW VKSTLSPGSR VVTDYYEKAD LMKDLEAVGF
     YLAGYGCMTC IGNSGPLPDP IAAAVEKGKL VVSAVLSGNR NFEGRVNPHT RFNYLASPML
     VVAYALAGRM DIDLEREPLG VGAQGPVFLR DVWPTPQEIQ DTILQAVKGE MFARQYANVF
     EGDEQWRALD VPTGDTYAWD PNSTYVANPP YFEGMTMAPK GVAPIAGARC LAMLGDSITT
     DHISPAGNIS AASPAGKWLI AHGVKTREFN SYGARRGHHE VMMRGTFANI RLRNELVPGT
     EGGWTTTEPG GDAVSIYDAA MQYQQQGTPL VIVAGKEYGT GSSRDWAAKG TVLLGVRAVI
     AESFERIHRS NLVGMGVLPL EFTNGESRTS HGLTGFETYE IVGLDDTLTP RKRLTVKATA
     PDGSVKSFEV LARIDTPEEL SYFKHGGILP YVLRSLVKRA
//
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