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Database: UniProt
Entry: A0A0N1FW02_9ACTN
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ID   A0A0N1FW02_9ACTN        Unreviewed;       904 AA.
AC   A0A0N1FW02;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=OV450_4223 {ECO:0000313|EMBL:KPI04595.1};
OS   Actinobacteria bacterium OV450.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592328 {ECO:0000313|EMBL:KPI04595.1, ECO:0000313|Proteomes:UP000037826};
RN   [1] {ECO:0000313|EMBL:KPI04595.1, ECO:0000313|Proteomes:UP000037826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV450 {ECO:0000313|EMBL:KPI04595.1,
RC   ECO:0000313|Proteomes:UP000037826};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (SEP-2015) 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=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC         aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC         Evidence={ECO:0000256|ARBA:ARBA00000118};
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   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000256|ARBA:ARBA00005026}.
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:KPI04595.1}.
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DR   EMBL; LJCW01000339; KPI04595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1FW02; -.
DR   PATRIC; fig|1592328.3.peg.6807; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000037826; Unassembled WGS sequence.
DR   GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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; CITRATE HYDRO-LYASE; 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:KPI04595.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          64..572
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          702..831
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
FT   REGION          398..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   904 AA;  97149 MW;  52F973A41FA994F2 CRC64;
     MSANSFDARS TLQVGDESYE IFRLDKVEGS ARLPYSLKVL LENLLRTEDG ANITADHIRS
     LGNWDSQAQP SEEIQFTPAR VIMQDFTGVP CVVDLATMRE AVKALGGDPA KINPLSPAEM
     VIDHSVIADK FGTKDAFAQN VELEYGRNKE RYQFLRWGQT AFDDFKVVPP GTGIVHQVNI
     EHLARTVMVR NGQAYPDTLV GTDSHTTMVN GLGVLGWGVG GIEAEAAMLG QPVSMLIPRV
     VGFKLTGELP TGTTATDLVL TITEMLRKHG VVGKFVEFYG EGVAATSLAN RATIGNMSPE
     FGSTAAIFPI DGETLKYLRL TGRDAQQVAL VEAYAKEQGL WLAPAAEPDF SEKLELDLST
     VVPSIAGPKR PQDRIVLANA AEQFAVDVRN YVSDDEEAGK ESFPASDAPA AVNGVPTRPT
     QVTLADGTSF EIDHGAVTVA AITSCTNTSN PYVMVAAALV AKKAVEKGLS RKPWVKTTLA
     PGSKVVTDYF DKAGLTPYLD KMGFNLVGYG CTTCIGNSGP LDEEISKAIN EHDLAVTSVL
     SGNRNFEGRI NPDVKMNYLA SPPLVVAYAI AGSMKVDITK DAIGIDTEGK PVFLQDIWPS
     EAEVNDVVAN AIGEDMFSKS YQDVFAGDAQ WQALSIPTGN TFEWDPQSTY VRKPPYFEGM
     TMETTPVSDI AGARVLAKLG DSVTTDHISP AGAIKADTPA GKYLTEHGVE RRDFNSYGSR
     RGNHEVMIRG TFANIRLRNQ IAPGTEGGFT RDFTVEGAPV AFIYDASQNY QAAGIPLVIL
     AGKEYGSGSS RDWAAKGTAL LGVKAVIAES YERIHRSNLI GMGVLPLQFP EGASAAALGL
     TGEETFSFTG VEELNNGTTP RTVKVTTDTG VEFDAVVRID TPGEADYYRN GGIMQYVLRN
     LIRG
//
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