ID Q9RNH9_STRCH Unreviewed; 904 AA.
AC Q9RNH9;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 139.
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=sacA {ECO:0000313|EMBL:AAD53955.1};
OS Streptomyces coelicolor.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=1902 {ECO:0000313|EMBL:AAD53955.1};
RN [1] {ECO:0000313|EMBL:AAD53955.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MT1110 {ECO:0000313|EMBL:AAD53955.1};
RX PubMed=11325949; DOI=10.1128/JB.183.10.3193-3203.2001;
RA Viollier P.H., Nguyen K.T., Minas W., Folcher M., Dale G.E., Thompson C.J.;
RT "Roles of aconitase in growth, metabolism, and morphological
RT differentiation of Streptomyces coelicolor.";
RL J. Bacteriol. 183:3193-3203(2001).
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}.
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DR EMBL; AF180948; AAD53955.1; -; Genomic_DNA.
DR RefSeq; WP_003972923.1; NZ_VNIH01000007.1.
DR AlphaFoldDB; Q9RNH9; -.
DR SMR; Q9RNH9; -.
DR OMA; NGGIMQY; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
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; 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:AAD53955.1};
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"
SQ SEQUENCE 904 AA; 97380 MW; CFE76ABC492E822D CRC64;
MSANSFDARS TLQVGDESYE IFRLDKVEGS ARLPYSLKVL LENLLRTEDG ANITADHIRA
LGGWDSQAQP SQEIQFTPAR VIMQDFTGVP CVVDLATMRE AVKELGGDPN KINPLSPAEM
VIDHSVIADK FGTNDAFQQN VDLEYGRNKE RYQFLRWGQT AFDDFKVVPP GTGIVHQVNI
EHLARVVMTR DGKAYPDTLV GTDSHTTMVN GLGVLGWGVG GIEAEAAMLG QPVSMLIPRV
VGFKLTGELT PGTTATDLVL TITEMLRKHG VVGKFVEFYG EGVAATSLAN RATIGNMSPE
FGSTAAIFPV DDETLNYMRL TGRSAHQVAL VEAYAKEQGL WLDPKAEPDF SEKLELDLST
VVPSIAGPKR PQDRIVLANA AEQFKQDVRN YVDSVDEAGQ ESFPASDAPA VTNGVPSNPV
PVTAPDGTTY ELDHGAVTVA AITSCTNTSN PYVMVAAALV AKKAVEKGLT RKPWVKTTLA
PGSKVVTDYF EKAGLTPYLD KVGFNLVGYG CTTCIGNSGP LPDEVSKAVN DHDLAVTSVL
SGNRNFEGRI NPDVKMNYLA SPPLVVAYAL AGSMKVDVTK DALGVDQDGN PVFLKDIWPS
EAEVNDVVAN AIGEDMFSKS YSDVFAGDAQ WQALSIPTGD TFEWDGESTY VRKPPYFEGM
GMEPAPVEDI SGARVLAKLG DSVTTDHISP AGAIKADTPA GKYLTEHGVE RRDFNSYGSR
RGNHEIMIRG TFANIRLRNQ IAPGTEGGYT RDFTQDGGPV SFIYDASRNY IEQGTPLVVL
AGKEYGSGSS RDWAAKGTAL LGVKAVVAES YERIHRSNLI GMGVLPLQFP EGHTAESLGL
TGEETFSVSG VTELNEGTTP RTVKVTTDTG VEFDAVVRID TPGEADYYRN GGILQYVLRS
LIRK
//
