ID E2PV06_STRCL Unreviewed; 913 AA.
AC E2PV06;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:EFG09903.1};
GN ORFNames=SCLAV_4830 {ECO:0000313|EMBL:EFG09903.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG09903.1, ECO:0000313|Proteomes:UP000002357};
RN [1] {ECO:0000313|EMBL:EFG09903.1, ECO:0000313|Proteomes:UP000002357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX PubMed=20624727; DOI=10.1093/gbe/evq013;
RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA Breitling R., Takano E.;
RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT evolutionary reservoir of secondary metabolic pathways.";
RL Genome Biol. Evol. 2:212-224(2010).
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; CM000913; EFG09903.1; -; Genomic_DNA.
DR AlphaFoldDB; E2PV06; -.
DR STRING; 1901.BB341_04765; -.
DR eggNOG; COG1048; Bacteria.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000002357; Chromosome.
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:EFG09903.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002357}.
FT DOMAIN 69..577
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 707..840
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 402..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 98214 MW; 3D9BCE5FB76FA6AF CRC64;
MKETVVSANS FDARSTLRVG DESYEIFKLD KVEGSARLPY SLKVLLENLL RTEDGANITA
DHIRALGGWD SQAQPSQEIQ FTPARVIMQD FTGVPCVVDL ATMREAVKEL GGDPAKINPL
APAELVIDHS VIADKFGTKD AFGQNVELEY GRNKERYQFL RWGQTAFDEF KVVPPGTGIV
HQVNIEHLAR TVMVRNGQAY PDTLVGTDSH TTMVNGLGVL GWGVGGIEAE AAMLGQPVSM
LIPRVVGFKL TGELTPGTTA TDLVLTITEM LRKHGVVGKF VEFYGEGVAA TSLANRATIG
NMSPEFGSTA AIFPIDGETL NYLRLTGRSQ QQVALVEAYA KEQGLWLDPT AEPDFSEKLE
LDLSTVVPSI AGPKRPQDRI VLANAAEQFA LDVRNYVADD EEAGKESFPA SDAPASSDGV
PTKPTLVTAP DGSTYEIDHG AVTVAAITSC TNTSNPYVMV AAALVAKKAV EKGLTRKPWV
KTTLAPGSKV VTDYFDKAGL TPYLDKVGFN LVGYGCTTCI GNSGPLPEEV SKAVNEADLA
VTSVLSGNRN FEGRINPDVK MNYLASPPLV VAYALAGSMK VDITREALGI DTEGNPVYLK
DIWPTEAEVN DVVANAIGED MFAKSYQDVF AGDAQWQALP IPTGNTFEWD TESTYVRKPP
YFEGMEMEPA PVQDIAGARV LAKLGDSVTT DHISPAGAIK ADTPAGQYLT EHGVERRDFN
SYGSRRGNHE VMIRGTFANI RLRNQIAPGT EGGFTRDFTQ AATADAAPVS FIYDASRNYI
EQGIPLVILA GKEYGSGSSR DWAAKGTALL GVKAVIAESY ERIHRSNLIG MGVLPLQFPE
GASAQSLGLT GEETFSFTGV TELNEGTTPR TVKVTTDTGV EFDAVVRIDT PGEADYYRNG
GIMQYVLRNL IRG
//
