ID A0A0M8T8C9_9ACTN Unreviewed; 884 AA.
AC A0A0M8T8C9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=ADK54_03640 {ECO:0000313|EMBL:KOU53781.1};
OS Streptomyces sp. WM6378.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU53781.1, ECO:0000313|Proteomes:UP000037774};
RN [1] {ECO:0000313|Proteomes:UP000037774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-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:KOU53781.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGDD01000015; KOU53781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8T8C9; -.
DR PATRIC; fig|1415557.3.peg.786; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000037774; 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; 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; 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:KOU53781.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 71..542
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 672..795
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 383..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 93275 MW; EB183A6220045B6D CRC64;
MPQARGAGRY ISLAAAEENG LTGLHAAPRS VRILVENVLR AAVKSRDEAA VGRAMASSAA
LISACAGAGP EEEITFSPTR LVLQDHTGIP VLSDLASLRS LIAERGLDPR RARPALPVDI
VVDHSVEVNA WARPGALALN MSREYELNRE RYRFLRWAQR EMSGLRVVPP GRGIVHQMNL
EHLARVVMPD ADGLLAPDFV LGTDSHTPMV GALGVLGWGV GGIEAETALL GHSVSLLSPP
VVGVRLTGEL PVGSTATDLA LTMTRFLRDT GVVGQFVEFF GPGVPTLSLP DRATVSNMAP
EYGCTVAFFP VDEATLDYLR LTGRPEQDVS VVEAYAKEQG LFVPLGSAEE PRCARTVEFD
LSSVEPSVAG PRRPQERLPL AAVAGSFPGG PRSGDDHADE GPADGAVGIA AITSCTNTSN
PESMVIAGLV ARNAVERGLS VPPWVKTTLA PGSRAVPRYL EAAGLLPYLQ KLGFDVAGFG
CTTCIGNSGG LAPVAEEAVR REGTRLAAVL SGNRNFEGRI HPDVAAAYLA SPALVVAYAL
AGSVRTDLSS EPLGTGADGR GVRLADLWPT PAQIATAVAH VAREHFVVEK EALFQGGSEW
QDLSFPEGPV YDWPADSTYL VRSPFFDPTG RTGTADLRGA RVLVFAGDST TTDHISPAGT
IAEDSPAGRH LAGAGIARAD YNSYGCRRAN HEVLVRGAFA NPGFRNKLTP SQGGSRTLHV
PSGEVMSVYD AASRYFAERT PVVILAGRDY GFGSSRDWAA KGPALLGVRA VLAESFERIH
RSNLVGMGIV PLQFPPGRGP KELGLTGRET FEITGLETLR PRGEVTVRAL GPGGQLVGAW
RMLARVDTAR ELDYVRQGGF LRAVAAPLLD PSPPAGEPAR QGAS
//
