ID A0A0S9RBV3_9ACTN Unreviewed; 933 AA.
AC A0A0S9RBV3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.99 {ECO:0000256|ARBA:ARBA00013250};
DE AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000256|ARBA:ARBA00031613};
DE AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000256|ARBA:ARBA00030846};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=Probable 2-methyl-cis-aconitate hydratase {ECO:0000256|ARBA:ARBA00033025};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN Name=acnA {ECO:0000313|EMBL:KQP79669.1};
GN ORFNames=ASF37_01225 {ECO:0000313|EMBL:KQP79669.1};
OS Aeromicrobium sp. Leaf289.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP79669.1, ECO:0000313|Proteomes:UP000051640};
RN [1] {ECO:0000313|Proteomes:UP000051640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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:KQP79669.1}.
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DR EMBL; LMNK01000001; KQP79669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S9RBV3; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000051640; Unassembled WGS sequence.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:KQP79669.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051640}.
FT DOMAIN 76..604
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 734..862
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 418..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 933 AA; 100343 MW; 66E30F172FBF5BF0 CRC64;
MEHDAKETLM VDSFNAEQTL EVGDASYTYF KLDAVKGDGL DVASLPFSLK VLLEALLRTE
DGADITKADI EALAGWDANA DPSKEIQFTP ARVIMQDFTG VPCVVDLATM REAMADLGGD
ATKINPLAPA EMVIDHSVIA DVFGTPEAFE RNVEIEYERN RERYQFLRWG QGAFDDFKVV
PPGTGIVHQV NIEKLARVVF DKNGVVYPDS CVGTDSHTTM VNGLGVVGWG VGGIEAEAAM
LGQPISMLIP RVVGFKLSGE LPQGATATDL VLVITEMLRK HGVVGKFVEF YGSGVGAVPL
ANRATIGNMS PEYGSTIAVF PIDDETTKYL RLTGRDEEQI ALVEAYAKAQ GLWHDPDHEP
RFSEYLELDL GDVVPSIAGP KRPQDRVSLT ESKGSFRTAL ADYTEQDVNG YDEAVAESFP
ASDAPSSSDD GTNGDKPNAP APSGAGRPSN PQHVRLEDGT EFELDHGAVT IAAITSCTNT
SNPSVMIGAG LLAKKAVEKG LQRKPWVKTT LAPGSKVVTD YYAKSGLDVY LDKLGFNLVG
YGCTTCIGNS GPLIPEVSAA VNEGDLAVTA VLSGNRNFEG RINPDIKMNY LASPPLVIAY
ALAGSMDVDL FNEPLGTDAD GNDVFMKDIW PSASEVEDVI ASSISSDTFS KEYADVFAGD
ERWQNLPTPD GDVFEWDPES TYVRKAPYFD GMDREPSPVE EVSGARVLLK LGDSVTTDHI
SPAGAIKKDS PAGAYLSEHG IEPRDFNSYG SRRGNHEVMI RGTFANIRLR NQMAPGTEGG
YTRNLIADGE VTSVFEASEA YQEAGVPLVV LAGKEYGSGS SRDWAAKGTA LLGVKVVIAE
SYERIHRSNL IGMGVLPLQY PEGENAESLG LTGEETFDFT GITKLNDGET PRTVHVKAGD
VEFDAVVRID TPGEANYYRN GGIMPYVLRS LLD
//
