ID A0A0F2CAK6_9MICO Unreviewed; 954 AA.
AC A0A0F2CAK6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:KJQ54695.1};
GN ORFNames=RS85_01425 {ECO:0000313|EMBL:KJQ54695.1};
OS Microbacterium sp. SA39.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ54695.1, ECO:0000313|Proteomes:UP000033425};
RN [1] {ECO:0000313|EMBL:KJQ54695.1, ECO:0000313|Proteomes:UP000033425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA39 {ECO:0000313|EMBL:KJQ54695.1,
RC ECO:0000313|Proteomes:UP000033425};
RA Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N., Brader G.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (JAN-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:KJQ54695.1}.
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DR EMBL; JXRU01000031; KJQ54695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2CAK6; -.
DR STRING; 1263625.RS85_01425; -.
DR PATRIC; fig|1263625.4.peg.1435; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000033425; 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:KJQ54695.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000033425}.
FT DOMAIN 65..609
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 738..874
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 954 AA; 103052 MW; 5F3CC1C5B6F11489 CRC64;
MSTVNSFGAK STLTVGSTDY EIFRIDTVPG FDKLPFSLKV LLENLLRTED GANVTKAQIE
ALGSWDAAAE PNTEIQFTPA RVVMQDFTGV PCIVDLATMR EAVTALGGDA NRINPLSPAE
MVIDHSVIAD LFGSENALER NVEIEYERNG ERYQFLRWGQ TAFSDFKVVP PGTGIVHQVN
IEHLAKVIYD RDVDGVLRAY PDTCVGTDSH TTMVNGLGVL GWGVGGIEAE AAMLGQPVSM
LIPRVVGFKL SGEIPAGVTA TDVVLTITEQ LRQHGVVGKF VEFYGEGVAS VPLANRATIG
NMSPEFGSTA AIFPIDDVTL DYLRLTGRSD EAVALVEAYA KEQKLWHDAS VEPTFSEYLE
LDLGTVVPSI AGPKRPQDRI LLSEAKAQFE QDILNYASIG EETVEVEGTF PASDPGTAPG
VEREHVAENG VSHQHEAEHA ESMLLFSGGP HPASKPVEVA TPDGQRYMLD NGAVTLAAIT
SCTNTSNPSV MIAAGLVARK ARQKGLKQKP WVKTTLGPGS KVVTDYYEKS GLDKDLEGLG
FYTVGYGCTI CIGNSGPLIE EVSEAINSHD LAVTAVLSGN RNFEGRISPD VKMNYLASPP
LVIAYALAGS MHFDFENDAL GKGTDGEDVF LRDIWPTPAE VQELVDSSIS REQFIKQYAT
VFDGDERWRS LPTPDDAIFQ WDEDSTYVRK APYFDGMTME LTPVTDIHDA RVMATLGDSV
TTDHISPAGN IKAGTPAAEY LTAHGVDRKD FNSFGSRRGN HEVMIRGTFA NIRLKNAMVS
AVNDGQVVEG GFTRDFTQPG GPQSYIYDAS MNYQEQGTPL VIFGGKEYGS GSSRDWAAKG
TSLLGVKAVI TESFERIHRS NLIGMGVVPL QFPAGESWES LGLDGTETVS ITGLTELNNG
VTPKTVRVTA TPSEHSPEGK QTVEFDAVVR IDTPGEADYY RNGGILQYVL RSLV
//
