ID A0A257CLC0_9BURK Unreviewed; 980 AA.
AC A0A257CLC0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN Name=acnA {ECO:0000313|EMBL:OYT90077.1};
GN ORFNames=CFE43_20115 {ECO:0000313|EMBL:OYT90077.1};
OS Burkholderiales bacterium PBB3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=2015565 {ECO:0000313|EMBL:OYT90077.1, ECO:0000313|Proteomes:UP000216249};
RN [1] {ECO:0000313|EMBL:OYT90077.1, ECO:0000313|Proteomes:UP000216249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBB3 {ECO:0000313|EMBL:OYT90077.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:OYT90077.1}.
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DR EMBL; NKIK01000054; OYT90077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257CLC0; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000216249; Unassembled WGS sequence.
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; cd01586; AcnA_IRP; 1.
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 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:OYT90077.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000216249}.
FT DOMAIN 76..622
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 771..906
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 980 AA; 105804 MW; 20E42D788A93C7CA CRC64;
MPHAFASTLK TFKTASGKTG SFYSLPVLAK KFPNVKRLPV SMRIVLESVL RNCDGKKVTA
EPVAEVANWS PTGHRTNEIP FVVSRVVLQD FTGVPLLADL AAMRSVAVKL GKNPKRIEPL
VPVDLVVDHS VMVDHYGKKN SLDLNMKLEF QRNRERYEFM KWGMQAFDTF RVVPPGFGIV
HQVNLEYLAR GVHKTKGDAK NGPIYYPDTL VGTDSHTTMI NGIGVVAWGC GGIEAEAAML
GQPVYFLTPD VVGFELTGRL REGVTATDLV LTVTEILRRH KVVGKFVEFY GEGTRTLSLP
DRATIANMAP EYGATMGFFP VDEKTMEYFE GTGRTKPEME AFEAYFKAQG LFGVPKSGDI
DYSQVVKLDL GNVTPSLAGP KRPQDRIELG NVASQFESLF SKPNAENGFN QNASVFHTRH
LARASDVPAD AKIPKSPSTP LGAPRQVLEM ESSKPTLAAH HAAPSTVAAT AVAAGSKSDV
TIGNGDVLIA AITSCTNTSN PSVLLAAGLL AKKAVEAGLK VKPHIKTSLA PGSRIVTEYL
TETGLLPYLE KLGFALAGYG CTTCIGNAGD LTPELNDVIT KNDLICAAVL SGNRNFEARI
HPNLKANFLA SPPLVVAYAI AGTVNRDLMT QPVGKGKGGK DVYLGDIWPT SDEIYKLLKY
AMKGKAFREN YAKVKTEPGK LWDKIKGVAG QAYTWPTSTY IAEPPFFADF AMDSGASPAL
SMVSTATNGT ESSTEEQVQG ARIMALFGDS ITTDHISPAG SIKESSPAGQ WLRAHGVLKA
DFNSYGARRG NHDVMMRGTF ANVRIKNLMI PPDAAGSREE GGVTIYQHDG PDQGNKMFIY
DAAIQYMADG VPTVIFAGEE YGTGSSRDWA AKGTQLLGIK AVVAKSFERI HRSNLVGMGV
LPLQFKGSDS WQSLGLKGDE RIDVIPDAKL TPQSDATLRI TRADGSTQEL TLTLRVDTPI
EVDYYRAGGI LPFVLRQLLA
//
