ID A0A136JVM0_9BACT Unreviewed; 956 AA.
AC A0A136JVM0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ORFNames=UZ17_ACD001001847 {ECO:0000313|EMBL:KXK01218.1};
OS Acidobacteria bacterium OLB17.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1617423 {ECO:0000313|EMBL:KXK01218.1, ECO:0000313|Proteomes:UP000070331};
RN [1] {ECO:0000313|EMBL:KXK01218.1, ECO:0000313|Proteomes:UP000070331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB17 {ECO:0000313|EMBL:KXK01218.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Dutilh B.E., Jetten M.S.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (OCT-2015) 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:KXK01218.1}.
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DR EMBL; LLEU01000036; KXK01218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136JVM0; -.
DR STRING; 1617423.UZ17_ACD001001847; -.
DR PATRIC; fig|1617423.3.peg.1925; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000070331; Unassembled WGS sequence.
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; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:KXK01218.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 80..622
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 752..879
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 423..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 103340 MW; B618F5D4A0037014 CRC64;
MTHELFGSRQ TFKTGKGTDG IFYSLPALEK AGLGTISRLP VSIRIVLESV LRNFDGGVKV
SEQSIRDLAA WTPNGERVSE IPFIVARVLL QDFTGVPLLV DLAAMRSAVD RMGGDVKVVE
PLVPVDLVID HSVQVDFAGS QIAYERNMEV EFRRNDQRYR FLKWGMQAFN GFGVIPPGIG
IVHQVNLEYL AKGVFEKNGT YFPDSLVGTD SHTTMINGLG IVAWGVGGIE AEAGMLGQPV
YFLTPDVVGV HISGELPSGA TATDLVLRIT EELRKTNVVG KFVEYFGEGA AALNATDRAT
IANMAPEYGA TMGFFGVDEK TLDYMRNTGR SDEQIETIRN YYLAQEMFGI PRSGDVDYSQ
VVEIDLSTIK PAVAGPKRPQ DRIELDQLDD RFKELFTMPA ASGGFGKKAS DLEERFPVTI
GSVEPECVGG GGEQGQRTAP EAAHRNTSTK NTSVATELEM MNNRPTPNCV PLDENGNGKV
SIGNGDVLIA AITSCTNTSN PSVMLAAGLL AKKAVEKGLK PPKYVKTSLA PGSRVVTEYL
EKTGLQPYLD QLGFELVGYG CTTCIGNSGP LDPAIEAQVT GNDLIAASVL SGNRNFEARV
HQNIKANFLM SPPLVVAFAL AGTVLNDMET EPLGKDKDGN DVFLKDIWPS LDEVRGLLAA
AYDAETYKKL YSQFADQNPL WNNITSSTGA IYEWDPDSTY IQEPPYFDNF GKPTEGFADI
RSARALAIFG DSVTTDHISP AGAIKANSPA GEYLQSLGVE PKDFNSYGSR RGNDRVMLRG
TFANVRIKNT MVSPTEGGFT KHYPDGEETT IYDAAMRYAA EGVPLVIFAG KEYGTGSSRD
WAAKGTALMG VKAVVAESFE RIHRSNLVGM GVLPLQFKDG QTAASLGLDG TETFDLSGLG
GIDVQPRQDV KLTIRKANGS SVETTVRLRI DTPIEVEYYK AGGILPYVLH QLTKGS
//
