ID A0A0N8KFA3_9RHOB Unreviewed; 919 AA. AC A0A0N8KFA3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 13-SEP-2023, entry version 33. 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 Name=acnA {ECO:0000313|EMBL:KPQ13578.1}; GN ORFNames=HLUCCO18_17360 {ECO:0000313|EMBL:KPQ13578.1}; OS Rhodobacteraceae bacterium HLUCCO18. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae. OX NCBI_TaxID=1666917 {ECO:0000313|EMBL:KPQ13578.1, ECO:0000313|Proteomes:UP000050333}; RN [1] {ECO:0000313|EMBL:KPQ13578.1, ECO:0000313|Proteomes:UP000050333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLUCCO18 {ECO:0000313|EMBL:KPQ13578.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-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=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 -!- 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:KPQ13578.1}. 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; LJSY01000062; KPQ13578.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0N8KFA3; -. DR STRING; 1666917.HLUCCO18_17360; -. DR EnsemblBacteria; KPQ13578; KPQ13578; HLUCCO18_17360. DR PATRIC; fig|1666917.4.peg.3216; -. DR UniPathway; UPA00223; UER00718. DR Proteomes; UP000050333; 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:0047780; F:citrate dehydratase 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 NCBIfam; TIGR01341; aconitase_1; 1. DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1. DR PANTHER; PTHR11670:SF54; CITRATE HYDRO-LYASE; 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, 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361275}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}. FT DOMAIN 80..584 FT /note="Aconitase/3-isopropylmalate dehydratase large FT subunit alpha/beta/alpha" FT /evidence="ECO:0000259|Pfam:PF00330" FT DOMAIN 714..839 FT /note="Aconitase A/isopropylmalate dehydratase small FT subunit swivel" FT /evidence="ECO:0000259|Pfam:PF00694" SQ SEQUENCE 919 AA; 99729 MW; 43A400A7100941A5 CRC64; MPITVGHDTA KTRKTLKVGD RTYAYYSIAA AEAAGLGDFS KLPAALKVVL ENMLRFEDGK TVSVDDIKAF STWAAQGGKN PREIAYRPAR VLMQDFTGVP AVVDLAAMRD GIKALGGDAQ KINPLNPVDL VIDHSVMIDE FGNPRAFQMN VDREYERNME RYTFLKWGQS AFDNFRVVPP GTGICHQVNL EYLAKTIWSD TDQSGEMVAY PDTLVGTDSH TTMVNGAAVL GWGVGGIEAE AAMLGQPISM LIPEVVGFEL TGEMMEGTTG TDLVLKVVEM LRAKGVVGKF VEFYGAGLDT LPLADRATIA NMAPEYGATC GFFPIDGETL RYLRNTGRPE EVLDLVETYA KENGFWRGAD YAPVYTDTLS LDMCTIVPAI SGPKRPQDYT TLDRAARAFF EVVSEFRGED ESRRATDMAS EGPTPDALID PRRTAKVEGE EYELRDGSVV IASITSCTNT SNPYVMIGAG LVARKARALG LTRKPWVKTS LAPGSQVVSA YLEAAGLQED LDAIGFNLVG YGCTTCIGNS GPLQPEISKA ISDNDLIATS VLSGNRNFEG RISPDVRANY LASPPLVVAY ALAGDMNIDI SSEPLGQTPE GRDVYLKDVW PTQKEIADLV EATVTREAFQ TKYADVFKGD EKWQGVEVPQ QETYDWPATS TYIQNPPYFE GMGAEPGTIS NIEGARVLAI LGDMITTDHI SPAGSFKETT PAGKYLTERQ VPVREFNSYG SRRGNHQIMM RGTFANIRIR NEMLDGVEGG YTLGPDGQQT SIFDAAMAYM EEGTPLVIFG GEQYGAGSSR DWAAKGTALL GVKAVIAESF ERIHRSNLVG MGVIPFEFTG GDTRKTLGLK GDETVDIHGL DAVTPLMETR ATITYGDGTT KDITLKCRID TAIEIEYIEH GGVLHYVLRD LAKAPVAAE //