ID A0A1G0WBR1_9BACT Unreviewed; 754 AA.
AC A0A1G0WBR1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-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=Citrate hydro-lyase {ECO:0000256|ARBA:ARBA00029682};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN ORFNames=A2475_11205 {ECO:0000313|EMBL:OGV18857.1};
OS Ignavibacteria bacterium RIFOXYC2_FULL_35_21.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798452 {ECO:0000313|EMBL:OGV18857.1, ECO:0000313|Proteomes:UP000177327};
RN [1] {ECO:0000313|EMBL:OGV18857.1, ECO:0000313|Proteomes:UP000177327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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:OGV18857.1}.
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; MHAY01000100; OGV18857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0WBR1; -.
DR STRING; 1798452.A2475_11205; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000177327; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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; cd01584; AcnA_Mitochondrial; 1.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01340; aconitase_mito; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 34..477
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 558..685
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 754 AA; 82270 MW; 61A61A3A0AA70300 CRC64;
MIFDIEMIKA RYSSFATKVD EAKKVTGKPM TLAEKILYAH LHPDSPLKEF KRGVDYVYFA
PDRVAMQDAT AQMALLQFMQ AGRPNVAVPS TVHCDHLIPA KINAAKDLEA AKDMNKEVYD
FLSSVSNKYG IGFWKPGAGI IHQVILENYA FPGGMMIGTD SHTVNAGGLG MVAIGVGGAD
AVDVMAGFPW ELKFPKLIGV RLTGKMSGWT SAKDVILKVA GILTVKGGTG AIVEYFGDGA
NSISCTGKGT ICNMGAEIGA TTSIFGFDDK MYNYLVATNR KEVADMAKNI ALHLAGDKEV
YVHPDKYFDQ VIEINLSELE PHINGPFTPD LAWPISQFAK AVKENNYPEK LDVGLIGSCT
NSSYEDISRS ASLAMQAVEK KLKVKSQFTV TPGSEMVRYT IERDGYIDLF EKIGGVVLAN
ACGPCIGQWM RPGADKQERN SIITSFNRNF AKRNDGNPNT HSFVASPEMV TAMAIAGSLL
FNPLKDKLVN EEGKEVMLAE PSGEELPSKG FAVEDAGYQA PAADGSGVEV IVNPKSDRLQ
ILSPFNSWNG EDLKGLKLLI KVKGKCTTDH ISMAGPWLKY RGHLDNISNN MLTGAVNSYN
EKTNEVKNQL TGQYAGVPDV QRDYKAKGIG TVVVGDENYG EGSSREHAAM EPRHLGVRVV
LAKSFARIHE TNLKKQGMLA LTFANKEDYE KIKEDDTIDL LGLKTFAPSV PLTMVFNHKD
GSKDEIILNH TYNEAQIEWF KAGGALNIIK KQFS
//