ID R5ZUP5_9BACT Unreviewed; 746 AA.
AC R5ZUP5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BN693_01172 {ECO:0000313|EMBL:CDA43153.1};
OS Prevotella sp. CAG:5226.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262930 {ECO:0000313|EMBL:CDA43153.1, ECO:0000313|Proteomes:UP000018184};
RN [1] {ECO:0000313|EMBL:CDA43153.1, ECO:0000313|Proteomes:UP000018184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:5226 {ECO:0000313|Proteomes:UP000018184};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- 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:CDA43153.1}.
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DR EMBL; CBBW010000092; CDA43153.1; -; Genomic_DNA.
DR AlphaFoldDB; R5ZUP5; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000018184; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018184}.
FT DOMAIN 35..477
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 556..683
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 746 AA; 80449 MW; 44693D8147ECF17F CRC64;
MTYDINMIKD FYASYAQKVN MIRSKVGRPL TYAEKVLFSH ASSDADNYDY SRGTDYATFQ
PNRVCMQDAT AQMAILQFMN AGRAQTVVPS TVHCDHLIQA YKGSEVDLPT ARKVNSEVYN
FLQSAAKRYG MGFWGPGAGI IHQVVLENYA FPGGMMVGTD SHTPNAGGLG MAAIGVGGAD
AVDVMVGTPW ELKVPRLIGV KLTGKLSGWT SPKDVILYLA GKLTTKGATN AIIEYFGPGA
ATIPATGKAT ICNMGAEVGA TTSMFAYDAQ MAAYLKCTGR ADVAELADEV AMDLRADAEV
EANPEQYYDQ CITINLDELT PYVNGPFTPD AACQVSEMAA KVKNENLPQQ VDVCLIGSCT
NSSYQDMARA ASVVKSMLAA GHALKSQLIV CPGSELVRTT AERDGILDVF VKAGATIMTN
ACGPCIGQWK RENPHPERPN SIVTSFNRNF AKRADGNPNT YAFVASPETA VGYAFTGDLT
KHPSFMPELN CCMPQGEALP ANGYASDAAC VQAIKPAYNI QPDASVEVEI KPDSERLQRL
QPFAAWNGED FQQLPLLIKV KGKCTTDHIS MAGPWLRYRG HLQNISRNML LGAVNAFTGE
TGCVKDLTTG QDSEVWQAAA HYRDAKGGSV IVAEDNYGEG SSREHAAMEP RYLGVKVVLV
KSFARIHETN LKKQGVLALT FANPADYEKV KEGDAFTVKC SSLAVGKQVQ IDIHHANGET
DTIWANHTYN NLQIAWFKAG SALAAS
//
