ID A0A0W0VMV7_9GAMM Unreviewed; 943 AA.
AC A0A0W0VMV7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, 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_1 {ECO:0000313|EMBL:KTD21490.1};
GN ORFNames=Lisr_1599 {ECO:0000313|EMBL:KTD21490.1};
OS Legionella israelensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=454 {ECO:0000313|EMBL:KTD21490.1, ECO:0000313|Proteomes:UP000054761};
RN [1] {ECO:0000313|EMBL:KTD21490.1, ECO:0000313|Proteomes:UP000054761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD21490.1,
RC ECO:0000313|Proteomes:UP000054761};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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:KTD21490.1}.
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DR EMBL; LNYH01000093; KTD21490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0VMV7; -.
DR STRING; 454.Lisr_1599; -.
DR PATRIC; fig|454.4.peg.1741; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000054761; 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 NCBIfam; TIGR01341; aconitase_1; 1.
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, 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054761}.
FT DOMAIN 130..612
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 741..868
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 943 AA; 104527 MW; 7FF9E079E9B3284B CRC64;
MLPIKNWIMG AKQKNNQAII NESSEDSFPA SDPPSWAGGI QEIKQHTIVS DLVLTSEFHK
STQQILSIHG IAYHYYSLRA AEQGGLKDLS KLPYTLKILL ENLLRHLDGQ SVTVDDLKAI
IEWLKLKTSN REIVYRPARV LMQDFTGVPA IVDLAAMRAA IEKLGGNPEQ INPLSAVDLI
IDHSIQIDQF LIPDAFTINA TMEMERNYER YEFLRWGQKA FRNFRVVPPD TGICHQVNLE
YLAKTVWTQE INGKIYAYPD TLVGTDSHTT MINGLGVLGW GVGGIEAEAA MLGQPISLLI
PEVIGVKLTG QLQEGITATD LVLSVTHLLR EKGVVGKFVE FFGDGLRHLS LADRATISNM
SPEYGATCGF FPIDEATLDY LRLSGREEQS VALVEAYAKI QGLWHDPQAE LIYTDLVTLD
LSTIRACIAG PKRPQDQVEL SKLANTFDKL LAENKRSEER EQSFDTDMNY ELHHGDVVIA
AITSCTNTSN PNVLIAAGLL AKKAVEKGMT RKPWVKTSFA PGSQVVTLYL EKTNLQKYLN
ELGFTLAGYG CTTCIGNSGP LPEPVEKIVI ENDLIVSAVL SGNRNFEGRI HPLVKANWLA
SPPLVVAFAI AGTVLIDLTK DPLGEDKARN PVYLHDLWPT NDEIAREVAT ITNKMFHDTY
ANIFTGTDEW RSMKISESDT YAWPLDSTYI QHPPFFDGMG VTPEKIKNIK GARILALFGD
SITTDHISPA GSIKPESPAG EYLQSKGVTI KDFNSYGSRR GNHEVMVRGT FANIRIRNEM
TPELEGGFTK YIPTGEIMSI YDAAMRYKNG RTALVVIAGR EYGTGSSRDW AAKGPKLQGV
VAVMAESFER IHRSNLIGMG ILPLEFPEGV TRKTLQISGS EVIDIIGLTH QMKPRMPVKV
VIHREDGNQS EVTLISRIDT LNELDYYKNG GILHYVLRGM LKK
//
