ID A0A078L2R1_9GAMM Unreviewed; 946 AA.
AC A0A078L2R1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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_2 {ECO:0000313|EMBL:CDZ79451.1};
GN ORFNames=BN59_03769 {ECO:0000313|EMBL:CDZ79451.1};
OS Legionella massiliensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1034943 {ECO:0000313|EMBL:CDZ79451.1, ECO:0000313|Proteomes:UP000044071};
RN [1] {ECO:0000313|EMBL:CDZ79451.1, ECO:0000313|Proteomes:UP000044071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUN-2014) 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}.
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DR EMBL; CCSB01000005; CDZ79451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078L2R1; -.
DR STRING; 1034943.BN59_03769; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000044071; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000044071}.
FT DOMAIN 133..615
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 744..871
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 946 AA; 105664 MW; CC87BEC04428B2E6 CRC64;
MLQIKRWINW IISPKLERNQ AIINESSEES FPASDPPSWA AGTHDLKHHR TSSNLVLTHE
FHKSIQQILS VNGNEYHYYS LKEAEQGGLK DLSKLPFTLK ILLENLLRHL DGHTVTVDDL
KAIIEWLKLK SSDHEIAYRP ARVLMQDFTG VPAIVDLAAM RAAIKKLGGN SEKINPLSPV
DLIIDHSIQV DEFLTPNAFT VNAQMEMERN HERYEFLRWG QKAFKNFRVV PPDTGICHQI
NLEYLAKTVW TQQINGKIYA YPDTLVGTDS HTTMINGLGV LGWGVGGIEA EAAMLGQPIS
LLIPEVIGVK LVGQLQEGIT ATDLVLSITH LLREKGVVGK FVEYFGDGLR YLSIADRATI
GNMSPEYGAT CGFFPIDEIT LDYLRLSGRE EQDIALVEAY AKTQGLWHDP HLEPVYTDIV
TLDLSSIKAC IAGPKRPQDR IELSYLTSTF HQFLTENNRT EEKEKSFITD SNFEMHHGDV
VIAAITSCTN TSNPNVLVAA GLLAKKAVEK GITRKSWVKT SFAPGSQVVT RYLEETNLQK
YLNELGFTLV GYGCTTCIGN SGPLLESVEK TVIEHDLIVS AVLSGNRNFE GRIHPLVKAN
WLASPPLVVA FALAGTTLID LTKDPLGKDA SGNPVYLKDI WPTNAEIACE VAKISRNMFH
DTYAHIFEGT DEWRAMKISK SDTYAWPVNS TYIQHPPYFD EMNVNPEKIK EIKGARILAL
FGDSITTDHI SPAGSIKPDS PAGKYLQYKG VSIKDFNSYG SRRGNHEVMM RGTFANIRIR
NEMTPDVEGG FTKHIPSNEI LPIYDAAMRY KKERTALVII AGKEYGTGSS RDWAAKGPKL
QGVLAVIAES FERIHRSNLI GMGILPLEFP EGVTRKTLQI TGSELIDIVG LTHEMKPRMQ
VKIIIHKEDK TQNEIHLILR IDTLNELDYY KNGGILHYVL RGMLKT
//