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Database: UniProt
Entry: A0A078L2R1_9GAMM
LinkDB: A0A078L2R1_9GAMM
Original site: A0A078L2R1_9GAMM 
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
//
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