ID A0A0W0YWF6_9GAMM Unreviewed; 891 AA.
AC A0A0W0YWF6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:KTD60838.1};
GN ORFNames=Lsha_1555 {ECO:0000313|EMBL:KTD60838.1};
OS Legionella shakespearei DSM 23087.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD60838.1, ECO:0000313|Proteomes:UP000054600};
RN [1] {ECO:0000313|EMBL:KTD60838.1, ECO:0000313|Proteomes:UP000054600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD60838.1,
RC ECO:0000313|Proteomes:UP000054600};
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:KTD60838.1}.
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DR EMBL; LNYW01000043; KTD60838.1; -; Genomic_DNA.
DR RefSeq; WP_018578136.1; NZ_LNYW01000043.1.
DR AlphaFoldDB; A0A0W0YWF6; -.
DR STRING; 1122169.Lsha_1555; -.
DR PATRIC; fig|1122169.6.peg.1792; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000054600; 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:UP000054600}.
FT DOMAIN 76..562
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 691..817
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 891 AA; 97664 MW; 688FC2D7A78E03A5 CRC64;
MKVGRDSLST KCKLDVDGKT YHYYSLKEAE NKHFKGINRL PYSLKVLFEN LLRFEDDNTV
TTKDIKAIAE WLETKTSQNE IAFRPARVLM QDFTGVPAVV DLAAMRDAIV KMGGNPDKIS
PLSPVDLVID HSVMVDKFGT SDSLAVNTEI EMERNNERYE FLRWGQKAFS NFQVVPPGTG
ICHQVNLEYL GKTVWSSDCD GELYAYPDTL VGTDSHTTMI NGLGILGWGV GGIEAEAAML
GQPVSMLIPE VIGFKLTGKL KEGITATDLV LTVTQMLRKK GVVGKFVEFY GPGLNDLPLA
DRATISNMAP EYGATCGFFP VDKETIKYLE LSGRDKHTIA LVEAYAKAQG MWYDKDSADP
VFTDTLQLDL DTVEPSLAGP KRPQDKVNLS SLPVEFDKFL QETGKSTEKN KEFSVKNKNY
SMKHGNVVIA AITSCTNTSN PSVLMAAGLV AKKAIEKGLQ RKPWVKSSLA PGSKVVTDYL
KHAGLQTYLD QLGFNLVGYG CTTCIGNSGP LPDVISHSIS EHDLVVSSVL SGNRNFEGRV
HPQVRANWLA SPPLVVAYAL SGTTCSDLSK EPLGKDSNGN DVYLKDIWPT NAEVATEVAK
VTGGMFRKEY AEVFLGDAHW QAIKTGTGKT YEWDADSTYI QHPPFFEDLK AKPEAIKPIH
NAYILALFGD SITTDHISPA GSIKASSPAG LYLKSKGVDE KDFNSYGSRR GNHEVMMRGT
FANIRIRNEM TPGQEGGITR FVPTGAIMPI YDAAMLYQAE HQDLVVIAGK EYGTGSSRDW
AAKGTNLLGV KAVITESFER IHRSNLIGMG VLPLQFCNDM TRKTLGLDGS ERVSIDISDA
LKPGAMVPVT IERANGQKEQ IQALCRIDTA DELEYYKNGG ILQYVLRNLC A
//
