ACON_LEGPH
ID ACON_LEGPH Reviewed; 891 AA.
AC P37032; Q5ZUV2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Aconitate hydratase A {ECO:0000303|PubMed:8366052};
DE Short=ACN {ECO:0000303|PubMed:8366052};
DE Short=Aconitase {ECO:0000303|PubMed:8366052};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:Q8ZP52};
DE AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE AltName: Full=IP210 {ECO:0000303|PubMed:8366052};
DE AltName: Full=Iron-responsive protein-like {ECO:0000305|PubMed:8366052};
DE Short=IRP-like {ECO:0000305|PubMed:8366052};
DE AltName: Full=Major iron-containing protein {ECO:0000303|PubMed:8366052};
DE Short=MICP {ECO:0000303|PubMed:8366052};
DE AltName: Full=Probable 2-methyl-cis-aconitate hydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE EC=4.2.1.99 {ECO:0000250|UniProtKB:Q8ZP52};
DE AltName: Full=RNA-binding protein {ECO:0000305|PubMed:8366052};
GN Name=acn; OrderedLocusNames=lpg1690;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RX PubMed=8366052; DOI=10.1128/jb.175.17.5666-5676.1993;
RA Mengaud J.M., Horwitz M.A.;
RT "The major iron-containing protein of Legionella pneumophila is an
RT aconitase homologous with the human iron-responsive element-binding
RT protein.";
RL J. Bacteriol. 175:5666-5676(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and probably
CC the 2-methylcitrate cycle I (propionate degradation route). Catalyzes
CC the reversible isomerization of citrate to isocitrate via cis-
CC aconitate. The apo form of AcnA functions as a RNA-binding regulatory
CC protein (PubMed:8366052). Could catalyze the hydration of 2-methyl-cis-
CC aconitate to yield (2R,3S)-2-methylisocitrate (By similarity).
CC {ECO:0000250|UniProtKB:Q8ZP52, ECO:0000269|PubMed:8366052}.
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:0000250|UniProtKB:Q8ZP52};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000250|UniProtKB:Q8ZP52};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P09339};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P09339};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000305}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8366052}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; L22081; AAA25295.1; -; Genomic_DNA.
DR EMBL; AE017354; AAU27770.1; -; Genomic_DNA.
DR PIR; B48642; B48642.
DR RefSeq; WP_010947417.1; NC_002942.5.
DR RefSeq; YP_095717.1; NC_002942.5.
DR AlphaFoldDB; P37032; -.
DR SMR; P37032; -.
DR STRING; 272624.lpg1690; -.
DR PaxDb; P37032; -.
DR PRIDE; P37032; -.
DR EnsemblBacteria; AAU27770; AAU27770; lpg1690.
DR GeneID; 66490822; -.
DR KEGG; lpn:lpg1690; -.
DR PATRIC; fig|272624.6.peg.1771; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_6; -.
DR OMA; NGGIMQY; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0003994; F:aconitate hydratase activity; ISS:UniProtKB.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
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 PANTHER; PTHR11670; PTHR11670; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01341; aconitase_1; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW RNA-binding; Tricarboxylic acid cycle.
FT CHAIN 1..891
FT /note="Aconitate hydratase A"
FT /id="PRO_0000076662"
FT BINDING 435
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 501
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 504
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 891 AA; 98209 MW; F81FC99520859B48 CRC64;
MKVGQDSLST KSQLTVDGKT YNYYSLKEAE NKHFKGINRL PYSLKVLLEN LLRFEDGNTV
TTKDIKAIAD WLHNKTSQHE IAFRPTRVLM QDFTGVPAVV DLAAMRTAIV KMGGNADKIS
PLSPVDLVID HSVMVDKFAS ADALEVNTKI EIERNKERYE FLRWGQKAFS NFQVVPPGTG
ICHQVNLEYL GKTVWNSEND GQLYAYPDTL VGTDSHTTMI NGLGVLGWGV GGIEAEAAML
GQPVSMLIPE VIGFKLSGKL KEGITATDLV LTVTQMLRKK GVVGKFVEFY GPGLNDLPLA
DRATISNMAP EYGATCGFFP VDKETIKYLE LTGRDKHTIA LVEAYAKAQG MWYDKDNEEP
VFTDSLHLDL GSVEPSLAGP KRPQDKVNLS SLPVEFNNFL IEVGKEKEKE KTFAVKNKDF
QMKHGHVVIA AITSCTNTSN PSVLMAAGLV AKKAIEKGLQ RKPWVKSSLA PGSKVVTDYL
RHAGLQTYLD QLGFNLVGYG CTTCIGNSGP LPDDISHCVA EHDLVVSSVL SGNRNFEGRV
HPQVRANWLA SPPLVVAYAL CGTTCSDLSR EPIGQDKEGN DVYLKDIWPS NEEIAAEVAK
VSGTMFRKEY AEVFKGDAHW QAIQTSSGQT YEWNPDSTYI QHPPFFENLS LKPEPLKPIK
QAYVLALFGD SITTDHISPA GSIKASSPAG LYLKSKGVDE KDFNSYGSRR GNHEVMMRGT
FANIRIRNEM TPGQEGGVTR YVPTGETMSI YDAAMRYQEN QQDLVIIAGK EYGTGSSRDW
AAKGTNLLGV KAVITESFER IHRSNLIGMG ILPLQFKEGT TRKTLKLDGS ERISIEISDK
LTPGAMVPVT IERQDGDIEK IETLCRIDTA DELEYYKNGG ILQYVLRKIS S
