ID Q04NA2_LEPBJ Unreviewed; 755 AA.
AC Q04NA2;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE AltName: Full=Citrate hydro-lyase {ECO:0000256|ARBA:ARBA00029682};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN Name=acnA {ECO:0000313|EMBL:ABJ77618.1};
GN OrderedLocusNames=LBJ_4240 {ECO:0000313|EMBL:ABJ77618.1};
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=355277 {ECO:0000313|EMBL:ABJ77618.1, ECO:0000313|Proteomes:UP000000656};
RN [1] {ECO:0000313|EMBL:ABJ77618.1, ECO:0000313|Proteomes:UP000000656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB197 {ECO:0000313|EMBL:ABJ77618.1,
RC ECO:0000313|Proteomes:UP000000656};
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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 -!- 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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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DR EMBL; CP000351; ABJ77618.1; -; Genomic_DNA.
DR RefSeq; WP_002755870.1; NC_008511.1.
DR AlphaFoldDB; Q04NA2; -.
DR KEGG; lbj:LBJ_4240; -.
DR PATRIC; fig|355276.3.peg.4236; -.
DR HOGENOM; CLU_006714_2_2_12; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000000656; Chromosome 2.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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; cd01584; AcnA_Mitochondrial; 1.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01340; aconitase_mito; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 34..477
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 558..684
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 755 AA; 81958 MW; A0DF50441BB335A8 CRC64;
MAFDIEMIRA RYAKIGDLVT KARNVVGRPL TLTEKILYSH LWEGEPKTGY EKGKSYVDFA
PDRVAMQDAT AQMALLQFMS AGRNKVAVPS TVHCDHLIQA KDGAVEDLKT ANTVNKEVYD
FLSSVSNKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTVNAGGLG MIAIGVGGAD
AVDVMAGMAW ELKFPKLIGV KLTGKLSGWA SAKDIILKVA GILTVKGGTG AIVEYFGEGA
DSLSCTGKGT ICNMGAEIGA TTSVFGYDRN MREYLLKTNR KDVAELADKI VEHLNGDKEV
YADPAKYFDQ LIEINLSELE PYINGPFTPD LATPLSKFKE AVQQNGWPTN LEVGLIGSCT
NSSYEDITRA ASVARQAAEK NLEVKAEYTV TPGSEMIRYT IERDGLIKTF SDIGGVVLAN
ACGPCIGQWS RHTKDPERKN SIITSFNRNF AKRNDGLAGT HAFVASPEIV TAFAIAGTLD
FNPITDSLKS KDGKEVKLDP PTGLDFPPKG FDVKDAGFIA PAADGSKVNV VVDRQSDRLQ
LLLPFAPWEK ADLKGLKLLI KAKGKCTTDH ISMAGPWLKY RGHLDNISNN LLIGAVNAFN
DKTNEVKNQL SGTYEPVPQT ARAYKAKGIG SIVVGDENYG EGSSREHAAM EPRHLGVRAV
LVKSFARIHE TNLKKQGMLA LTFVDKADYD KIQEEDTIDI LGLTSFQEGT PLTLVLHHKD
GSSQEIKVNH TFNAQQIAWF KAGSALNLIS EEQKK
//
