ID A6LAX6_PARD8 Unreviewed; 749 AA.
AC A6LAX6;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
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 OrderedLocusNames=BDI_1074 {ECO:0000313|EMBL:ABR42840.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR42840.1, ECO:0000313|Proteomes:UP000000566};
RN [1] {ECO:0000313|EMBL:ABR42840.1, ECO:0000313|Proteomes:UP000000566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC {ECO:0000313|Proteomes:UP000000566};
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR42840.1; -; Genomic_DNA.
DR RefSeq; WP_011966311.1; NC_009615.1.
DR AlphaFoldDB; A6LAX6; -.
DR STRING; 435591.BDI_1074; -.
DR PaxDb; 435591-BDI_1074; -.
DR KEGG; pdi:BDI_1074; -.
DR PATRIC; fig|435591.13.peg.1064; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_006714_2_2_10; -.
DR BioCyc; PDIS435591:G1G5A-1109-MONOMER; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000000566; Chromosome.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000566}.
FT DOMAIN 35..478
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 555..684
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 749 AA; 81749 MW; E5C80A3F7CDB7AF1 CRC64;
MVYDIDMLRN FYANFPRRVD TARERIGGRP MTLAEKILYA HLYDESSTRL FKRGEDYVNF
RPDRVAMQDA TAQMALLQFM NAGKEKSAVP ATVHCDHLIQ ANMGAKTDID TATKSNSEVY
DFLKSVSDKY GIGFWKPGAG IIHQVVLENY AFPGGMMVGT DSHTPNAGGL GMVAIGVGGA
DAVDVMTGME WELKMPKLIG VKLTGSLNGW ASPKDVILKL AGILTVKGGT NAIIEYFGPG
TASISATGKA TICNMGAEVG ATTSLFPFDN TMAQYLRATG RDEVASWAEA IGEYLEADMD
VRAEPDKFYD RVIVINLSEL EPHINGPFTP DAATPISEFA AKVKANGYPR KMEVGLIGSC
TNSSYQDLSR AASIARQAYE DKIPVAAPLI INPGSEQIRY TAERDGIIGD FERIGATIMA
NACGPCIGQW KRHTDDNTRK NSIVTSFNRN FAKRADGNPN THAFVASPEL TLALTIAGDL
CFNPLTDTLK TEDGKVVKLK EPKGSDFPPK GFEVKDNGYL APTGKNVVVN IDPESNRLQA
LKPFAPWNGE DFTDMPLLIK AEGKCTTDHI SMAGPWLRFR GHLENISDNM LMGAVNAFNG
KTNSVLNQLN NEYEAVSAVA KQYKANSISS IVVAEENYGE GSSREHAAME PRFLNVKVIL
AKSFARIHET NLKKQGMLAL TFANKEDYSK IRENDHISII GLKDFQPGKP LTAVLLHADG
TQESFPVNHT YNDLQIKWFK AGSALNTAH
//
