ID D9QLC0_BRESC Unreviewed; 897 AA.
AC D9QLC0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Bresu_0661 {ECO:0000313|EMBL:ADK99975.1};
OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=633149 {ECO:0000313|EMBL:ADK99975.1, ECO:0000313|Proteomes:UP000002696};
RN [1] {ECO:0000313|Proteomes:UP000002696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC {ECO:0000313|Proteomes:UP000002696};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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; CP002102; ADK99975.1; -; Genomic_DNA.
DR RefSeq; WP_013268079.1; NC_014375.1.
DR AlphaFoldDB; D9QLC0; -.
DR STRING; 633149.Bresu_0661; -.
DR KEGG; bsb:Bresu_0661; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_5; -.
DR InParanoid; D9QLC0; -.
DR OrthoDB; 9764318at2; -.
DR BioCyc; BSUB633149:G1GM8-662-MONOMER; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000002696; Chromosome.
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:UP000002696}.
FT DOMAIN 78..562
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 692..819
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 897 AA; 96581 MW; 22AC30486CC290DE CRC64;
MPSVDSLSTR RDLTVGRKKY AYYSLPAAQE AGLGGIDRLP RSMKVLLENL LRNEDGVSVT
EADLKAVAAW IENKGSVEHE IAFRPARVLM QDFTGVPAVV DLAAMRDAMA KLGADAAKIN
PLVPVDLVID HSVMVDNFGT TAAFGQNVER EYERNIERYK FLRWGSSAFN NFRVVPPGTG
ICHQVNLENL AQTVWTAPEG KATVAYPDTV VGTDSHTTMI NGLAVLGWGV GGIEAEAAML
GQPIPMLIPE VIGFKLSGTM PEGTTATDLV LTVTQMLRKK GVVGKFVEFF GPALPNMTIE
DQATIANMAP EYGATCGFFP VSAATIGYLT ATGRDKARVA LVEAYAKAQG LWIDETSEDP
VFSDVLELDI STVVPSLAGP KRPQDKVELT VAAPSFETAL GEVFNRATDA ARFPVAGQSF
DIGDGDVVIA AITSCTNTSN PSVLIAAGLV AQKANKLGLK TKPWVKTSLA PGSQVVTDYL
TAAGLQKELD ALGFNLVGYG CTTCIGNSGP LDPAISQTIN DNAIVATSVL SGNRNFEGRV
NPDVQANYLA SPPLVVAYAL AGSMRIDITT QPIGQDKKGN DVFLKDVWPT TAEIAAIQKK
AVTSAMFAKR YADVFKGDAH WQGIAVEGGQ TYEWDAASTY VANPPYFEGL SMEPTPVTDI
VEGRVLAIFG DSITTDHISP AGSIKKTSPA GQYLTNRGVE SEEFNSYGAR RGHHEVMMRG
TFANIRIRNR ITPDIEGGVT KHFPSQDTMS IYDAAMRYQS EGRPLVVFAG KEYGTGSSRD
WAAKGTRLLG VRAVIAESYE RIHRSNLVGM GVVPLQFKAD GWSKLGLTGE EIVTIRGLSD
VNVGRLRPRQ DLWVELFRPS DGKMARFPVR CRIDNQTELD YFKAGGVMPY VLRNLAG
//
