ID A0A0S1XYI4_9BORD Unreviewed; 887 AA.
AC A0A0S1XYI4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 {ECO:0000313|EMBL:ALM82810.1};
GN ORFNames=ASB57_07465 {ECO:0000313|EMBL:ALM82810.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM82810.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM82810.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM82810.1,
RC ECO:0000313|Proteomes:UP000064621};
RA Hou L.;
RT "Draft genome of Bordetella sp. N.";
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}.
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DR EMBL; CP013111; ALM82810.1; -; Genomic_DNA.
DR RefSeq; WP_057651656.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1XYI4; -.
DR STRING; 1746199.ASB57_07465; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000064621; 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 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; 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; 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:UP000064621}.
FT DOMAIN 77..553
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 682..808
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 887 AA; 94328 MW; 410C78D3AA0B5293 CRC64;
MTFQAADTLR ALPIEGQPPA RFYSLSVLEE LGYGAISRLP HSIRIILESV LRNLDGTSVQ
ESHLRELAAW HPKGTRDSEI PFVVSRIVAP DSSGVPLLAD LAAMREAAAD AGMDPAAIEP
LVPVDLIVDH SISVEHAGSS DALAHNMAVE YERNAERYSF LKWAANAFSA FRIFPPGTGI
IHQINLELLA RGVHQKDGIA YFDTLVGTDS HTPMINGIGV VGWGVGGIEA EAAMLGQPIY
VVAPDVVGVE LVGTPRPGIL ATDIVLTVVQ ALRARKVVGK FVEFFGAGVT ALAAVDRTTI
ANMAPEYGAT LALFPVDERT LDYLRSVGRK EQELAALEGY FRAQGMFGVP AAGSIDYSDT
LRIDLAAVEP SVAGPSRPQD RIALADLKDS VRQLLQAKTA AAAVDVPSSE TSLRDGDVVL
AAITSCTNTS NYRSILAAGV LARNAVRKGL HAASHVKTSF TPGSRAVTEY LKAAGLDTAL
DNLGFQVAGY GCATCMGNSG PLAPTIADEI KRRDLTVAAV LSGNRNFEAR IHQAIKANYL
MSPPLVVAFA IAGTTAFDPA ADALGVGADG APVYLADIWP TDAEMAEVLP YAVDPNNVLR
VYAAPPENPL WSALDAPAGD LFTWQQGSTY LKRPPFFDGV TRDIPAQSAI SGARALAILG
DSVTTDHINP GGSIPAESES GQYLISLGVA PADFNSYISR RAHDDVMVRS TFANVRVRNL
MVPEVGSRTL HQPDGAPMSI FAAATWYAEQ GIPMIVFAGE EYGNGSSRDW AAKGPRLLGI
RAVIAKSFER IHRSNLVGMG ILPLEFLNGQ DAQSLGLTGD ESFDLPGDLA AIQPRQSVDL
VIHRKDGTTQ TVTLRARIDS AIEAAYFHHG GILPYVLRSR LDQQTTA
//