ID A4YKB5_BRASO Unreviewed; 911 AA.
AC A4YKB5;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
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:CAL74341.1};
GN OrderedLocusNames=BRADO0393 {ECO:0000313|EMBL:CAL74341.1};
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL74341.1, ECO:0000313|Proteomes:UP000001994};
RN [1] {ECO:0000313|EMBL:CAL74341.1, ECO:0000313|Proteomes:UP000001994}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
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; CU234118; CAL74341.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YKB5; -.
DR STRING; 114615.BRADO0393; -.
DR KEGG; bra:BRADO0393; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_5; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000001994; 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:UP000001994}.
FT DOMAIN 82..575
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 705..837
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 911 AA; 99031 MW; 330C5F793A830CD9 CRC64;
MGFPRMTSLD SFKCRKTLKV GTKSYIYYSL PTAEKNGLKD ISKLPYSMKV LLENLLRNED
GRTVTKDDIV AVSKWLRKKS LEHEIAFRPA RVLMQDFTGV PAVVDLAAMR NAMQKLGGDA
EKINPLVPVD LVIDHSVIVN YFGDNKAFGK NVAEEYKQNQ ERYEFLKWGQ KAFSNFSVVP
PGTGICHQVN LEYLAQTVWT KKEKMTVGRT KGTFEVAYPD SLVGTDSHTT MVNGLAVLGW
GVGGIEAEAC MLGQPLSMLL PDVVGFKLTG ALKEGVTATD LVLTVTQMLR KLGVVGKFVE
FFGPGLDHLS VADKSTIANM APEYGATCGF FPVDTATIDY LKTSGRKGPR VALVEAYAKA
QGLFRTAKSA DPVFTETLNL DLGDVVPSMA GPKRPEGRIA LPAVAEGFAT ALAGEYKKPD
AAEQRFAVEG KDFDIGHGDV VIAAITSCTN TSNPSVLIGA GLLARNAAAK GLKAKPWVKT
SLAPGSQVVA EYLANSGLQK DLDKVGFNLV GFGCTTCIGN SGPLPEEISK SINDNGVVAA
AVLSGNRNFE GRVSPDVQAN YLASPPLVVA YALAGTVTKD LAVEPIGIGK DKKPVYLKDI
WPTTKEVNDF VKKFVKASIF KKRYADVFKG DTNWRKIKTV ESETYRWNMS STYVQNPPYF
EGMKKEPEPI KDIVEARVLA LFGDKITTDH ISPAGSIKLT SPAGKFLSEH QVRPADFNQY
GTRRGNHEIM MRGTFANIRI KNFMLKGADG NIPEGGLTKH WPDGEQMSIY DAAMKYQEEG
VPLVVFAGAE YGNGSSRDWA AKGTRLLGVR AVICQSFERI HRSNLVGMGV LPLTFQEGTS
WSSLGLKGGE KVTIKGLQGD LKPRQTLTAE IVSADGAAQQ VPLLCRIDTL DELDYYRNGG
ILHYVLRKLA A
//
