ID I1J8H1_SOYBN Unreviewed; 901 AA.
AC I1J8H1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=100499625 {ECO:0000313|EnsemblPlants:KRH76600};
GN ORFNames=GLYMA_01G162800 {ECO:0000313|EMBL:KRH76600.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH76600.1};
RN [1] {ECO:0000313|EMBL:KRH76600.1, ECO:0000313|EnsemblPlants:KRH76600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH76600};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH76600.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH76600}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH76600};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH76600.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH76600.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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|RuleBase:RU361275};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CM000834; KRH76600.1; -; Genomic_DNA.
DR RefSeq; XP_003517155.1; XM_003517107.3.
DR AlphaFoldDB; I1J8H1; -.
DR SMR; I1J8H1; -.
DR STRING; 3847.I1J8H1; -.
DR PaxDb; 3847-GLYMA01G36750-1; -.
DR EnsemblPlants; KRH76600; KRH76600; GLYMA_01G162800.
DR GeneID; 100499625; -.
DR Gramene; KRH76600; KRH76600; GLYMA_01G162800.
DR KEGG; gmx:100499625; -.
DR eggNOG; KOG0452; Eukaryota.
DR HOGENOM; CLU_013476_2_1_1; -.
DR InParanoid; I1J8H1; -.
DR OMA; NGGIMQY; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000008827; Chromosome 1.
DR ExpressionAtlas; I1J8H1; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0003994; F:aconitate hydratase activity; IBA:GO_Central.
DR GO; GO:0030350; F:iron-responsive element binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006101; P:citrate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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:SF62; ACONITATE HYDRATASE 1; 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|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|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT DOMAIN 67..569
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 698..825
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 901 AA; 98522 MW; 0C5960FF5ECFEC76 CRC64;
MATENPFNSI LRTLEKPGGA GEFGKYFSLP ALNDPRIDRL PYSVRILLES AIRNCDEFQV
KSNDIEKIID WENTSPKLVE IPFKPARVLL QDFTGVPAVV DLACMRDAMN KLGGDSNKIN
PLVPVDLVID HSVQVDVARS ENAVQANMEL EFQRNKERFG FLKWGSNAFN NMLVVPPGSG
IVHQVNLEYL GRVVFNTNGV LYPDSVVGTD SHTTMIDGLG VAGWGVGGIE AEAAMLGQPM
SMVLPGVVGF KLLGKLRDGV TATDLVLTVT QMLRKHGVVG KFVEFYGEGM SELSLADRAT
IANMSPEYGA TMGFFPVDHV TLQYLRLTGR SDETVSMIES YLRANKMFVD YSEPQVERVY
SSYLELNLED VEPCVSGPKR PHDRVPLREM KVDWHACLNN KVGFKGFAVS KESQNKVAEF
TFQGTPAHLR HGDVVIAAIT SCTNTSNPSV MLGAALVAKK ACELGLQVKP WIKTSLAPGS
GVVTKYLQRS GLQKYLNELG FNIVGYGCTT CIGNSGDINE AVASAITEND IVAAAVLSGN
RNFEGRVHPL TRANYLASPP LVVAYALAGT VDIDFDTEPI GIGKDGTEIF FKDIWPSSEE
IANVVQSSVL PDMFRDTYNA ITQGNPMWNN LSVPTGTLYA WDPTSTYIHE PPYFRDMSMS
PPGSHGVKDA YCLLNFGDSI TTDHISPAGS IHKDSPAARY LIERGVDRRD FNSYGSRRGN
DEVMARGTFA NIRIVNKFLN GEVGPKTIHI PSGEKLSVFD VAEKYKSEGH DMIILAGAEY
GSGSSRDWAA KGPMLLGVKA VIAKSFERIH RSNLVGMGII PLCFKPGEDA DSLGLTGQER
YTIDLPSNVN EIRPGQDVTV VTDTGKSFVS TLRFDTEVEL AYFNHGGILQ YVIRNLINAK
H
//
