ID V4MNV2_EUTSA Unreviewed; 962 AA.
AC V4MNV2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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 ORFNames=EUTSA_v10024325mg {ECO:0000313|EMBL:ESQ54648.1};
OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ54648.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ54648.1, ECO:0000313|Proteomes:UP000030689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA Mitchell-Olds T., Schumaker K.S., Wang X.;
RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL Front. Plant Sci. 4:46-46(2013).
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; KI517384; ESQ54648.1; -; Genomic_DNA.
DR RefSeq; XP_006413195.1; XM_006413132.1.
DR AlphaFoldDB; V4MNV2; -.
DR STRING; 72664.V4MNV2; -.
DR EnsemblPlants; ESQ54648; ESQ54648; EUTSA_v10024325mg.
DR Gramene; ESQ54648; ESQ54648; EUTSA_v10024325mg.
DR KEGG; eus:EUTSA_v10024325mg; -.
DR eggNOG; KOG0452; Eukaryota.
DR OMA; NELPATM; -.
DR Proteomes; UP000030689; Unassembled WGS sequence.
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:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0043436; P:oxoacid metabolic process; IEA:UniProt.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 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:SF72; ACONITATE HYDRATASE 2, 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.
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:UP000030689}.
FT DOMAIN 160..664
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 761..889
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 962 AA; 105185 MW; AD3ACF7AB4BA9151 CRC64;
MSGKMASGGA GPCIVDGFEK TDEKLCSALL NRTLDGIPTL SPDIFSVQPW SLSEEFLPTV
ERSFLFLVKN PPENDYPLMT EQVYTWRTKQ CKREASASEH AYKDILTSLP KPGGGEYGKY
YSLPALNDPR IDRLPYSIRI LLESAIRNCD NYQVTKDDVE KIIDWENTST KQVETAFKPA
RVILQGVTGV PALVDLASMR DAMKNLGSDP NKINPLVPVD LVIDHSVQVD AAGTDKARLI
IEEYEFKRNK ERFAFLKWGS SAFHNMLVVP PGSGIVHQVN LEYLGRVVFN SGGFLYPDSV
VGTDSHTTMI DGLGVAGWGV GGIEAEAAML GQPMSMVLPG VVGFKLDGKL REGVTTTDLV
LTVTQILRKH GVVSKFVEFY GEGMSKLSLA DRATIANMSP EYGATMGFFP VDHVTLEYLK
LTGRSDETVA MIESYLRANN MFVDYSEPQQ ERAYTSYLQL DLGHVEPCIS GPKRPHDRVL
LKDMKADWHA CLDNPVGFKG FAIPKEKQED TVKFLFEEKL PAELKHGSVV IAAITSCTNT
SNPSVMLGAA LVAKKAYDLG LMVKPWVKTS LAPGSGVVTK YLDQSGLQEY LDKQGFQIFG
YGCTTFIGNS GNLKKSVESA IKNNDVVVAS VLSGNQNFEG RVHPLTRANY LASPPLVVAY
ALAGTVDIDF EKEPIGTGRD DKSVYLRDIW PTNEEIAQVV QSNVLSDMFK STYKTITEGN
PLWNELPATM KDAYCLLNFG DSITTDHISP AGDIQKDSPA AKFLIDNGVS QEDFNSYGSR
RGNDEVMARG TFASIRIVNK LADGEVGPKT VHIPTGEKLT VFDAASRYKT AGQDTVILAG
AEYGSGSSRD WAAKGPLLLG VKAVTAKSFE RIHRSNLAGM GIIPLCFKAG EDADTLGLTG
HERYTVHLPT KVSDIRPGQD VTVTTDTGKS FVCTLRFDTE VELAYYDHGG ILPYVIRSLS
TK
//