ID A0A1J7GFJ2_LUPAN Unreviewed; 1228 AA.
AC A0A1J7GFJ2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=TanjilG_06512 {ECO:0000313|EMBL:OIV99207.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIV99207.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIV99207.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIV99207.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBUNIT: Component of complex II composed of eight subunits in plants:
CC four classical SDH subunits SDH1, SDH2, SDH3 and SDH4 (a flavoprotein
CC (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a
CC large and a small subunit.), as well as four subunits unknown in
CC mitochondria from bacteria and heterotrophic eukaryotes.
CC {ECO:0000256|ARBA:ARBA00011313}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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DR EMBL; CM007373; OIV99207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7GFJ2; -.
DR STRING; 3871.A0A1J7GFJ2; -.
DR EnsemblPlants; OIV99207; OIV99207; TanjilG_06512.
DR Gramene; OIV99207; OIV99207; TanjilG_06512.
DR OMA; WFRFRGH; -.
DR Proteomes; UP000188354; Chromosome LG13.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045281; C:succinate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProt.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0043436; P:oxoacid metabolic process; IEA:UniProt.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR CDD; cd03499; SQR_TypeC_SdhC; 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; 2.
DR Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 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 InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR014314; Succ_DH_cytb556.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
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; 2.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 2.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000188354};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1158..1178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 148..651
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 780..907
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT DOMAIN 1056..1114
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 1228 AA; 134975 MW; 5CFCBE49F371ECF4 CRC64;
MYIATSSLLR ATRSKIISSS ISRTFSYHSS STYRSFSSTV ARSFCSSVPR WSHRIDWRYP
FTLRSQIRAV APVIERFHRK IATIANENPF KGNLTSLPKP GGGEFGKFYS LPSLNDPRID
RLPYSIRILL ESAIRNCDNF QVTKEDVEKI IDWENSYTKQ VEIPFKPARV LLQDFTGVPA
VVDLACMRDA MNKLGGDSNK INPLVPVDLV VDHSVQVDVA RSENAVQANM ELEFQRNKER
FAFLKWGSTA FRNMLVVPPG SGIVHQVNLE YLGRVVFNNE GLLYPDSVVG TDSHTTMIDG
LGVAGWGVGG IEAEAAMLGQ PMSMVLPGVV GFKLSGKLRD GVTATDLVLT VTQILRKHGV
VGKFVEFYGD GMGKLSLADR ATIANMSPEY GATMGFFPVD HVTLQYLKLT GRSDETVAMI
ETYLRANNMF VDYNEPQQDR VYSSYLELNL SDVEPCISGP KRPHDRVPLK EMKADWHSCL
DSKVGFKGFA IPKEAQGKVA KFDFHGQPAE LKHGSVVIAA ITSCTNTSNP SVMLGAGLVA
KKAHELGLQV KPWVKTSLAP GSGVVTKYLL QSGLQKYLNE QGFHIVGFGC TTCIGNSGDL
NESVASAISE NDIVAAAVLS GNRNFEGRVH ALTRANYLAS PPLVVAYALA GTVDIDFEKE
PIGTGKDGKN VFLRDIWPSN EEIAEAVQSS VLPNMFRSTY EAITKGNPMW NQLQVPADKL
YSWDTNSTYI HEPPYFKNMT MDPPGAHGVK DAYCLLNFGD SITTDHISPA GSIHKDSPAA
KYLLERGVDR KDFNSYGSRR GNDEVMARGT FANIRLVNKL LNGEVGAKTV HIPTGEKLYV
FEAAMRYRSA GEDTIVIAGA EYGSGSSRDW AAKGPMLLGV KAVIAKSFER IHRSNLVGMG
IIPLCFKSGE DADTLGLTGH ERYTIDLPSK ISEIRPGQDV TVTTDNGKSF TCTVRFDTEV
ELAYFNHGGI LPYVIRNLIK YALGFHKVFQ DLRHTGSMSF DPRNKRKIKI ESMNHISVKI
PNENPSNGNL IGKFGNRNSL PSLNNPIAKL GGDSIDKIND SLSYKASGHD TNVLAGAGYV
NGSSRVWASK NPMLLGVNAV MARSLDRSMD SNALGLTGHK RHMSDTTSTI SETRAYGFRP
LSPHLPVYQP QLSSTLSIFN RISGALLSTV ILLFYMIYMK VGLISLSYDS FYQFLFYSSK
LNLLAVEISG LALSYHLYAG IRHLVQKL
//
