ID A0A1Z5JNF1_FISSO Unreviewed; 655 AA.
AC A0A1Z5JNF1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=FisN_8Lh211 {ECO:0000313|EMBL:GAX15489.1};
OS Fistulifera solaris (Oleaginous diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC Fistulifera.
OX NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX15489.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX15489.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX15489.1,
RC ECO:0000313|Proteomes:UP000198406};
RX PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT by the genome and transcriptome.";
RL Plant Cell 27:162-176(2015).
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004689}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000256|ARBA:ARBA00009396}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX15489.1}.
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DR EMBL; BDSP01000092; GAX15489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5JNF1; -.
DR InParanoid; A0A1Z5JNF1; -.
DR OrthoDB; 375at2759; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000198406; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01025; LeuA_type1; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR005671; LeuA_bact_synth.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR00973; leuA_bact; 1.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:GAX15489.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198406};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAX15489.1}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..655
FT /note="2-isopropylmalate synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012961472"
FT DOMAIN 84..354
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 655 AA; 70083 MW; CC18341F42A9C749 CRC64;
MKLILSAAVV TSLWLAPQTV TAFTPSALQS RSPWTNRVTQ LSVKKQLTSL ALSSKAIDET
QPFLLERRPR PPYVPGKISD PDYVRIFDTT LRDGEQSPGA TLTSSEKLDI ARKLAQLGVD
IIEAGFPIAS PDDFNAVKQI ADIVGNEVFE DGYVPVICGL SRANPKDIET AWNAVKGAKL
PRVHTFIATS PIHMEAKLNK TPDEVVDIAV NAVKFAKSLG CNDIEFSPED AGRSDPEFLY
RILSEVIQAG ATTLNIPDTT GWNMPWEFGE LIKNLRENVQ GAENVVFSTH CQNDLGLATA
NSLAGALNGA RQLECTINGI GERAGNASLE EVVMALALKG ATKFQGGPGT GKLYTAINSV
YITPASKMVA EYTGMACQPH KAIVGANAFQ HESGIHQDGM IKNKSTYEIM TPESIGLMRG
DSQSGAGIVL GKHSGRNAVG TRLRELGYDL DADKLNAIFT RFKQVAERKK GGLEDDDLEA
LVSDQMGRSD ILWEVTGLQV STGISGIPTA TVKMRGPDGM ERFVASTGTG PVDAAYKAID
QIMGVSVVLE SYQLNSVTEG IEALATTRVT ISPKAGGPND TQSIHSQLGN RNLKFSGSGS
DTDIMTSSAR AYVSALNKLL NCNARRRAEV IAEEDKSGIG DAIAAEPMQV VEVEA
//
