ID M2XVI5_GALSU Unreviewed; 663 AA.
AC M2XVI5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=Gasu_48120 {ECO:0000313|EMBL:EME27668.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME27668.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
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}.
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DR EMBL; KB454529; EME27668.1; -; Genomic_DNA.
DR RefSeq; XP_005704188.1; XM_005704131.1.
DR AlphaFoldDB; M2XVI5; -.
DR STRING; 130081.M2XVI5; -.
DR EnsemblPlants; EME27668; EME27668; Gasu_48120.
DR GeneID; 17086557; -.
DR Gramene; EME27668; EME27668; Gasu_48120.
DR KEGG; gsl:Gasu_48120; -.
DR eggNOG; KOG2367; Eukaryota.
DR OMA; NTMRMLV; -.
DR OrthoDB; 375at2759; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000030680; 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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:EME27668.1};
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:UP000030680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EME27668.1}.
FT DOMAIN 132..394
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 90..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 73437 MW; 904DFE16EF1F0EEE CRC64;
MTLATLTYIH SCSVRNERSN TFMAFHATPS ILHSKQGLLE NIGKPLSIDR TAFSMRRSCF
VENQLHKRRL VQSWGNKEYT KAANGFRSLQ GSNNGYKESS SSHSWDDEPP LPPPIWKPTK
HDLVTGRDPT RVKFFDTTLR DGEQSPGATL TGEEKLVIAR QLAKLGVDII EAGFPVASNG
DFEAVRNIAR TVGTRENPPI ICGLARAVES DIARCWEAVK DAAFARIHTF IATSDIHMEH
KLKKSRSQVL ETVTRTVQYA KSLCEDIEFS AEDATRSDPE FLYEVFSRAI EAGATTINVP
DTVGYTTPAE FGSLMRGIRR NVRGIENVCL SVHGHDDLGL AVSNFLSAIE NGAQQVECTV
NGIGERAGNA SLEEIVMALY VRRQYYNNKL GRPDPNALLT CVDTQEIWKT SKLVSNLTGM
IVQPNKAIVG SNAFAHESGI HQDGILKNRL TYEIMDARLI GMQENQLVLG KHSGRHAFRK
RLGELGFDLT EDELNRAFVR FKELADKKKE VTLWDLESIV NDEVRLQGTE YLKLERVQVQ
CGDKLISTAT VTIMHMELSR ELTAVSIGTG PVDAAFKALN SIEGVPKVVL QEYMVNSITQ
GIDALGEVTV RIRGETDSRS FIGSAANTDI VVASVQAYVN ALNRLARYAQ YPKSVHPQKD
AVV
//
