ID A0A1J4UP52_9ARCH Unreviewed; 511 AA.
AC A0A1J4UP52;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=AUJ14_05035 {ECO:0000313|EMBL:OIO24977.1};
OS Candidatus Micrarchaeota archaeon CG1_02_55_22.
OC Archaea; Candidatus Micrarchaeota.
OX NCBI_TaxID=1805250 {ECO:0000313|EMBL:OIO24977.1, ECO:0000313|Proteomes:UP000182370};
RN [1] {ECO:0000313|EMBL:OIO24977.1, ECO:0000313|Proteomes:UP000182370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_55_22 {ECO:0000313|EMBL:OIO24977.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO24977.1}.
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DR EMBL; MNVH01000061; OIO24977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4UP52; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000182370; 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 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 9..272
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 511 AA; 53642 MW; BDF3A6FDF879285D CRC64;
MVTVGTRKVI IFDTTLRDGE QSPGASMTLD EKVAVARQLC RLGVDVIEAG FPVASQDDFA
AVRTIAGEAR GPIIAALCRA DRNDITCAWE AVRGAQRPRI HTFIATSDVH LEHKLRMTRP
EVLGRITDSV SFARSLCQDV EFSAEDASRS DESFLKAAIR AAVAAGATTI NIPDTVGYSQ
PQEFGELVSE IVSMPEITAG GVTVSVHCHD DLGLAVANSL EAIRRGAGQV ECTVNGIGER
AGNAALEEVV MNLRTRGESF GVQTGIKANE LYQSSRLVSR VTGIAVQRNK AVVGANAFSH
EAGIHQHGML ANRATYEIML PAEVGWIGEG MVIGKHSGRH AIGSCIKEAG ITFTDEQLAQ
VVSKVKSLAD RQKSVSAEEV VAIAEGMLHE GVEPALRVVE YAAFTGNGAP ATASLAVVVD
GRTVKASNHG IGIVDASFSA LKAATGIDAR LAEYSLKAVA GGSNALAEVT VAVESGGRIA
RSRGVHEDVA VASLNAFVAA FNRLLALRGI T
//
