ID A0A0G1YDP3_9BACT Unreviewed; 591 AA.
AC A0A0G1YDP3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=UY90_C0055G0002 {ECO:0000313|EMBL:KKW41361.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWA2_54_9.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619059 {ECO:0000313|EMBL:KKW41361.1, ECO:0000313|Proteomes:UP000034940};
RN [1] {ECO:0000313|EMBL:KKW41361.1, ECO:0000313|Proteomes:UP000034940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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. {ECO:0000256|RuleBase:RU003523}.
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:KKW41361.1}.
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DR EMBL; LCRV01000055; KKW41361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1YDP3; -.
DR PATRIC; fig|1619059.3.peg.811; -.
DR Proteomes; UP000034940; Unassembled WGS sequence.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
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 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 Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 37..326
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 591 AA; 64710 MW; 639A39C91B456062 CRC64;
MPRRTAERTP GAETAADRLM REAYEVQIGK RRATTRLFIN DVTLRDGEQA PGNTMSEEEK
LEIAKQLVRM GIPGIEAGFP IASPGDFRAV ERIANEVGSQ KLPRPSHESV YPRISGLARL
KRKDIQRVLD AVGGAPHHGV HTFVSTSQDQ IDKFDGDIRK AGGRPGNLSS LIHRVVIPGI
ETEIPYIREQ DTNAVIQFSP EDWTRTEESV SDEVILAAAQ MGAHIINLPD TVGIAVPMQI
VKRVAHVRKL LDEHGFQHVV ISWHGHNDTG NAVANAHAAL EAGAQQFEPT ILGIGERAGN
FSFEGFLAGL DANLHYYEEA TGRRITDPIV RKQVMKTALL LSSILGKDIS PEHPIVGENA
FAHEAGIHQD GHLKAKRSGS GRRAYEILTA ERYGATSKLI LGKHSGWGGI KDYLEGKKLP
FRETDRQLFT DAVSATADRL QRRKGLSDSE VMEEAYYPSV IEITGGAYIA DVTEIDRVDG
KFAVRITTRD GEQIIGVASA KDEGELDAIM QGMKQIIPGV EMPRDGFHTR AVGEGSGTAA
VSSFTIRNGF EVTHSATHRD THVAERTALI KAFNAMKAMD DYKAMMEASE E
//
