ID Q1DCT2_MYXXD Unreviewed; 421 AA.
AC Q1DCT2;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN OrderedLocusNames=MXAN_1284 {ECO:0000313|EMBL:ABF89693.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF89693.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF89693.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004689}.
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DR EMBL; CP000113; ABF89693.1; -; Genomic_DNA.
DR RefSeq; WP_011551401.1; NC_008095.1.
DR AlphaFoldDB; Q1DCT2; -.
DR STRING; 246197.MXAN_1284; -.
DR EnsemblBacteria; ABF89693; ABF89693; MXAN_1284.
DR GeneID; 41358729; -.
DR KEGG; mxa:MXAN_1284; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_4_2_7; -.
DR Proteomes; UP000002402; Chromosome.
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 CDD; cd03174; DRE_TIM_metallolyase; 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; 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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT DOMAIN 30..295
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 421 AA; 45911 MW; 38487DE6E7581404 CRC64;
MRDPARTVSH SEFIHDWNGR GAAPSPAFPV EINDETLRDG MQATAVTSPT VEEKRGLLEL
MQHIGVSAVS LGMPAAGPWA LEEVVTLARH IREEALRLEP NCAARTLHSD IVPIVEAVQR
AGQPIVVHTF IGSSPLRQCA EAWDLDFILR SSTAAIDFAV RQGLEVAFIT EDTTRSTPET
LELLFRAAVE HGASRLVLCD TVGHATPAGT RALVRWTRDL VERLGSPVKV EWHGHNDRGL
ALINALVALE AGATRVHGCG LGIGERTGNA PVELLLLNLK LLGWIDQDLT RLVDYVLTLA
QVCRVPIPRN YPLVGEDAFR TATGVHSAAI IKALERGDDW LADHIYSSVP AGEFGRRQQL
ELGPMSGMSG VRYWLMVRGL QENEQLCEEI LRRAKSAAST LTEEEVWSIV QAHGGQGRSC
A
//
