ID B0P8G3_9FIRM Unreviewed; 403 AA.
AC B0P8G3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=2-isopropylmalate synthase 1 {ECO:0000313|EMBL:EDS12209.1};
DE EC=2.3.3.13 {ECO:0000313|EMBL:EDS12209.1};
GN Name=leuA {ECO:0000313|EMBL:EDS12209.1};
GN ORFNames=ANACOL_01052 {ECO:0000313|EMBL:EDS12209.1};
OS Anaerotruncus colihominis DSM 17241.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS12209.1, ECO:0000313|Proteomes:UP000003803};
RN [1] {ECO:0000313|EMBL:EDS12209.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS12209.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS12209.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS12209.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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:EDS12209.1}.
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DR EMBL; ABGD02000007; EDS12209.1; -; Genomic_DNA.
DR RefSeq; WP_006874447.1; NZ_DS544177.1.
DR AlphaFoldDB; B0P8G3; -.
DR STRING; 169435.ERS852551_00004; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_4_0_9; -.
DR Proteomes; UP000003803; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.238.260; -; 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; PTHR42880; HOMOCITRATE SYNTHASE; 1.
DR PANTHER; PTHR42880:SF1; ISOPROPYLMALATE_HOMOCITRATE_CITRAMALATE SYNTHASE FAMILY PROTEIN; 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 Acyltransferase {ECO:0000313|EMBL:EDS12209.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 32..285
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 403 AA; 43822 MW; F4B14AEB4B91E90B CRC64;
MNLSYYKENA WWVSPFNETG PVREQTQPAG HVEIHDATLR DGEQTPGVVF SAEDKVRIAE
KLVEAGVTRI EAGMPAVSAE DRRAITEIAH RFPQAQVYAF ARAKTQDIDM ARDAGVKGVV
IEIPIGYPKL KYQFGWTWEH VLEKSVDCIN YARSQGLKAV YFPYDTTRAR AEDLEKLLTG
LMQSAPPDSV GVVDTMGCAL PQAVAYLVRE VKRLTNGLPV EVHTHNDFGL AVAGELAGIA
AGADVVHTCV NGLGERTGNA ALEEMILCMN ILLEMDTPYR LDRLGELCAL VEKLSGVAAA
PNKPFVGARN YMRESGIGVD LVRSCPLAMF ATDPALFGRS GEIALGKKSG KASVQYYLER
CGMTATDEQA AEMLARVKAR GLEKRGLLDE AEFREIAAAC LGA
//
