ID E6W4A0_DESIS Unreviewed; 407 AA.
AC E6W4A0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN OrderedLocusNames=Selin_0019 {ECO:0000313|EMBL:ADU64778.1};
OS Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC Desulfurispirillum.
OX NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU64778.1, ECO:0000313|Proteomes:UP000002572};
RN [1] {ECO:0000313|EMBL:ADU64778.1, ECO:0000313|Proteomes:UP000002572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC {ECO:0000313|Proteomes:UP000002572};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA Bini E., Woyke T.;
RT "Complete sequence of Desulfurispirillum indicum S5.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP002432; ADU64778.1; -; Genomic_DNA.
DR RefSeq; WP_013504667.1; NC_014836.1.
DR AlphaFoldDB; E6W4A0; -.
DR STRING; 653733.Selin_0019; -.
DR KEGG; din:Selin_0019; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_2_0; -.
DR InParanoid; E6W4A0; -.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000002572; 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 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; 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 Pyruvate {ECO:0000313|EMBL:ADU64778.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002572};
KW Transferase {ECO:0000256|RuleBase:RU003523, ECO:0000313|EMBL:ADU64778.1}.
FT DOMAIN 13..275
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 407 AA; 44584 MW; 1236A825C0A2D904 CRC64;
METFPASHTP HSPFFLDVTL RDGNQALPRP WSLKQKQQVF QHLIRLEVPG AEVGFASASA
VDFEACCALA QEAPASMVIS SLSRARTAEI DASWEAVSHA AQPRVHIVYP VSPSVVNQVL
RCTPHEAARA VRQAVRHARR LAGKRGSVQF SGEHFGDCLD DIALALDIFQ VAIEEGADVI
NLPNTVERFR PMVFVEIARQ VMEYFRGRSA FAVHCHNDLG MATATTVESY FAGATQLEVS
LNGLGERAGN ASLYEVVCAL ENSGVHTGIQ RQYIFETARE VAELSAIAVG PKTPIIGSDV
FSHRSGIHQD GAIKSRSGRG VYLPFVTGAV GRADGEQLRF TSQSGTAVLQ DCLNRAGIHL
DAVTLREYYR YLEKRSDAEG EMDERAILRH YRQWCAGSQI SPEIPAR
//
