ID B5YFP3_THEYD Unreviewed; 413 AA.
AC B5YFP3;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=2-isopropylmalate synthase 2 {ECO:0000313|EMBL:ACI20810.1};
DE EC=2.3.3.13 {ECO:0000313|EMBL:ACI20810.1};
GN OrderedLocusNames=THEYE_A1277 {ECO:0000313|EMBL:ACI20810.1};
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI20810.1, ECO:0000313|Proteomes:UP000000718};
RN [1] {ECO:0000313|Proteomes:UP000000718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87
RC {ECO:0000313|Proteomes:UP000000718};
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI20810.1, ECO:0000313|Proteomes:UP000000718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87
RC {ECO:0000313|Proteomes:UP000000718};
RX PubMed=25635016;
RA Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA Robb F.T., Ward N.L., Eisen J.A.;
RT "Genome Sequence of the Sulfate-Reducing Thermophilic Bacterium
RT Thermodesulfovibrio yellowstonii Strain DSM 11347T (Phylum Nitrospirae).";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP001147; ACI20810.1; -; Genomic_DNA.
DR RefSeq; WP_012545541.1; NC_011296.1.
DR RefSeq; YP_002249091.1; NC_011296.1.
DR AlphaFoldDB; B5YFP3; -.
DR STRING; 289376.THEYE_A1277; -.
DR EnsemblBacteria; ACI20810; ACI20810; THEYE_A1277.
DR KEGG; tye:THEYE_A1277; -.
DR PATRIC; fig|289376.4.peg.1247; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_4_2_0; -.
DR InParanoid; B5YFP3; -.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000000718; Chromosome.
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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:ACI20810.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000718};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACI20810.1}.
FT DOMAIN 7..278
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 413 AA; 45926 MW; EDCEA85488B14CAF CRC64;
MITKGKVYLI DVTNRDGVQT SRILLPKLSK TLLNLYLDEM GVYQSEIGFP TLKHEVNYIN
ANLELVELGA FKRIHLEGWA RAIPEDVELA FKNCPKIKHL NLSVSTSEIM IQGKFQGRKT
WDDIVKGMYN AVKLAKELGA ETVGFNAEDA SRTELSRLIE FILAGKEAGG DRFRYCDTLG
CEDPITIYER IHTLALATRF PIEMHCHNDL GMAEAVSVAG AQGTIEAGVD SYINTTVNGY
GERAGNADLV STILALKFSH GLKEKCPLDE HVNLKMAWKI AKYASYAFNI PIPINQPGVG
ANAFAHESGI HADGVLKDRA NYELYSPEDV GRGEPELLET GRIITTGEYG GIKGFRYVYS
KLGIEFHDDN EARNILELVQ YANLHTQKPL TDDELKFIAT YPDIVRQILT VTP
//
