ID G7VE76_9CREN Unreviewed; 520 AA.
AC G7VE76;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=P186_2662 {ECO:0000313|EMBL:AET34046.1};
OS Pyrobaculum ferrireducens.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET34046.1, ECO:0000313|Proteomes:UP000005867};
RN [1] {ECO:0000313|EMBL:AET34046.1, ECO:0000313|Proteomes:UP000005867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1860 {ECO:0000313|EMBL:AET34046.1,
RC ECO:0000313|Proteomes:UP000005867};
RX PubMed=22247528; DOI=10.1128/JB.06465-11;
RA Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT pyrobaculum able to grow with various electron acceptors.";
RL J. Bacteriol. 194:727-728(2012).
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from pyruvate: step 1/3. {ECO:0000256|ARBA:ARBA00004743}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154}.
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DR EMBL; CP003098; AET34046.1; -; Genomic_DNA.
DR AlphaFoldDB; G7VE76; -.
DR STRING; 1104324.P186_2662; -.
DR KEGG; pyr:P186_2662; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_7_0_2; -.
DR BioCyc; PSP1104324:GJSN-2606-MONOMER; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000005867; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR CDD; cd07941; DRE_TIM_LeuA3; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005675; Citramal_synthase.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR00977; citramal_synth; 1.
DR PANTHER; PTHR43538:SF1; (R)-CITRAMALATE SYNTHASE; 1.
DR PANTHER; PTHR43538; ALPHA-IPM SYNTHASE/HOMOCITRATE SYNTHASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR SUPFAM; SSF51569; Aldolase; 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:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AET34046.1}.
FT DOMAIN 1..249
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 520 AA; 57697 MW; EAC71B8445058B35 CRC64;
MSFTLQDKIN IALKLDELGV DYIEGGWPYS NPKDLEFFKL MKEYPLTRAK LAAFGSTRRR
GLRPHQDESL NSIVKADVPA AVIFGKSWTL HVDKVLEATR EENLAMIAES VEYLRQHGME
VIYDAEHFFQ GYQEDPEYAL ATIEAAWRAG ARVVVLADTN GGTPPNEVYR IVQEVRRRFP
NMPLGAHMHN DIGCAVANTL MAVAAGARHV QGTINGVGER TGNADLVAVL PTLELKMGFR
VLRDEPPPAK YSKLREVSRL VYEALGMAPN PYQPYVGEFA FAHKGGVHAD AVMKVPRAYE
HVDPALVGNR RVFVVSEMAG GASVVLKAAE ELGLELEKRD EAVRRALEEI KRMEKEGYSF
DLAPASALLI LMRHLGLYTE RFQLLEWKVV TGPSEHSYAF VKVRVGESVR LEAGEGVGPV
HAVDVALRRA LTASFPELVD VALSDYKVVL PTAKKSTESV VRVLAEFRDG QRMWRTVGVS
TNIVKASIKA LTDGYDFALQ IKNGWGKKPI YLGKKDVLIK
//
