ID F4FYR4_METCR Unreviewed; 523 AA.
AC F4FYR4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN OrderedLocusNames=Mcup_0194 {ECO:0000313|EMBL:AEB94303.1};
OS Metallosphaera cuprina (strain Ar-4).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=1006006 {ECO:0000313|EMBL:AEB94303.1, ECO:0000313|Proteomes:UP000007812};
RN [1] {ECO:0000313|EMBL:AEB94303.1, ECO:0000313|Proteomes:UP000007812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar-4 {ECO:0000313|EMBL:AEB94303.1,
RC ECO:0000313|Proteomes:UP000007812};
RX PubMed=21551305; DOI=10.1128/JB.05038-11;
RA Liu L.J., You X.Y., Zheng H., Wang S., Jiang C.Y., Liu S.J.;
RT "Complete genome sequence of Metallosphaera cuprina, a metal sulfide-
RT oxidizing archaeon from a hot spring.";
RL J. Bacteriol. 193:3387-3388(2011).
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, ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP002656; AEB94303.1; -; Genomic_DNA.
DR RefSeq; WP_013736803.1; NC_015435.1.
DR AlphaFoldDB; F4FYR4; -.
DR STRING; 1006006.Mcup_0194; -.
DR GeneID; 10492389; -.
DR KEGG; mcn:Mcup_0194; -.
DR PATRIC; fig|1006006.8.peg.195; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_7_0_2; -.
DR OrthoDB; 6555at2157; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000007812; 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; 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: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:0000256|RuleBase:RU003523}.
FT DOMAIN 6..272
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 523 AA; 58149 MW; DB8756FC2A3E20AB CRC64;
MVKKSIEILD TTLRDGAQAA SISFTLREKI RIALLLDDLG VDYIEAGWPG SNPKDYEFFR
EIKNYSLKNS KIAAFASTRK KDVRPEKDQN LLSILESDVN SAVLFGKSWT LHVKEVLKTT
LEDNLMIIAD SIEFLKDHGL EVIFDAEHFY QGFKEDPDYA LKVVNVAGEA GAKVVALADT
NGGTLPHEVM EITKYVAERT RVKLGVHMHN DSGTAVANSL VGVVSGATHV QGTINGIGER
TGNADLIQII PNLAIKMGYK VLKENESLKK LRTVSSVVYE LAGLHPNPFQ PYVGENAFAH
KAGVHADAVM KNTKAYEHID PTLIGNQRKV IISELSGTSN LINYLEKIGI KIEKKEEKLK
RALSIIKELE ARGYSFDLAP ESALLIVLKE LGLYEKFFDL KYWKVINEDK LALAVIKVNS
RVEVAEGAGP INAADLALRR CLVKDFPELE KVKLTDYRVI LPGEVKNTES VVRVTIEFND
GDRTWRTEGV STSVIEASVM ALTDGFDYYL QLNKKLKPLF LKD
//
