ID C1FHL1_MICCC Unreviewed; 662 AA.
AC C1FHL1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN ORFNames=MICPUN_96641 {ECO:0000313|EMBL:ACO70119.1};
OS Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO70119.1, ECO:0000313|Proteomes:UP000002009};
RN [1] {ECO:0000313|EMBL:ACO70119.1, ECO:0000313|Proteomes:UP000002009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000064};
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; CP001576; ACO70119.1; -; Genomic_DNA.
DR RefSeq; XP_002508861.1; XM_002508815.1.
DR AlphaFoldDB; C1FHL1; -.
DR STRING; 296587.C1FHL1; -.
DR GeneID; 8246860; -.
DR KEGG; mis:MICPUN_96641; -.
DR eggNOG; KOG2367; Eukaryota.
DR InParanoid; C1FHL1; -.
DR OMA; KSWDFHV; -.
DR OrthoDB; 297661at2759; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000002009; Chromosome 10.
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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 64..337
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 662 AA; 69766 MW; 7D76CD8D66680F6A CRC64;
MSLSLLSGAP LASRSVANLN RRRAGGRARK SKEIPSLFRV PGSVRAVVPR AADSPGSAGD
DADVVCYDTT LRDGSQQVGI SLTCDDKLAV AEHLVGLGVA YIEGGYPGSN PKDVEFFSRW
TSSGLADRAA AGGTKLAAFG MTRRRGVTAD DDEGLKALTD CPAPCVCIVA KAWDEQCEKV
LGVSPEENIA MIEESVAHLV AAGKEVLVDC EHYFDGRKAN PEFAVKCAAA AAKSGAKFVV
LCDTNGGTLP WDVEEFTREV KEAVDATGAD CSVGIHCHND TSLAVANSIA AVRGGATMVQ
GCVNGYGERT GNADLLVVAA NLELKMGRTA LPEGSLQRLT QVSAAVAKLC SQHQDPRQPY
MGSSAFAHKG GLHVAALQKM PASYNHIVPT LVGNEARSVI SELSGRGNIL SAAMASGREV
SKETAAQVLS QIKDLESRGF VLEDAGASVD ILFRRADPNY RAPFNVLEFN VTASNSSFGG
FTPNDLLVGG DERLQDVLPE DELEAPFTHP QQAGYKKGSV AVNQVVVKVD VFDNDTTPAS
RNTQLCVAEG NGPVNALANA LRLSLTDKFP QLKQIHLQDY KVDLLSTAGT SAAVTRVTMD
FADRDTDITW RTVGAHASII EASFRALVDG MEYGIAQCSD DGCMVDPGPA HAADREGAPS
SR
//
