ID D3RYJ8_FERPA Unreviewed; 489 AA.
AC D3RYJ8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Putative (R)-citramalate synthase CimA {ECO:0000256|HAMAP-Rule:MF_01028};
DE EC=2.3.3.21 {ECO:0000256|HAMAP-Rule:MF_01028};
GN Name=cimA {ECO:0000256|HAMAP-Rule:MF_01028};
GN OrderedLocusNames=Ferp_1410 {ECO:0000313|EMBL:ADC65561.1};
OS Ferroglobus placidus (strain DSM 10642 / AEDII12DO).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Ferroglobus.
OX NCBI_TaxID=589924 {ECO:0000313|EMBL:ADC65561.1, ECO:0000313|Proteomes:UP000002613};
RN [1] {ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D.,
RA Lovley D., Kyrpides N., Anderson I.J., Woyke T.;
RT "Complete sequence of Ferroglobus placidus DSM 10642.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADC65561.1, ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RX PubMed=22180810; DOI=10.4056/sigs.2225018;
RA Anderson I., Risso C., Holmes D., Lucas S., Copeland A., Lapidus A.,
RA Cheng J.F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Woyke T.,
RA Lovley D., Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Ferroglobus placidus AEDII12DO.";
RL Stand. Genomic Sci. 5:50-60(2011).
CC -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A
CC to form (R)-citramalate. {ECO:0000256|HAMAP-Rule:MF_01028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+);
CC Xref=Rhea:RHEA:19045, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30934, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.21; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01028};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from pyruvate: step 1/3. {ECO:0000256|HAMAP-
CC Rule:MF_01028}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01028}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|ARBA:ARBA00006154, ECO:0000256|HAMAP-
CC Rule:MF_01028, ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP001899; ADC65561.1; -; Genomic_DNA.
DR RefSeq; WP_012965904.1; NC_013849.1.
DR AlphaFoldDB; D3RYJ8; -.
DR STRING; 589924.Ferp_1410; -.
DR PaxDb; 589924-Ferp_1410; -.
DR GeneID; 8778928; -.
DR KEGG; fpl:Ferp_1410; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_0_1_2; -.
DR OrthoDB; 6555at2157; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000002613; Chromosome.
DR GO; GO:0043714; F:(R)-citramalate synthase activity; IEA:InterPro.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR CDD; cd07940; DRE_TIM_IPMS; 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 HAMAP; MF_01028; CimA; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR024890; Citramalate_synthase_CimA.
DR InterPro; IPR011830; LEU1_arch.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR02090; LEU1_arch; 1.
DR PANTHER; PTHR42880:SF2; (R)-CITRAMALATE SYNTHASE CIMA; 1.
DR PANTHER; PTHR42880; 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|HAMAP-Rule:MF_01028};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_01028};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624, ECO:0000256|HAMAP-
KW Rule:MF_01028}; Reference proteome {ECO:0000313|Proteomes:UP000002613};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01028}.
FT DOMAIN 3..255
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 489 AA; 52640 MW; D7149DF34F88CBB1 CRC64;
MSVIILDTTL RDGEQTPGVS LSVEQKLMIA EALDNLGVDI IEAGTAIASE GEFKAIKAIS
EAGLKAEICS FGRIKKEDID AAADAGADSI FMVAPSSDIH INSKFPGKTR EDIIQMSIEM
VEYAKERGLI VEFGGEDASR ADFEFIKKLL KAGEEAGADR LTFTDTVGVL TPERAQQIMS
ELKKVVKKPV AFHGHDDFGL ATANTIFAVK GGADEIHCCV NGLGERAGNA ALEEVVMALE
YLYGIKTKIN KKAIYPTSKL VEKLTRVVVP PNKPIVGENA FTHESGIHTS AVLRDAKTYE
PISPEVIGRS RSIVLGKHAG KASVEAIMKE LGYKATKEQM QEILKRVKEI GDKGKRVTDA
DVRAIIETVL QIKRERKVEL VDLNVVSGAN IMPTASVKLK INGKEYVEAG VGVGPVDAAI
NAIKRAVKEY ADIELVSYHV DAITGGTDAL VDVIVQLKKG DKIVTARGAR TDIIMASVEA
FVEGLNMLL
//
