ID F3ZZQ8_MAHA5 Unreviewed; 523 AA.
AC F3ZZQ8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN OrderedLocusNames=Mahau_2778 {ECO:0000313|EMBL:AEE97905.1};
OS Mahella australiensis (strain DSM 15567 / CIP 107919 / 50-1 BON).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family IV. Incertae Sedis; Mahella.
OX NCBI_TaxID=697281 {ECO:0000313|EMBL:AEE97905.1, ECO:0000313|Proteomes:UP000008457};
RN [1] {ECO:0000313|Proteomes:UP000008457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC {ECO:0000313|Proteomes:UP000008457};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Teshima H., Brettin T.,
RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Pukall R.,
RA Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Mahella australiensis DSM 15567.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEE97905.1, ECO:0000313|Proteomes:UP000008457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC {ECO:0000313|Proteomes:UP000008457};
RX PubMed=21886860;
RA Sikorski J., Teshima H., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Huntemann M.,
RA Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Land M., Hauser L., Ngatchou-Djao O.D., Rohde M.,
RA Pukall R., Spring S., Abt B., Goker M., Detter J.C., Woyke T., Bristow J.,
RA Markowitz V., Hugenholtz P., Eisen J.A., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Mahella australiensis type strain (50-1
RT BON).";
RL Stand. Genomic Sci. 4:331-341(2011).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00034270};
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; CP002360; AEE97905.1; -; Genomic_DNA.
DR RefSeq; WP_013782328.1; NC_015520.1.
DR AlphaFoldDB; F3ZZQ8; -.
DR STRING; 697281.Mahau_2778; -.
DR KEGG; mas:Mahau_2778; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_7_0_9; -.
DR OrthoDB; 9804858at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000008457; Chromosome.
DR GO; GO:0043714; F:(R)-citramalate synthase activity; IEA:RHEA.
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:UniProtKB-KW.
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 Acyltransferase {ECO:0000313|EMBL:AEE97905.1};
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:UP000008457};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 4..266
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 523 AA; 57606 MW; 72F265C8ACF70D96 CRC64;
MQKIYIYDST LRDGMQAEGI SFSLEDKLKI VEQLDAMGVD YIEAGNPGSN PKDLDLFNVL
QEKGLGHARL VAFGSTRRAN IDAEGDRNLS AMLAAGTSAI AIFGKSWDFH VTQVLHTTLD
ENLRMIADSV AYMKQHGKEV IFDAEHFFDG YKRNPEYAMK TLEAAVNAGA DSLALCDTNG
GAFPMEIYDI TKCVVERFNI PVGIHCHNDG GMAVANTIMG VQAGAVQVQG TLNGYGERCG
NADLFPIIAN LQLKMGYRCI PDEKMAELTT ISRYISEIAN LPPDTKAPYV GASAFTHKAG
MHIDAVLKAP TSFEHIDPAL IGNSRRLLMS EMSGRSTVLT RMKRFDQSLT KDSPEVQAVI
DELKRLEYEG YQFEGAEASF DLLIMKQLGR YKKLFDIKDF KVIADQPWQS EDNSAVAMIK
VLVDGTEEMT AAEGDGPVDA LDKALRKALE VFYPQLKKMH LTDYKVRVLD SRAATAAKVR
VLIESSDGQY SWSTVGVSTN IIAASWIAMI DAIEYMLLKG DDI
//
