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Database: UniProt
Entry: C0QDD1_DESAH
LinkDB: C0QDD1_DESAH
Original site: C0QDD1_DESAH 
ID   C0QDD1_DESAH            Unreviewed;       530 AA.
AC   C0QDD1;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   Name=leuA3 {ECO:0000313|EMBL:ACN15195.1};
GN   OrderedLocusNames=HRM2_20970 {ECO:0000313|EMBL:ACN15195.1};
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN15195.1, ECO:0000313|Proteomes:UP000000442};
RN   [1] {ECO:0000313|EMBL:ACN15195.1, ECO:0000313|Proteomes:UP000000442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC   {ECO:0000313|Proteomes:UP000000442};
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN15195.1; -; Genomic_DNA.
DR   RefSeq; WP_015903966.1; NC_012108.1.
DR   AlphaFoldDB; C0QDD1; -.
DR   STRING; 177437.HRM2_20970; -.
DR   KEGG; dat:HRM2_20970; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_7_0_7; -.
DR   OrthoDB; 9803573at2; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000000442; 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: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   Acyltransferase {ECO:0000313|EMBL:ACN15195.1};
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:UP000000442};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          4..275
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   530 AA;  58410 MW;  06B1F866C3B053D6 CRC64;
     MKQVLIYDTT LRDGMQGENI CFSPEEKVKI AQKLDDMGIH YIEGGWPGSN PSAVRFFDLI
     KDVKFKCAKI AAFGSTRRAN TRAREDRNLQ ALVKCGAPVV TIFGKSWNLH VEKIMNNTAE
     ENLAMIEESI VFLIGEKREV IYDAEHFFDG FIADPDYAIA TLKAAIKGGC KTLVLCDTNG
     GTLPHELEKI TRTVTATMEQ TYDFPVQIGI HTHNDIGMAV ANAITAVRAG AGMVQGTING
     YGERCGNADL TSIIPILALK MDSPCVSPEN LKKLLPLSRF VSETANMTPL NSRPFVGKSA
     FTHKGGIHVS AVMKQSCAYE HMDPSLVGNK RRVLVSEQSG KSNVLYKAKE MGLDLGPDDA
     FSQNIISAIK ELEEDGYQFD VAEGSLKIIM EKLSEQYESH FELESFRVSI EKNRDQPCYA
     HATIKIRVGD TFEITAAEGD GPVSALDNAL RKALTKIYPT ISDMHLIDFK VRVIEGSGST
     DSKVRVLIES RDENNIFSTI GVSEDIIEAS WQALADSFQY KLALDKENSV
//
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