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Database: UniProt
Entry: A0A420V7V7_9ACTN
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ID   A0A420V7V7_9ACTN        Unreviewed;       538 AA.
AC   A0A420V7V7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   ORFNames=DC095_013560 {ECO:0000313|EMBL:RNC73883.1}, SFRA_005415
GN   {ECO:0000313|EMBL:RKM97979.1};
OS   Streptomyces xinghaiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1038928 {ECO:0000313|EMBL:RKM97979.1, ECO:0000313|Proteomes:UP000028058};
RN   [1] {ECO:0000313|EMBL:RKM97979.1, ECO:0000313|Proteomes:UP000028058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM97979.1,
RC   ECO:0000313|Proteomes:UP000028058};
RX   PubMed=25477406;
RA   Bekker O.B., Klimina K.M., Vatlin A.A., Zakharevich N.V., Kasianov A.S.,
RA   Danilenko V.N.;
RT   "Draft Genome Sequence of Streptomyces fradiae ATCC 19609, a Strain Highly
RT   Sensitive to Antibiotics.";
RL   Genome Announc. 2:0-0(2014).
RN   [2] {ECO:0000313|EMBL:RKM97979.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM97979.1};
RA   Danilenko V.N., Bekker O.B., Vatlin A.;
RT   "Genome sequencing of Streptomyces fradiae ATCC 19609.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:RNC73883.1, ECO:0000313|Proteomes:UP000245280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OlgR {ECO:0000313|EMBL:RNC73883.1,
RC   ECO:0000313|Proteomes:UP000245280};
RA   Danilenko V.N., Bekker O.B., Vatlin A.;
RT   "Genome sequencing of Streptomyces xinghaiensis (fradiae) OlgR.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RKM97979.1}.
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DR   EMBL; JNAD02000002; RKM97979.1; -; Genomic_DNA.
DR   EMBL; QFBD02000005; RNC73883.1; -; Genomic_DNA.
DR   RefSeq; WP_043461749.1; NZ_QFBD02000005.1.
DR   AlphaFoldDB; A0A420V7V7; -.
DR   OrthoDB; 9803573at2; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000028058; Unassembled WGS sequence.
DR   Proteomes; UP000245280; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000028058};
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   538 AA;  56547 MW;  808D85DE69F8FD7E CRC64;
     MTAQRFQLYD TTLRDGTQQE GMVLTVDDKL AVARHLDAFG VGFIEGGWPG AVPKDTEFFR
     RARTELRLDT AELAAFGATR KPGVAAAADP QVRALLDAET PVVTLVAKSH PRHVELALRT
     TLAENLAMIG DTVRLLVREG RRVFVDAEHY VDGYRLDRGH ALDVVRAAAD AGAEAVVLCD
     TNGGSLPDAV RAVVTATAGA TGVPLGIHCH DDSGCAVANT IAAVDAGVRH VQGTAHGYGE
     RCGNADLFTV AANLVLKRGL PVVPAARLRG MALSARAVAE LTGVPGRAAA PYVGPAAFTH
     KAGLHASALR VDPGLYQHID PALVGNGMRT LVSDMGGRSS VELKARELGY EVDAGSETVA
     RAAARIKDLE NRGHSFESAD ASFELLLREE LDGGGRPARP FEVVSWDVRV DAGPAGRAPT
     RARVRLRIDG VPLVAEGEGN GPVNALDRAL HAALDPFFPQ LSGLELTDYQ VRVLGRGSEA
     AARVLITFGD GRRTWGTVGV DENTVAASWR ALLDAVHYAL LDTAAPAAAE PTRCAAAG
//
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