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Database: UniProt
Entry: A0A250VC56_STROL
LinkDB: A0A250VC56_STROL
Original site: A0A250VC56_STROL 
ID   A0A250VC56_STROL        Unreviewed;       534 AA.
AC   A0A250VC56;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   Name=cimA {ECO:0000313|EMBL:GAX51674.1};
GN   ORFNames=SO3561_03181 {ECO:0000313|EMBL:GAX51674.1};
OS   Streptomyces olivochromogenes.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1963 {ECO:0000313|EMBL:GAX51674.1, ECO:0000313|Proteomes:UP000217446};
RN   [1] {ECO:0000313|Proteomes:UP000217446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3561 {ECO:0000313|Proteomes:UP000217446};
RA   Dohra H., Kodani S.;
RT   "Streptomyces olivochromogenes NBRC 3561 whole genome shotgun sequence.";
RL   Submitted (MAY-2017) 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:GAX51674.1}.
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DR   EMBL; BDQI01000005; GAX51674.1; -; Genomic_DNA.
DR   RefSeq; WP_067371367.1; NZ_KQ948457.1.
DR   AlphaFoldDB; A0A250VC56; -.
DR   STRING; 1963.AQJ27_20845; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000217446; Unassembled WGS sequence.
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; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:GAX51674.1};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217446};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          11..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   534 AA;  57786 MW;  1058017E68276A57 CRC64;
     MTETSELDDS FHVFDTTLRD GAQREGINLT VADKLAIARH LDDFGVGFIE GGWPGANPRD
     TEFFARAQQE IDFKHAELVA FGATRRAGGK ASEDPQVKAL LDSGAQVITL VAKSHDRHVE
     LALRTTLDEN LEMVRDTVSH LCAQGRRVFV DCEHFFDGYR ANPEYAKAVV RAAWEAGADV
     VILCDTNGGM LPAQVQAVVA TVLADTGARL GMHAQDDTGC AVANTLAAVD AGATHVQCTA
     NGYGERVGNS NLFPVVAALE LKYGKKVLPD GALREMTRIS HAIAEVVNLT PSTHQPYVGV
     SAFAHKAGLH ASAIKVDPDL YQHIDPEQVG NTMRMLVSDM AGRASIELKG KELGIDLGGD
     RELVGRVVER VKERELKGYT YEAADASFEL LLREEAEGRA RTYFQVESWR AIVEDRPDGT
     HANEATVKLF AKGERIVATA EGNGPVNALD RALRVALEKI YPQLAKLELV DYKVRILEGK
     HGTQSTTRVL ISTSDGAGEW STVGVAENVI AASWQALEDA YTYGLLRAGV EPAE
//
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