ID A0A402DVP8_9CELL Unreviewed; 548 AA.
AC A0A402DVP8;
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 Name=cimA {ECO:0000313|EMBL:GCE78197.1};
GN ORFNames=CBZ_32530 {ECO:0000313|EMBL:GCE78197.1};
OS Cellulomonas biazotea.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1709 {ECO:0000313|EMBL:GCE78197.1, ECO:0000313|Proteomes:UP000289954};
RN [1] {ECO:0000313|EMBL:GCE78197.1, ECO:0000313|Proteomes:UP000289954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC12680 {ECO:0000313|EMBL:GCE78197.1,
RC ECO:0000313|Proteomes:UP000289954};
RA Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA Otoguro M., Yanagida F., Hayakawa M.;
RT "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
RL Submitted (JAN-2019) 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:GCE78197.1}.
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DR EMBL; BIMR01000334; GCE78197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402DVP8; -.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00047; UER00066.
DR Proteomes; UP000289954; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 17..282
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 548 AA; 58966 MW; 5F4BFBD29088AFF5 CRC64;
MTALAPTPTG LPTALSFQVY DTTLRDGAQQ EGMNLSVADK LAIAPLLDEL GVGFIEGGWP
GAVPKDTEFF KRAAKELDLR NAELAAFGST RKAGTRAVDD PQVRALIDSE APVVALVAKS
DLRHAERALR TTGEENLAMI ADTVRLLVRE GRRVVVDAEH FFDGYRFDPA YSRSAVLAAF
EAGAEVVALC DTNGGMIPAW VARVVHEIRD AVGPDAVLGM HAHNDSGCAV ANTLAAVEAG
CSHVQGTVNG YGERTGNADL LSVVANLELK YGARVLRTDD ERPGGLSELT RIAHAIAEIT
NISPFARQPY VGASAFAHKA GLHASAIRVD PDLYQHIDPM QVGNDMRMLV SDMAGRASIE
LKGRELGFDL SGMPEVLGRV TDRVKDAEAR GYTYEAADAS FELLLVEEVH GARPQYFRVE
SWRAIVERVG GRGTLATAEA TVKLHAGGER FVSTGEGNGP VNALDHALRQ ALVRVYPEVE
QFELIDFKVR ILDSMHGTDA VTRVLIETTD GQRSWSTVGV GANLLEASWE ALTDSTIWGL
HERGVTPR
//
