GenomeNet

Database: UniProt
Entry: I4G1B9_MICAE
LinkDB: I4G1B9_MICAE
Original site: I4G1B9_MICAE 
ID   I4G1B9_MICAE            Unreviewed;       546 AA.
AC   I4G1B9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325};
DE            EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330};
GN   ORFNames=MICAC_2490006 {ECO:0000313|EMBL:CCI01730.1};
OS   Microcystis aeruginosa PCC 9443.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Microcystaceae; Microcystis.
OX   NCBI_TaxID=1160281 {ECO:0000313|EMBL:CCI01730.1, ECO:0000313|Proteomes:UP000003480};
RN   [1] {ECO:0000313|EMBL:CCI01730.1, ECO:0000313|Proteomes:UP000003480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9443 {ECO:0000313|EMBL:CCI01730.1,
RC   ECO:0000313|Proteomes:UP000003480};
RA   Genoscope - CEA;
RL   Submitted (APR-2012) 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:CCI01730.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAIJ01000167; CCI01730.1; -; Genomic_DNA.
DR   RefSeq; WP_002767151.1; NZ_HE972962.1.
DR   AlphaFoldDB; I4G1B9; -.
DR   HOGENOM; CLU_022158_7_0_3; -.
DR   UniPathway; UPA00047; UER00066.
DR   Proteomes; UP000003480; 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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:CCI01730.1};
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          7..277
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   546 AA;  60540 MW;  FB87B923E7002D37 CRC64;
     MNNGKRIWVY DTTLRDGAQR EGISLSLEDK IKIARELDRM GIPFIEGGWP GANPRDGQFF
     RKMHEEPLKQ AELVAFCSTR RPHVEAREDP MLTAILAART RWVTIFGKSW DLHVTEGLKT
     SLEENLAMIG DTIEYLRCQG RRVIYDAEHW FDGYKNHPEY ALLTLKTARD AGAEWLVFCD
     TNGGTLPQEI APIVEKVREQ LGIDPDEENA PQLGIHAHND AGTAVANSLA AVNEGARMIQ
     GTINGYGERC GNANLCTLIP NLQLKMGFSC LEENQLGRLT GTSRKISEMV NLAPDDHAPF
     VGRSAFAHKG GIHVSAVAKN PLTYEHINPE AIGNQRRIVI SDQSGLSNVL AKARSFGIDL
     NKDDPTCRQI LERLKILESQ GYQFEAAEAS FELLMREALG QRSHLFELKG FQVYCDMLRD
     SGNAIATIKV QVKEEDLLEV AEGNGPVAAL DMALRKALVK FYPEIANFHL TDYKVRILDS
     GSGTAAKTRV LIESSNGQQR WTTVGVSSNI LEASYQAVVE GIEYGLYLLQ NNKLELSGQF
     CPLGII
//
DBGET integrated database retrieval system