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Database: UniProt
Entry: A0A0S1SME1_9BACT
LinkDB: A0A0S1SME1_9BACT
Original site: A0A0S1SME1_9BACT 
ID   A0A0S1SME1_9BACT        Unreviewed;       549 AA.
AC   A0A0S1SME1; A0A0S1SHC7; A0A0S1SLS0; A0A0S1ST71; A0A0S1SXA7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:ALM12896.1};
GN   ORFNames=PeribacterD1_0195 {ECO:0000313|EMBL:ALM12896.1};
OS   Candidatus Peribacter riflensis.
OC   Bacteria; Candidatus Peregrinibacteria; Candidatus Peribacteria;
OC   Candidatus Peribacterales; Candidatus Peribacteraceae; Peribacter.
OX   NCBI_TaxID=1735162 {ECO:0000313|EMBL:ALM12896.1, ECO:0000313|Proteomes:UP000069135};
RN   [1] {ECO:0000313|Proteomes:UP000069135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Anantharaman K., Brown C.T., Burstein D., Castelle C.J., Probst A.J.,
RA   Thomas B.C., Williams K.H., Banfield J.F.;
RT   "Analysis of five complete genome sequences for members of the class
RT   Peribacteria in the recently recognized Peregrinibacteria bacterial
RT   phylum.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALM12896.1, ECO:0000313|Proteomes:UP000069135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIFOXYD1_FULL_PER-ii_59_16 {ECO:0000313|EMBL:ALM12896.1};
RX   PubMed=26844018;
RA   Anantharaman K., Brown C.T., Burstein D., Castelle C.J., Probst A.J.,
RA   Thomas B.C., Williams K.H., Banfield J.F.;
RT   "Analysis of five complete genome sequences for members of the class
RT   Peribacteria in the recently recognized Peregrinibacteria bacterial
RT   phylum.";
RL   PeerJ 4:E1607-E1607(2016).
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DR   EMBL; CP013065; ALM12896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S1SME1; -.
DR   STRING; 1735162.PeribacterB2_0195; -.
DR   KEGG; prf:PeribacterA2_0195; -.
DR   Proteomes; UP000069135; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.270; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          14..278
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   549 AA;  60113 MW;  26710420B86E070B CRC64;
     MESASSPITE PQQVIVFDTT LRDGDQAGVL FDEDQKVVIA HSLEDIGVDV IEAGNAFSGT
     FDQRSIARIA QEVRRPVICS LAICKRESVE ASAKALERAE HPRIHIYRAS SREHLDKVFH
     GMGEEQYLDD IAAHIELARR YVPDVEYSAE DATNTPREFL ARIGIRAAEA GATTFNIPDT
     YGQALPTEME ELMAYLSQNI PAIREHRMRQ STHNHDDHGL ATANTLYALK GMGDALKQAE
     LTVNGLGERA GNASLAETVM TARYRKDRFP MVNFDHIRAE MLVRLSRIVS ALSRVSVPRN
     TPFVGTGINA LGTGTHVAAQ DRIGIRNGAY RDNVPQDVGF DDFNIEFGAT SGKGVADVYA
     RQLGYHIPET DLVPFTAFAK AFAETKRGTE CRIVTPDEYR SLLFQYFGVG VPIESTGGTQ
     FLRAAKNGQW EVHLTVSGRN GEQTLTGHSE EKQGVLQAVT AILREQSGLD FQLIDQWEES
     DQTQGERSGS VTGVTIRIGK MECQGTAQGT DVTETTVRAL FDAVNKAKLA SLLTEQQSAT
     SVGAPGRVK
//
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