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Database: UniProt
Entry: A0A2A4G6X4_9FLAO
LinkDB: A0A2A4G6X4_9FLAO
Original site: A0A2A4G6X4_9FLAO 
ID   A0A2A4G6X4_9FLAO        Unreviewed;       390 AA.
AC   A0A2A4G6X4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE            EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN   ORFNames=B7P33_10535 {ECO:0000313|EMBL:PCE63704.1};
OS   Sediminicola luteus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Sediminicola.
OX   NCBI_TaxID=319238 {ECO:0000313|EMBL:PCE63704.1, ECO:0000313|Proteomes:UP000219559};
RN   [1] {ECO:0000313|EMBL:PCE63704.1, ECO:0000313|Proteomes:UP000219559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HQA918 {ECO:0000313|EMBL:PCE63704.1,
RC   ECO:0000313|Proteomes:UP000219559};
RA   Chen L.;
RT   "A new member of the family Flavobacteriaceae isolated from ascidians.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004689}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {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:PCE63704.1}.
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DR   EMBL; NBWU01000004; PCE63704.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4G6X4; -.
DR   OrthoDB; 9804858at2; -.
DR   Proteomes; UP000219559; Unassembled WGS sequence.
DR   GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd07940; DRE_TIM_IPMS; 1.
DR   Gene3D; 1.10.238.260; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
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; 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:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219559};
KW   Transferase {ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          6..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   390 AA;  42970 MW;  5478EE7FAA47B67F CRC64;
     MSKEKVHIFD TTLRDGEQVP GCKLDTQQKL IIAERLDLLG VDVIEAGFPI SSPGDFTSVS
     EIAKVVKEAT VCGLTRAVKK DIEVAAQALV HAKRPRIHTG IGTSDSHIRY KFNTTKDKII
     ERAVEAVKYA KSFVEDVEFY AEDAGRTDNE FLAKVCEEVI KAGATVLNIP DTTGYCLPEE
     YGAKMKYLRE NVKGIDKAIL SCHCHNDLGL ATANSIAGVQ HGARQIECTI NGIGERAGNT
     SLEEVVMILR QHPDLNLDTN INSRLLNEMS RMVSEKMGMI VQPNKAIVGS NAFAHSSGIH
     QDGVIKNRET YEIIDPADVG VDESSIVLTA RSGRAALAYR AKKVGYELSK RQLDVVYVEF
     LKFADRKKEV ADNDIHLIME LSKLEIENLA
//
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