ID A0A2I5TL90_SERS3 Unreviewed; 518 AA.
AC A0A2I5TL90;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=CWC46_15020 {ECO:0000313|EMBL:AUH01010.1}, Ser39006_015025
GN {ECO:0000313|EMBL:AUH05331.1};
OS Serratia sp. (strain ATCC 39006).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=104623 {ECO:0000313|EMBL:AUH05331.1, ECO:0000313|Proteomes:UP000017700};
RN [1] {ECO:0000313|EMBL:AUH05331.1, ECO:0000313|Proteomes:UP000017700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH05331.1}, and ATCC 39006 / SC
RC 11482 {ECO:0000313|Proteomes:UP000017700};
RX PubMed=24336377; DOI=10.1128/genomeA.01039-13;
RA Fineran P.C., Iglesias Cans M.C., Ramsay J.P., Wilf N.M., Cossyleon D.,
RA McNeil M.B., Williamson N.R., Monson R.E., Becher S.A., Stanton J.A.,
RA Brugger K., Brown S.D., Salmond G.P.;
RT "Draft genome sequence of Serratia sp. strain ATCC 39006, a model bacterium
RT for analysis of the biosynthesis and regulation of prodigiosin, a
RT carbapenem, and gas vesicles.";
RL Genome Announc. 1:E01039-E01039(2013).
RN [2] {ECO:0000313|EMBL:AUH05331.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH05331.1};
RA Wang G., Yang Y., Su Y.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AUH01010.1, ECO:0000313|Proteomes:UP000233778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH01010.1,
RC ECO:0000313|Proteomes:UP000233778};
RA Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA Fineran P.C.;
RT "Complete genome sequence of Serratia sp. ATCC 39006 LacA.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AUH05331.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:AUH05331.1};
RA Hampton H.G., Jackson S.A., Jauregui R., Poulter G.T.M., Salmond G.P.C.,
RA Fineran P.C.;
RT "Complete genome sequence of Serratia sp. ATCC 39006.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000064};
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 2 subfamily. {ECO:0000256|ARBA:ARBA00009767}.
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DR EMBL; CP025085; AUH01010.1; -; Genomic_DNA.
DR EMBL; CP025084; AUH05331.1; -; Genomic_DNA.
DR RefSeq; WP_021015739.1; NZ_CP025085.1.
DR AlphaFoldDB; A0A2I5TL90; -.
DR STRING; 104623.Ser39006_02475; -.
DR KEGG; sera:Ser39006_015025; -.
DR KEGG; serq:CWC46_15020; -.
DR OrthoDB; 9803573at2; -.
DR Proteomes; UP000017700; Chromosome.
DR Proteomes; UP000233778; Chromosome.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07942; DRE_TIM_LeuA; 1.
DR Gene3D; 3.30.160.270; -; 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; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR039371; LeuA_N_DRE-TIM.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR46911; -; 1.
DR PANTHER; PTHR46911:SF1; 2-ISOPROPYLMALATE SYNTHASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000017700};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 32..305
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 518 AA; 58985 MW; F7D8ADE94DF8F8BA CRC64;
MTAQLSGVKY RHSTPFSWQE RQWPDRMLKQ APRWCSVDLR DGNQALPEPM QMQQKLALYH
QLIAMGYKEI EVGFPAASET DYQFVRALID KQLIPDDVRI QVLTQARESL IAETVASLRG
VPEAVIHLYN STSPQQREQV FNLSCTQVTE LALQGIRWLM AAMEPIEQRW ILQYSPESFT
ATEMDFAVEI CNAVIDLWVG ETGRNIIINL PATVELSTPN VYADQIEWIS GQLHHRDKVT
LCIHPHNDRG CAVAAAEMAM LAGAERVEGT LFGNGERTGN VDLVTLGLNM LVQGIDPMID
FRSLPKVVNI YESSTGMAVP ARHPYAGSLV FTAFSGSHQD AIRKSLELQK YRTYWDVPYL
PLDPHDIGRN YEGIIRINGQ SGKGGLGYLL DYYYGIRPPR PLLIRFQQHI QVMADICNKE
LGHEFLYRQF LAFFDVEAKK FSHDEERPDA TQYNLQPQWD SHRTRDSQIM SYVWATWQND
LVFGVGRGNS EAESRNKAWF QLVMSLPAVA ENQTDRCL
//
