ID E4U3Q9_SULKY Unreviewed; 683 AA.
AC E4U3Q9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN OrderedLocusNames=Sulku_2675 {ECO:0000313|EMBL:ADR35325.1};
OS Sulfuricurvum kujiense (strain ATCC BAA-921 / DSM 16994 / JCM 11577 /
OS YK-1).
OG Plasmid pSULKU02 {ECO:0000313|EMBL:ADR35325.1,
OG ECO:0000313|Proteomes:UP000008721}.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfuricurvum.
OX NCBI_TaxID=709032 {ECO:0000313|EMBL:ADR35325.1, ECO:0000313|Proteomes:UP000008721};
RN [1] {ECO:0000313|EMBL:ADR35325.1, ECO:0000313|Proteomes:UP000008721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1
RC {ECO:0000313|Proteomes:UP000008721};
RC PLASMID=pSULKU02 {ECO:0000313|Proteomes:UP000008721};
RX PubMed=22675602; DOI=10.4056/sigs.2456004;
RA Han C., Kotsyurbenko O., Chertkov O., Held B., Lapidus A., Nolan M.,
RA Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A.,
RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Brambilla E.M., Rohde M., Spring S.,
RA Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of the sulfur compounds oxidizing
RT chemolithoautotroph Sulfuricurvum kujiense type strain (YK-1(T)).";
RL Stand. Genomic Sci. 6:94-103(2012).
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; CP002357; ADR35325.1; -; Genomic_DNA.
DR RefSeq; WP_013449937.1; NC_014755.1.
DR AlphaFoldDB; E4U3Q9; -.
DR KEGG; sku:Sulku_2675; -.
DR HOGENOM; CLU_004588_3_2_7; -.
DR OrthoDB; 9803573at2; -.
DR Proteomes; UP000008721; Plasmid pSULKU02.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:RHEA.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd07942; DRE_TIM_LeuA; 1.
DR Gene3D; 1.10.1220.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR039371; LeuA_N_DRE-TIM.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR46911; -; 1.
DR PANTHER; PTHR46911:SF1; 2-ISOPROPYLMALATE SYNTHASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 Plasmid {ECO:0000313|EMBL:ADR35325.1};
KW Pyruvate {ECO:0000313|EMBL:ADR35325.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008721};
KW Transferase {ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 29..302
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 683 AA; 76717 MW; C69654025D403BDB CRC64;
MHTHTKYTPY PTVTLDKREW ADKSATVAPR WVSTDLRDGN QALANPMGIE QKVAYFKALV
EFGFKEIEVA YPSASQTEFD FCRRLIEEGL IPEDVTIGVL VPSIECHIVR SFEALRGAKR
INIHLYNPTA ANQRSVVFRR SREQIIALAL EGVECIKREA QDFGGEVVFE YSPESFSQTE
LDFARDISNA VITAWEPTRE HPMILNLPNT LEACSPNIYA DRIEWMSKHI KNRESVIISV
HPHNDRGCAV ASSELAVLAG AQRVEGTILG NGERAGNVDL ITLAFNYFSQ GIDPCLRVEK
VDAILSRITS ITGMSVAERH PYVGSMIYTA FSGTHQDAIK KGMEHHREQN SPTWEVPYLA
IDPRDIGREY KDSIRINSQS GKGGVAYVLK EIYGIDVPND MQTKLADEVK RISQKRGGEI
SSDEVLGIYE GMMKRHENSW NAQEYNKHAS FVSTLALPVV DLLAPIEGEV ILDLGCGEGT
LALEIQKSGA KVTGVDLSHE MVKNSRAKGI DATVMSVTEL EFKNRFDAVF SNAVLHWVKE
SETAVRNIYE ALKPNGRFVA EFGGEGNCKT AVDAMKEVFK NHPEFGVFED PWYFPSIKEY
RTLLESCGFR VEYIELIPRP TPVDDIANWL DLFANGVTAH LSREEFSVFK EEVSRITKPK
LYDENDGWHV DYVRLRVKAV KGK
//
