ID A0A443HVU5_BYSSP Unreviewed; 1442 AA.
AC A0A443HVU5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:RWQ95959.1};
GN ORFNames=C8Q69DRAFT_491253 {ECO:0000313|EMBL:RWQ95959.1};
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ95959.1, ECO:0000313|Proteomes:UP000283841};
RN [1] {ECO:0000313|EMBL:RWQ95959.1, ECO:0000313|Proteomes:UP000283841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ95959.1,
RC ECO:0000313|Proteomes:UP000283841};
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Makela M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
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. LeuA type 2 subfamily. {ECO:0000256|ARBA:ARBA00009767}.
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:RWQ95959.1}.
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DR EMBL; RCNU01000004; RWQ95959.1; -; Genomic_DNA.
DR STRING; 264951.A0A443HVU5; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000283841; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR CDD; cd17947; DEADc_DDX27; 1.
DR CDD; cd07942; DRE_TIM_LeuA; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00572; LeuA_type2; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR005668; IPM_Synthase.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR039371; LeuA_N_DRE-TIM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR NCBIfam; TIGR00970; leuA_yeast; 1.
DR PANTHER; PTHR46911; -; 1.
DR PANTHER; PTHR46911:SF1; 2-ISOPROPYLMALATE SYNTHASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50991; PYR_CT; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000283841};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 315..343
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 346..520
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 547..694
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 831..1109
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 696..736
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 315..343
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..38
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..218
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..264
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1442 AA; 160047 MW; 6177C4F058DEA8C0 CRC64;
MAPISTKKRS REDDDFVLTL SDDENPVDVG ESEEEVDGDE FSNKPATKTS GTKRKREAND
AATGKAQQKK QKKQKRKQGG KGANDGEDEE VDEEEEEEDN ALAGAEDDGA LNPDFEFDVA
GASNRGVVED FDGWVMDGVK KSGGDKKGVD IDAIIERRRE RKKDAEERKK RKEQKKKENG
EWDPEASGSE GESANAGEDE EDEDAESVNF EDDELLAEDG FGMGAGDAKE SDDEDEEDKG
SGSDSEDGKE DGDDDDDDED AASDNDSIAS PVAHPDDEAS DSDDESVDEE EAEKRKAFFA
PEEKSTDKSD DNAKGSFQDY NLSRPILRGL AAVGFSTPTP IQRKTIPVAL LGKDIVGGAV
TGSGKTGAFI IPILERLLYR PRKIPTSRVA ILMPTRELAV QCYNVATKLA TFTDITFCQL
VGGFSLREQE NVLKKRPDVI IATPGRFIDH MRNSASFTVD TLEILVLDEA DRMLEDGFAH
ELNEILTTIP KSRQTMLFSA TMTDTVDKLI RVGLNRPVRL MVDSKKSTVT TLVQEFVRLR
PGREGMRLGY LMYLCEEIYT GRVIIFFRQK REAHRVRIVF GLLGLKAAEL HGSMTQEQRI
KSVEDFREGR VAFLLATDVA SRGLDIKGVE TVINYEAPQS HEIYLHRVGR TARAGRSGRA
CTIAAEPDRK VVKQAVKASK AQGAKVVSRV VEPAVADSWA KKVEALAEEV DEILKEEKQE
KQLSQAEMQV NKGENMLKHE REIMSRPKRT WFETERDKQM AKKAALLELN GEAGSKKKKV
KLSNKDKKKL DASRDRHEGR VLKDPSKKYK KFQPLHLPDR QWPNKTLDKP PRWLATDLRD
GNQSLVDPMN GEQKFRFFKM LVDIGYKEIE VAFPSASQTD FDFVRRLVET PGVVPDDVWL
QVLSPCREDL IRRTVDSLRG AKKAILHLYL ATSECFRRIV FGMTKEQSIE LAVRCTKFAR
SITKDDPSMA GTEWLYEFSP ETFSDTDPDF AVQICEAVKA AWEPTEDAPL IFNLPATVEM
ATPNVYADQV EYFCRNMTER EKFCVSLHPH NDRGCAVAAA ELAQMAGAQR VEGTLFGNGE
RTGNVDLVTL ALNLYTQGIH PNVDFSDINS IIKVVEESNK IPVNERWPYG GQLVVCAFSG
SHQDAIKKGF NLRDKAGASE DSRWEIPYLP LDPQDIGRNY EAVIRVNSQS GKGGAAWVIL
RSLELDLPRG LQVEFSKIVQ KETEAVNREL RPNEIVALFE KAYHLKTNPR FTLIDYNITT
DRSQSPAPPE PGKALNTKNL KRRFTGIIEI DGVQHPITGV GPGAISSLAN ALATLGIDLD
VVDYKEHSIG TGRDVKAATY IQCTAAGNQD SVWGVGIHQD VVQASLIALL SAASSFLTSR
AGSPAPFRPI RTVAFSEEDL EALEQLNNNV DLSRTAAGDE AAQAVQKQKV DVEKLAQQVE
NL
//
