ID A6QYH1_AJECN Unreviewed; 1466 AA.
AC A6QYH1;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:EDN05825.1};
GN ORFNames=HCAG_02428 {ECO:0000313|EMBL:EDN05825.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN05825.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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}.
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DR EMBL; CH476656; EDN05825.1; -; Genomic_DNA.
DR STRING; 339724.A6QYH1; -.
DR VEuPathDB; FungiDB:HCAG_02428; -.
DR HOGENOM; CLU_250461_0_0_1; -.
DR OMA; VNIHIMA; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000009297; 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 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:UP000009297};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 305..333
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 336..510
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 537..719
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 873..1151
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 25..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 686..724
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 305..333
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 32..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1466 AA; 162847 MW; 4DE10B2251123907 CRC64;
MAPIPIKRGA TDDFILTLSD DEDSNLFNGD IDLDDAGDHD LVSAERPKSK LKVSGTKRKR
DEEPTANGAH NKKSKKAQKK DRTKKQTDKD AGLERDSETE QDVSEDDDGA LDPDFVFDVG
GAAGMKLVED FDGWGLDERS GITIGGNGNK KTVDIDDIIS RRQQKMREKL VKKKKEQKKA
EERSGEEFTG IDSQDEGELA NAVDFEEDEL LAPDGFGMGA VSESEEESDK PVLDDTSEGE
AEADSSSDTD SDNDSVASPV PHPEDITSDD GSGDESEDAA EIEKQKSFFA PEEKPSANGD
LKSAKSFQAF SLSRPILRGL TSVGFTTPTP IQRKTIPVAL LGKDVVGGAV TGSGKTGAFI
IPILERLLYR PRKVPTSRVA ILMPTRELAV QCYNVATKLA TFTDITFCQL VGGFSLREQE
NILKKRPDVI IATPGRFIDH MRNSASFTVD TLEILVLDEA DRMLEDGFAD ELNEILTTIP
KSRQTMLFSA TMTNNVDKLI RVGLSRPVRL MVDAKKQTVG TLIQEFVRLR PGREEKRLGY
LIVLCKNIYK DRVIVFFRSK KEAHRVRIIF GLLGLKVTEL HGSMSQEQRI KSVESFRDGK
VSFLLATDVA SRGLDIKGVE TVINYEAPQS HAIYLHRVGR TARAGRSGRA CTLAAEPDRK
VVKAAVKTGR AQGAKIVSRL IETAEADKWA AKVEEMQEEV QEILREEKEE KQLAQAEMEV
TRGSNLLNHE KEIMSRPKRT WFESEKEKLQ AKQRSLEELN GPSKKKKGKL SGKDKKKLDD
NRERREGKIV NIHIMALLGS RISLYSIVVL YTIWATDGIP NPSHNPYNTI CLLRTEKLTS
PIRLKDPSTK YKPFKPLDLP NRQWPSKTLN KRPRWLATDL RDGNQSLVDP MDGDQKLRYF
RMLVEIGYKE IEISFPSASQ TDYDFTRRLV ESPSEVPADV WLQVLCPCRE DFIRRTVDSL
KGAKKAILHL YLATSECFRR IVFGMSKQES LEMAVRCTKY ARSITKDDPS TSGTEWLFEF
SPETFSDTDP DFVLEICEAV KAAWEPTVEA PLIFNLPATV EMSTPNVYAD QIEYFSTNIS
DREKVCVSLH PHNDRGCAVA AAELAQMAGA QRVEGTLFGN GERTGNVDLV TLALNLYTQG
ISPGVDFSDI NSVIKVVEAS NKIPVNERWP YGGQLVVCAF SGSHQDAIKK GFQLREKSKA
ADADRWQIPY LPIDPEDIGR NYEAIIRVNS QSGKGGVAWV ILRSLELDLP RGLQIAFSKV
IQTQADRLGR ELLPKEIVSL FEEAYHLKHK ARFSLVDYNI TTDRSQSPAP PEPGKALNTK
NLKRRFAGII EIDGIQHAIV GEHAIGAHRD TKAATYIECT SADSSEKVWG VGIHQDVVQA
SLTALLSAAS SIFLPIQFLT SRANTPVPFR PVNVKTLTEA DLEALKQIQG NIGPDRSLVR
DNANVGATIA QQKVDISKLE AQANNL
//
