ID A0A200QWC4_9MAGN Unreviewed; 368 AA.
AC A0A200QWC4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Aldehyde-lyase domain {ECO:0000313|EMBL:OVA14755.1};
GN ORFNames=BVC80_1819g79 {ECO:0000313|EMBL:OVA14755.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA14755.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA14755.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA14755.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC {ECO:0000256|ARBA:ARBA00005568}.
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:OVA14755.1}.
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DR EMBL; MVGT01001025; OVA14755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200QWC4; -.
DR STRING; 56857.A0A200QWC4; -.
DR InParanoid; A0A200QWC4; -.
DR OrthoDB; 324785at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:OVA14755.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402}.
FT DOMAIN 102..333
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT REGION 64..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 39315 MW; B4AC0FA808667FF4 CRC64;
MATSACNNSL IFALKNHSSN GNPSKTLTNF PSTPFSSPSL SIHLSPTTTA TTITSFSKSP
LTLKTLKPSS PPKSSSKTSD LALPDTNPKT LKSRLADGET LYGLFLLSFS PTLAEIAGLA
GYDFVVVDME HGHGGISDAL PCLHALAATG TPAILRLPES SPTWAKKALD LGPQGIMFPM
IDGPKSAKKA VSYCKFPPAG VRGSAHTVVR ASNYGINDGY LTNYEDELLI MCQVESEEAV
KKIEEIAKVD GVDCIQMGPL DLSADLGYLW DPGNKKVREM MRAAEKGVLG TKGGDGGGGA
YLAGFAMPHD SPEQLRMRGY HMISGAVDVG LFRSVVVEDV KRFKMGLMKG SDDEEGDEKD
KDEKYWSE
//
