ID A0A2U1KC58_ARTAN Unreviewed; 590 AA.
AC A0A2U1KC58;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE SubName: Full=NAD(P)-binding domain, RmlD-like substrate binding domain protein {ECO:0000313|EMBL:PWA34338.1};
GN ORFNames=CTI12_AA620100 {ECO:0000313|EMBL:PWA34338.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA34338.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA34338.1, ECO:0000313|Proteomes:UP000245207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC TISSUE=Leaf {ECO:0000313|EMBL:PWA34338.1};
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000256|ARBA:ARBA00007637}.
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:PWA34338.1}.
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DR EMBL; PKPP01022965; PWA34338.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1KC58; -.
DR STRING; 35608.A0A2U1KC58; -.
DR Proteomes; UP000245207; Unassembled WGS sequence.
DR CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43000; DTDP-D-GLUCOSE 4,6-DEHYDRATASE-RELATED; 1.
DR PANTHER; PTHR43000:SF41; NAD(P)-BINDING DOMAIN, RMLD-LIKE SUBSTRATE BINDING DOMAIN PROTEIN-RELATED; 1.
DR Pfam; PF01370; Epimerase; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000245207}.
FT DOMAIN 1..232
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
FT DOMAIN 336..465
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 590 AA; 66396 MW; B942F18E681E5A72 CRC64;
MHFAAQTHVD NSFGNSFEFT KNNIYGTHVL LEACKVTRGQ IRRFIHVSTD EVYGETEEDA
VVGNHEASQL LPTNPYSATK AGAEMLVMAY GRSYGLPVIT TRGNNVYGPN QFPEKLIPKF
ILLAMRGQPL PIHGDGSNVR SYLYCEDVAE AFEVVLHKGE VGHVYNIGTK KERRVNDVAR
DVCNLFNIDP ESSIKFVENR PFNDQRYFLD DEKLKCLGWS ERTTWQEGLK KTMEWYTSNP
DWWGDVSGAL LPHPRMLMMP GGVEKVIDVP ENVQSDSPHA AVNSSQFQKV VPAAKTSTNS
ATKPSFKFLI YGKTGWIGGL LGKICEKQGI QYEYGKGRLE DRSSIVADIK NVKPTHVFNA
AGVTGRPNVD WCESHKTETI RTNVSGTLTL ADVCRDQGIL VMNFATGCIF EYDAAHPEGS
GIGFLEEDTP NFTGSFYSKT KAMVEELLKE YDNVCTLRVR MPISSDLNNP RNFVTKIARY
DKVVNIPNSM TILDELLPIS IEMAKRNLKG IWNFTNPGVV SHNEVLELYK QYINPEFKWK
NFTLEEQAQV IVAPRSNNEL DTSKLKKEFP ELLSIKESLV KYVFAPNKKA
//