ID A0A2P6V120_9CHLO Unreviewed; 475 AA.
AC A0A2P6V120;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=NAD(P)-binding Rossmann-fold superfamily isoform 1 {ECO:0000313|EMBL:PSC67789.1};
GN ORFNames=C2E20_8590 {ECO:0000313|EMBL:PSC67789.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC67789.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC67789.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC67789.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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:PSC67789.1}.
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DR EMBL; LHPF02000048; PSC67789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6V120; -.
DR STRING; 554055.A0A2P6V120; -.
DR Proteomes; UP000239649; Unassembled WGS sequence.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR PANTHER; PTHR43242; NAD(P)-BINDING ROSSMANN-FOLD SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR43242:SF1; NAD(P)-BINDING ROSSMANN-FOLD SUPERFAMILY PROTEIN; 1.
DR Pfam; PF01370; Epimerase; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000239649}.
FT DOMAIN 6..110
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT DOMAIN 269..468
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT REGION 122..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 49821 MW; B8F3FD5BA824EA9F CRC64;
MSPPAVLVVG GSGYIAQFLV HHFAQSGCQV GLCYHSTLPP SLPKNVTAFK VDLVSGAGLA
EALTALTAGG RPLTAVINCA AISQPAACER DPAAAEAINV PTKLLDALEQ WWAARQVAAA
AARGGGGEQQ PAAQGAQQQQ QTGQQQQAEQ QQQQQQQQQQ QQQQQHGKKL GLAKLLSRIS
AGAAGLVHHH QANGSSSGAD ANGGGRSSGT GGMRGFSSGG PRDRNGATGG SRGLGSGRYG
TSGPRLGGGA DGGGGGSLGG GTGGEQPPLL IQFSTDQVYD GSKQRWREDD ECRPVNAYGR
SKLKAEQAVA ARWPNHAILR SSIIYGPDPP LAPVGRTLFL QFIDSVLQDQ RPTPFYVDEF
RSPVRVRDIV RVVQTLIFRQ GELKHRLFNM GGPDRLSRAD MALAVAEAHG HSPACIQSVP
AASVGRRGAG GVAVVSPADI SMDSSRLEQE LHLPLTPFKT ALEHIFKAHD HHDHQ
//