GenomeNet

Database: UniProt
Entry: A0A0S3RM23_PHAAN
LinkDB: A0A0S3RM23_PHAAN
Original site: A0A0S3RM23_PHAAN 
ID   A0A0S3RM23_PHAAN        Unreviewed;       309 AA.
AC   A0A0S3RM23;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=Vigan.03G141300 {ECO:0000313|EMBL:BAT81638.1};
GN   ORFNames=VIGAN_03141300 {ECO:0000313|EMBL:BAT81638.1};
OS   Vigna angularis var. angularis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT81638.1, ECO:0000313|Proteomes:UP000291084};
RN   [1] {ECO:0000313|EMBL:BAT81638.1, ECO:0000313|Proteomes:UP000291084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX   PubMed=26616024; DOI=10.1038/srep16780;
RA   Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA   Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA   Tomooka N.;
RT   "The power of single molecule real-time sequencing technology in the de
RT   novo assembly of a eukaryotic genome.";
RL   Sci. Rep. 5:16780-16780(2015).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; AP015036; BAT81638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S3RM23; -.
DR   Proteomes; UP000291084; Chromosome 3.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42938:SF25; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291084}.
FT   DOMAIN          76..288
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          204..264
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   309 AA;  34303 MW;  CD56C45D4C791F99 CRC64;
     MSSRVILNRK SDVNRVLSDP FSHTQRLHHL HRTTTKSFFE YIHSIGIMES NGNLVKHVEK
     QTTRVLFCGP HFPASHEYTA EYLQNHPSTK VDVLSFEDVR KDIANYNVCI VKSIRLDSDI
     ISCTAQMQLI MQYGVGLEGV DIDAATKHGI KVARIPSDVT GNSTSCTEMA IYLMLGLLRK
     HNELQVSIQQ KKLGELITET LFGKTGALLV NIARGGIVDY EAVINNLESG HLGGLGTDVA
     WTEPFNPDDQ IFKFKNVIMT PHVAGVTEHS YRSMAKAVGE VVLQLHAGLP LTGIELLVML
     LFSFMPGFL
//
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