ID V5GY93_ANOGL Unreviewed; 331 AA.
AC V5GY93;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:JAB65383.1};
GN Name=SERA {ECO:0000313|EMBL:JAB65383.1};
OS Anoplophora glabripennis (Asian longhorn beetle) (Anoplophora nobilis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Cerambycidae; Lamiinae; Lamiini; Anoplophora.
OX NCBI_TaxID=217634 {ECO:0000313|EMBL:JAB65383.1};
RN [1] {ECO:0000313|EMBL:JAB65383.1}
RP NUCLEOTIDE SEQUENCE.
RA Scully E.D., Hoover K., Carlson J.E., Tien M., Geib S.M.;
RT "Midgut Transcriptome Profiling of Anoplphora glabripennis, a
RT Lignocellulose Degrading, Wood-Boring Cerambycid.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; GALX01003083; JAB65383.1; -; Transcribed_RNA.
DR RefSeq; XP_018575708.1; XM_018720192.1.
DR AlphaFoldDB; V5GY93; -.
DR EnsemblMetazoa; XM_018720192.1; XP_018575708.1; LOC108914380.
DR GeneID; 108914380; -.
DR KEGG; agb:108914380; -.
DR OrthoDB; 6392at2759; -.
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 CDD; cd12173; PGDH_4; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42938:SF22; D-3-PHOSPHOGLYCERATE DEHYDROGENASE; 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 6..307
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 331 AA; 35774 MW; 4611A18DC75C78E9 CRC64;
MDIKKVLVAD AVDAACVELL QQNSFEVDCK YKLPKDQLIA EIPNYDGLIV RSDTKVTEDV
IKAATKLKVI GRAGAGVDNI DVNAATSKNV LVLNTPGGNA ISACELTCSL ITSLARNVVP
AAASLKAGKW DRKLYTGHEL YGKTLAILGL GRIGREVAIR MQAWGMKTVG YDPIVSSEDA
KKFNVEFLTL EQIWPIADYI TVHTPLIPET RNLICEAVLN KCKKGVRIVN VARGGIINEK
ELLKALKSGQ CGGAAIDVFE QEPPTNPVTL ELIQQEKVIA TPHLGASTTE AQIRVAVEIS
EQFIALTGKN PKYSTTSGVI NRSVLENLKN N
//
