ID A0A226N7G3_CALSU Unreviewed; 444 AA.
AC A0A226N7G3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=2-ketogluconate reductase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=ASZ78_013475 {ECO:0000313|EMBL:OXB63504.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB63504.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB63504.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB63504.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB63504.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:OXB63504.1}.
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DR EMBL; MCFN01000157; OXB63504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226N7G3; -.
DR STRING; 9009.A0A226N7G3; -.
DR Proteomes; UP000198323; Unassembled WGS sequence.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
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 GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR013706; PDEase_N.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF288; GRHPR REDUCTASE; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF08499; PDEase_I_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000198323}.
FT DOMAIN 21..115
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 116..250
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 283..342
FT /note="3'5'-cyclic nucleotide phosphodiesterase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08499"
FT REGION 411..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OXB63504.1"
SQ SEQUENCE 444 AA; 48907 MW; 612CA39A032B4B64 CRC64;
VMAEQELPGL LIMDIGGTHG VQENIAALLK KHFFVITMKE LLENKKEMGK KIQSIFVSEL
RPTIDRELLE SLPNLKVIGN SGVGVDHLNL KMISNFGIKV TNTPHAVADS TADMGMALML
ASARRLVEGS QIAVSPDTKY FAADWLGVEV TGATLGIIGM GRIGYKVAQR ARAFEMKILY
HNRNRRSKED EQAVGAHYTE MEDLLQQSDF VMLVVNLTPE TEKLIGKREL GLMKPTATLI
NISRGRNISR RWLWLCGEVN LTAKQGNGVN TEDGDMGCDL WHLLDTEDEL SDIQSDSVPS
EVRDWLASTV TRQMGMMLKR TEEKPWFRSI VHAVEAGIFV ERVYRRTSNT VGLSYPPAAI
GVLKIPVSAL VSFVEALQVG SSKHKNPHHS LTHAADGTQT VHQLLFKTGR VLEDPPPWAP
PEVDPPPSAP PEVDPPPSAP PGLL
//