ID G0EHI4_PYRF1 Unreviewed; 343 AA.
AC G0EHI4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:AEM38559.1};
GN OrderedLocusNames=Pyrfu_0690 {ECO:0000313|EMBL:AEM38559.1};
OS Pyrolobus fumarii (strain DSM 11204 / 1A).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrolobus.
OX NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM38559.1, ECO:0000313|Proteomes:UP000001037};
RN [1] {ECO:0000313|EMBL:AEM38559.1, ECO:0000313|Proteomes:UP000001037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037};
RX PubMed=21886865;
RA Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M.,
RA Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Huber H.,
RA Yasawong M., Rohde M., Spring S., Abt B., Sikorski J., Wirth R.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the hyperthermophilic chemolithoautotroph
RT Pyrolobus fumarii type strain (1A).";
RL Stand. Genomic Sci. 4:381-392(2011).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP002838; AEM38559.1; -; Genomic_DNA.
DR AlphaFoldDB; G0EHI4; -.
DR STRING; 694429.Pyrfu_0690; -.
DR KEGG; pfm:Pyrfu_0690; -.
DR eggNOG; arCOG01754; Archaea.
DR HOGENOM; CLU_019796_1_3_2; -.
DR InParanoid; G0EHI4; -.
DR Proteomes; UP000001037; Chromosome.
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:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd05303; PGDH_2; 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; FORMATE DEHYDROGENASE 1; 1.
DR PANTHER; PTHR42938:SF9; 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; PS00670; D_2_HYDROXYACID_DH_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001037}.
FT DOMAIN 38..340
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 140..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 343 AA; 38024 MW; 10D1F5943611AEB8 CRC64;
MHYLLSVSFI GWGASGPAFG AEAWLIAFRV TRLDGMKVLV TDPVDKLLLG ILEKHGLQVD
YRPGVPREEL LKIIGDYDIL VVRSRTKVDR EVIDRGEKLK VIARAGVGLD NIDVQHAIEK
GIKVVNAPGA AAQSVAELTI GLLIAAARFF KAHIVSLERR EWSKGRWTGV ELSGKTLGVI
GFGRIGYRVA KIARGLGMRV LAYDVVDASD RAREIGAEFT RDLDVVLRES DAITLHVPLT
KETYHLIDRD ALEKMKDGVI IVNTSRGPVI DTKALLEYLE SGKVFAAALD VLEHEPPKEE
WEWRLVHHPR VIVTPHIGAE TREAKRRVAE ETAYAILEAL GMR
//
