GenomeNet

Database: UniProt
Entry: A7HJ87_FERNB
LinkDB: A7HJ87_FERNB
Original site: A7HJ87_FERNB 
ID   A7HJ87_FERNB            Unreviewed;       303 AA.
AC   A7HJ87;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:ABS59970.1};
DE            EC=1.1.1.95 {ECO:0000313|EMBL:ABS59970.1};
GN   OrderedLocusNames=Fnod_0103 {ECO:0000313|EMBL:ABS59970.1};
OS   Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS59970.1, ECO:0000313|Proteomes:UP000002415};
RN   [1] {ECO:0000313|EMBL:ABS59970.1, ECO:0000313|Proteomes:UP000002415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC   {ECO:0000313|Proteomes:UP000002415};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABS59970.1, ECO:0000313|Proteomes:UP000002415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC   {ECO:0000313|Proteomes:UP000002415};
RX   PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA   Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA   DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA   Noll K.M.;
RT   "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT   the Thermotogales.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000771; ABS59970.1; -; Genomic_DNA.
DR   RefSeq; WP_011993293.1; NC_009718.1.
DR   AlphaFoldDB; A7HJ87; -.
DR   STRING; 381764.Fnod_0103; -.
DR   KEGG; fno:Fnod_0103; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_3_0; -.
DR   OrthoDB; 9786364at2; -.
DR   Proteomes; UP000002415; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002415}.
FT   DOMAIN          10..302
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          105..279
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   303 AA;  33091 MW;  BF5D198A7A55532F CRC64;
     MRVHINDPLD KQATEKLASL PNIQLTSQHY EKEELIKLMP EIEILVVRSA TKVTADIIEA
     GTKLKIIGRA GTGLDNIDVK VAEAKGIKVI NTPGANSISV AELTIGLMIA CSRHIARGTI
     DLKNGKWTKK ELEGHELYKR TVGIIGFGNI GREVAKRLLA FDMNVLAYDP IVKETDMNVK
     LVDLDTLISN SDYITIHVPL TPETKNLINK DTISKMKDGV IIINAARGGI VDESALYEAL
     LSGKIYAAGL DVFEVEPPTD ELRQKLLSLP NVVATPHVGA STFEAQERVG MLLVERLIKE
     IAG
//
DBGET integrated database retrieval system