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Database: UniProt
Entry: A0A101HYD2_9BACT
LinkDB: A0A101HYD2_9BACT
Original site: A0A101HYD2_9BACT 
ID   A0A101HYD2_9BACT        Unreviewed;       352 AA.
AC   A0A101HYD2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KUK84435.1};
DE   Flags: Fragment;
GN   ORFNames=XE01_1414 {ECO:0000313|EMBL:KUK84435.1};
OS   Synergistales bacterium 58_81.
OC   Bacteria; Synergistota; Synergistia; Synergistales.
OX   NCBI_TaxID=1635274 {ECO:0000313|EMBL:KUK84435.1, ECO:0000313|Proteomes:UP000054873};
RN   [1] {ECO:0000313|Proteomes:UP000054873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+)
CC         + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95;
CC         Evidence={ECO:0000256|ARBA:ARBA00001878};
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}.
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:KUK84435.1}.
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DR   EMBL; LGGV01000140; KUK84435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101HYD2; -.
DR   STRING; 1635274.XE01_1414; -.
DR   PATRIC; fig|1635274.3.peg.303; -.
DR   Proteomes; UP000054873; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   CDD; cd04902; ACT_3PGDH-xct; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR029009; ASB_dom_sf.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR045626; PGDH_ASB_dom.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF19304; PGDH_inter; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          276..352
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KUK84435.1"
SQ   SEQUENCE   352 AA;  37818 MW;  EF9ED2218A0FD3F7 CRC64;
     ADIVTLHVPL TRETHGMIDA KTMKACKRGA FIVNCARGGL VDENACAEAV RSGHLSGAAF
     DVFDGEPVRQ DHPLFAEDIR DRIVLTPHIG ANTEEAQSAV ATIACSNLLA ALKGKPCENA
     VNLPFVEQTL SDGSRAFLSL ARKLGFLAAH LVREPVKNIR IALRGPLFSP GDDPICFEIP
     YHYSPFSVAG LKGFLEYSHG PEVNYMSAPL IAADKGIRVE EARTSGGTWK NQIDLSLSVE
     EQRETVTVSG TVTEEGRQRV VNICGYWIEF IPEGTVLLFS NHDRPGVIGK VGTLLGKAGA
     NIANFALGRK NGSGLAVGAL QIDDDISGAI VETMKEDVDL LWAEKINFAE AL
//
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